| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-2220SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB600-1384SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NBP2-13075SS | |||
| Azide and BSA Free | NBP2-80594 | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NBP2-36440SS | |||
| Azide and BSA Free | NBP2-80679 | |||
| Conjugate | Catalog # | Availability | Size | Price |
|---|---|---|---|---|
| Alexa Fluor 405 | NLS1878AF405 | |||
| Alexa Fluor 488 | NLS1878AF488 | |||
| Alexa Fluor 647 | NLS1878AF647 | |||
| Alexa Fluor 700 | NLS1878AF700 | |||
| Biotin | NLS1878B | |||
| DyLight 405 | NLS1878V | |||
| DyLight 488 | NLS1878G | |||
| DyLight 550 | NLS1878R | |||
| DyLight 650 | NLS1878C | |||
| FITC | NLS1878F | |||
| HRP | NLS1878H | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-662SS | |||
| Azide and BSA Free | NBP2-80932 | |||
![Detection of LC3B in mouse ES cell lysates using Rabbit anti- [Catalog # NB100-2220]. LC3 detected at a molecular weight of approximately 17 kDa. Atg5-/- ES cells from Dr. Noboru Mizushima [Mizushima, N. et al. J. Cell Biol. 152 (2001)] Photo courtesy of Dr. Beth Levine, UT SW Medical Center.](http://images.novusbio.com/fullsize/LC3B-Antibody-Western-Blot-NB100-2220-img0047.jpg)
![<b>Biological Strategies Validation. </b>Detection of LC3I and LC3II in mouse cochlea cell line SV-K1 using Rabbit anti- [Catalog # NB100-2220]. Cells were treated with CQ (1 uM), and As2O3 (1 uM) for 24 hrs. Image from verified customer review.](http://images.novusbio.com/fullsize/LC3B-Antibody-Western-Blot-NB100-2220-img0056.jpg)
![Staining of rat brain tissue section. Analysis using Rabbit anti-LC3B Antibody [Catalog # NB100-2220]. Image from verified customer review.](http://images.novusbio.com/fullsize/LC3B-Antibody-Immunohistochemistry-NB100-2220-img0037.jpg)
![FFPE (Formalin-Fixed Paraffin-Embedded) tissue section of mouse brain using 1:200 dilution of Rabbit anti-LC3B antibody [Catalog # NB100-2220]. The specific signal of LC3 was detected using HRP-conjugated secondary antibody with DAB (3, 3 -diaminobenzidine) reagent, and nuclei of cells were counterstained using hematoxylin. This LC3B antibody generated a low to moderate levels of cytoplasmic staining in the glial cells. The neurons depicted a moderate to strong staining for LC3 in their cytoplasm.](http://images.novusbio.com/fullsize/LC3B-Antibody-Immunohistochemistry-Paraffin-NB100-2220-img0048.jpg)
![Analysis using the Biotin conjugate of Rabbit anti-LC3B Antibody [Catalog # NB100-2220]. Staining of brain, cerebral cortex, neurons with cell processes.](http://images.novusbio.com/fullsize/LC3B-Antibody-Immunohistochemistry-NB100-2220-img0053.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB100-2220] - P53 mediates topotecan-induced autophagy through the activation of sestrin 2 & AMPK in colon cancer cells with wild-type p53.A. HCT116 & LS-174T cells were treated with various concentrations of TPT for 24 h. The levels of P53, sestrin2 & p-AMPK were analysed by immunoblotting. B. HCT116 cells were transfected with p53 or sestrin 2 siRNAs for 24 h, treated with or without 1 µg/mL TPT for an additional 24 h, & the indicated proteins were then analysed by immunoblotting. C. HCT116 cells were transfected with LKB1 or CaMKK beta siRNAs, treated with or without 1 µg/mL TPT for an additional 24 h, & the indicated proteins were detected by immunoblotting. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23024792), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-310202415334948.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB100-2220] - Specific inhibitor SP600125 or siRNA directed JNK blocked ceramide-induced autophagy & up-regulation of LC3 expression. (A) SUNE1 cells were treated with 20 μM ceramide for 24 h in the absence or presence of SP600125 or JNK1/2 siRNA. Lysates were analyzed by immunoblotting. (B) Autophagosome formation was visualized using YFP-LC3 expressing & observed under a confocal microscope. Representative immunofluorescence pictures are shown at the original magnification × 1000. (C) The expression of LC3 mRNA was examined by RT-PCR analysis. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/21943220), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-31020241535643.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB100-2220] - Glutamine deprivation induces IL-8 secretion.(a) RT–PCR analysis of LC3, IL-8, CHOP & GADD34 in U2OS cells subjected to glutamine deprivation (−Q) or exposed to TPG (1 μM). (b) Immunoblot analysis of ER stress- & autophagy-related proteins in U2OS cells subjected to glutamine deprivation or TPG treatment. Samples are run in triplicate. (c) Cytokine array analysis of conditioned media from U2OS & A549 cells grown in the presence (+Q) or absence (−Q) of glutamine. (d) IL-8 enzyme-linked immunosorbent assay of conditioned media from U2OS & A549 cells grown in the presence (+Q) or absence (−Q) of glutamine. Error bars in all figures represent s.d. of three biological replicates. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/ncomms5900), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-310202415395934.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB100-2220] - NDs API improves ATO-based therapy in vivo. HepG2 tumor-bearing nude mice administered intravenously (i.v.) w/ NS (200 μL), NDs (5 mg kg−1), ATO (0.75 mg kg−1), ATO (1.5 mg kg−1), NDs–0.75 mg kg−1 ATO mixture,/NDs–1.5 mg kg−1 ATO mixture daily for 5 consecutive days every week, w/ 13-week cycles c Immunoblots of autophagy-related proteins LC3-II, p62 (left); semi-quantified analysis (n = 3) in tumor tissues from mice after treatment (right). GAPDH used as loading control. Normalized band densities shown below each band. Image collected & cropped by CiteAb from following publication (//pubmed.ncbi.nlm.nih.gov/30341298), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-31020241539454.jpg)
![Immunocytochemistry/ Immunofluorescence: LC3B Antibody - BSA Free [NB100-2220] - NDs API improves the ATO-based therapy in vivo. HepG2 tumor-bearing nude mice administered intravenously (i.v.) w/ NS (200 μL), NDs (5 mg kg−1), ATO (0.75 mg kg−1), ATO (1.5 mg kg−1), NDs–0.75 mg kg−1 ATO mixture,/NDs–1.5 mg kg−1 ATO mixture daily for 5 consecutive days every week, w/ 13-week cycles. g Immunostaining of LC3 & ATG13 in tumor tissues of NDs–1.5 mg kg−1 ATO-treated mice. Schematic showing (left) & imaging (right) indicate that LC3/Atg13 puncta in periphery & around the blood vessels inside the tumors. Scale bars: 20 μm. Error bars s.d. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30341298), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-310202415382444.jpg)
![Immunohistochemistry: LC3B Antibody - BSA Free [NB100-2220] - LC3, CRF, & HIF-1 alpha expression. (a) for each antibody the spatial distribution of immunohistochemical staining was the same in cases with spontaneous & induced labor. (b) The analysis of data from optical density values of Western blotting bands shows no differences of LC3-II & HIF-1 alpha expression between groups. On the contrary CRF is higher in spontaneous labor. LC3-II, HIF-1 alpha , & CRF are normalized onto alpha -tubulin. (c) No correlation between LC3-II & CRF expression was found. SP: spontaneous labor; PG: induction with prostaglandin; PO: induction with prostaglandin & oxytocin; OX: induction with oxytocin. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23956998), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-310202415392554.jpg)
![Immunocytochemistry/ Immunofluorescence: LC3B Antibody - BSA Free [NB100-2220] - The time-dependent effects of melatonin on the LC3-II & Beclin 1 expression in U87MG (a, b) & A172 (c, d) cells. The cells were treated with 1 mM melatonin for 4, 12, 24 or 36 h. PBS was used as a negative control, & rapamycin (Rap 200 nM) served as a positive control. The levels of LC3-II & Beclin-1 expression were determined by a Western blot analysis. The protein bands for each regimen were quantified by densitometry, & their differences are presented in the graph. The values represent the mean ± S.E.M. for three separate determinations. Statistical significance * at P 10 puncta per cell from three independent experiments is depicted. Bars represent mean±s.d. from three independent experiments (>50 cells per experiment). The statistical significance (P value) was determined by a two-tailed, paired Student’s t-test. *P<0.05. (c) Immunoblot analysis of U2OS cells subjected to glutamine deprivation with or without 400 nM BafA1. Cells were pretreated with BafA1 for 1 h before & during exposure to glutamine-deficient medium. Autophagic activity was monitored by detection of p62 & LC3-II proteins. (d) U2OS mCherry-GFP-LC3 cells were cultured in the presence (+Q) or absence (−Q) of glutamine for 18 h. Red vesicles denote autolysosomes, whereas yellow vesicles represent autophagosomes. Bars indicate numbers of yellow vesicles (autophagosomes) or red vesicles (autolysosomes) per cell±s.d. (e) Images of U2OS mCherry-GFP-LC3 cells cultured for 18 h in the presence (+Q) or absence (−Q) of glutamine. Scale bar, 10 μm. (f) Phagophore formation in mCherry-ULK1. Scale bar, 10 μm. (g) mCherry-ATG5-expressing U2OS cells after 24 h in the presence (+Q) or absence (−Q) of glutamine. Scale bar, 10 μm. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/ncomms5900), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-31020241554193.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB100-2220] - Glucocorticoids promote BCG survival in macrophages by inhibiting autophagy. (a) RAW264.7 cells were pretreated with dexamethasone (DEX) (1 μM) or vehicle control ethanol (mock) for 6 hr & then challenged with M. bovis BCG (MOI 5) or treated with the vehicle control DMSO or rapamycin (4 μM). LC3 level was detected with Western blot analysis. & GAPDH was used as the loading control. Full-length blots are presented in Supplementary Fig. 12. Data are representative of three independent experiments with similar results. (b,c) RAW264.7 cells were treated as described in (a), & viable bacilli were determined by CFU assays at 6 hpi (b). Survival rate was calculated compared with that of mock-treated cells (c). Data are shown as the mean ± SEM of three independent experiments. *p < 0.05. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-017-01174-9), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-310202415532059.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB100-2220] - CysC regulates AMPK activity during the induction of autophagy. (a) Immunoblotting analysis of autophagy regulators. N2a cells expressing SOD1 treated with or without CysC (1 μM) for 6 h. The lysates analyzed by immunoblotting using antibodies for phosphorylated AMPK (pAMPK), phosphorylated mTOR (pmTOR), phosphorylated PKCδ (pPKCδ), Myc & beta -actin. (b) Inactivation of AMPK by mutant SOD1 expression. Each relative pAMPK level normalized by beta -actin in (a) is quantified. *P<0.05, **P<0.01 versus mock. (c) Activation of AMPK by CysC treatment. Relative levels of pAMPK for CysC-treated samples normalized by that of PBS-treated control, which is shown as the broken line, in (a) quantified. *P<0.05 versus PBS-treated controls. (d) CysC induced autophagy through the AMPK activation. N2a cells treated with CysC (1 μM), CC (5 μM) or AICA-riboside (AICAR, 5 mM) for 12 h. The lysates analyzed by immunoblotting using antibodies against pAMPK, LC3 & Tubulin (left panel). Quantification of immunoblots was plotted (right panel). (e) The effect of pAMPK activation on neuroprotection by CysC. N2a cells expressing G85R SOD1 mutant treated with CysC (0.2 μM), CC (5 μM) or AICAR (5 mM). Cell viability was measured by the MTS assay. Data expressed as means±S.E.M. from 3 independent experiments. Each experiment was performed in triplicate. *P<0.01 compared to non-treated control, #P<0.01 compared to CysC-treated one. (f) Immunoblotting analysis of pAMPK in SOD1 transgenic mouse spinal cords. The spinal cord lysates from the transgenic mice at indicated ages analyzed for the levels of pAMPK, SOD1 & beta -actin (upper panel). Expression levels of pAMPK normalized by beta -actin (lower panel). All data expressed as means±S.E.M. from 3 independent experiments Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/cddis2014459), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-310202415535189.jpg)
![Immunocytochemistry/ Immunofluorescence: LC3B Antibody - BSA Free [NB100-2220] - Vps34 inhibition blocks autophagy initiation & causes accumulation of ubiquitin-positive & p62-positive structures. a Representative confocal images of cortical neurons treated with vehicle, Bafilomycin A1 (BafA1) at 50 nM, VPS34IN1 at 3 µM or cotreated for 3 h. Arrows highlight LC3 & p62 structures. Right panel, bar graphs denote average object intensity, per cell (mean ± SEM, N = 49-60 cells, from three independent experiments). Scale bar, 10 µm. ***p < 0.001 in one-way ANOVA, Holm–Sidak’s multiple comparisons test. b Representative confocal images of cortical neurons treated as in a & immunostained for LAMP-1, LC3, & p62. Airyscan insets highlight position of LC3 & p62 structures relative to LAMP-1-positive membranes. Scale bar, 10 µm. c Representative confocal images of cultured cortical neurons treated with vehicle or VPS34IN1 at 3 µM for 24 h. Arrows highlight p62 & ubiquitin colocalization. Scale bar, 10 µm Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41467-017-02533-w), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-310202415535128.jpg)
![Immunocytochemistry/ Immunofluorescence: LC3B Antibody - BSA Free [NB100-2220] - ORP1L & VAP-A form cholesterol-dependent ER-AV contact sites(a) MelJuSo cells expressing GFP or GFP-tagged ORP1L mutants were fixed & stained for LC3 & Calnexin. Y477 & D478 in the FFAT motif were mutated to alanines (A) in the ORP1L ydaa mutant. Scale bar, 10 μm. Right: co-immunoprecipitation for ORP1L (mutants) with VAP-A. GFP-ORP1L mutants or GFP were isolated from lysates of HEK293T cells co-overexpressing HA-VAPA using GFP-Trap beads. Western blot filters were probed for isolated GFP-tagged proteins, the associated HA-VAP-A & the input HA-VAP-A, as indicated. (b) Cryo-immuno-EM on HeLa cells expressing HA-LC3 & GFP-ORP1L delta ORD, as detected by HA10 nm & GFP15 nm gold antibodies. Insets show ORP1L labelling in the membrane contact site between ER & autophagosome. The membranes of the ER are depicted in the bottom inset. Scale bar, 50 nm. (c) Three-colour super-resolution image of an autophagosomal vesicle labelled by LC3 (green), ORP1L (blue) & the ER protein VAP-A (red). Scale bar, 500 nm (d) MelJuSo cells cultured either in lipid depleted serum or control medium were fixed & stained for LC3 & ER marker Calnexin. Scale bar, 10 μm. Right panel: Manders coefficient for LC3 localization to the ER was calculated on at least 10 cells over three independent experiments. Bars indicate mean+s.d. Student's t-test statistical analysis (****P<0.0001). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27283760), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-31020241554525.jpg)
![Immunohistochemistry: LC3B Antibody - BSA Free [NB100-2220] - OSI induces autophagy through upregulation of MCT1 in CRC cells.a Immunoblotting analysis of MCT1 expression in CRC cells treated with or without 5 μM OSI for 24 h. b Immunoblotting analysis of MCT1 & phosphorylated AMPK in tumor xenografts obtained from vehicle- or OSI-treated mice. (Each protein of interest from each group was electrophoretically transferred onto a PVDF membrane, incubated with indicated primary & secondary antibodies, & developed as a digital image.) c Immunohistochemical analysis of MCT1 expression in tumor xenografts. Scale bar, 50 μm. d Relative intensity of MCT1 staining in (c). e CRC cells were transfected with siScramble or siMCT1 for 24 h, followed by treatment with or without 5 μM OSI for another 24 h. The protein levels of LC3, phosphorylated AMPK, phosphorylated LKB1 & MCT1 were analyzed by immunoblotting. f CRC cells were treated as in (e), the endogenous LC3 puncta were analyzed by immunofluorescence. Scale bar, 10 μm. g The number of LC3 puncta in (f). h CRC cells were transfected with empty vector or Flag-MCT1 plasmid for 48 h, the protein levels of MCT1 & phosphorylated AMPK were analyzed by immunoblotting. i CRC cells were treated as in (h), the endogenous LC3 puncta were analyzed by immunofluorescence. Scale bar, 10 μm. j The number of LC3 puncta in (i). k Immunoblotting analysis of LC3, MCT1 & phosphorylated AMPK levels in CRC cells co-transfected with Flag-MCT1 & DN-AMPK plasmids for 48 h. l CRC cells were treated as in (k), the endogenous LC3 puncta were analyzed by immunofluorescence. Scale bar, 10 μm. m The number of LC3 puncta per cell in (l). Data are presented as mean SEM, Student’s t-test, & are representative of three independent experiments. *P < 0.05; ***P < 0.001 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31409796), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-310202415532016.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB100-2220] - Abrogation of autophagy by siRNAs targeting autophagy-related genes in gastric cancer cells induced tumor-intrinsic PD-L1 expression. a Inhibition of autophagy by knockdown of ATG5 in AGS & NCI-n87 gastric cancer cells induced the expression of PD-L1 in the presence & absence of INF-gamma (200 U/mL) as shown by flow cytometry analysis at 48 h post-transfection. b The induction of PD-L1 was confirmed by Western blots at 72 h post-transfection. The knockdown efficacies of ATG5 & ATG7 siRNA were verified. The conversion of LC3B-I to LC3B-II was reduced. Results were averaged & blots were representative of 4 independent experiments. The ratio of PD-L1 MFI minus isotype control was shown as mean ± S.D. relative to Ctrl from 4 independent experiments, *p < 0.05 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30925913), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-31020241682127.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB100-2220] - OSI induces autophagy through upregulation of MCT1 in CRC cells.a Immunoblotting analysis of MCT1 expression in CRC cells treated with or without 5 μM OSI for 24 h. b Immunoblotting analysis of MCT1 & phosphorylated AMPK in tumor xenografts obtained from vehicle- or OSI-treated mice. (Each protein of interest from each group was electrophoretically transferred onto a PVDF membrane, incubated with indicated primary & secondary antibodies, & developed as a digital image.) c Immunohistochemical analysis of MCT1 expression in tumor xenografts. Scale bar, 50 μm. d Relative intensity of MCT1 staining in (c). e CRC cells were transfected with siScramble or siMCT1 for 24 h, followed by treatment with or without 5 μM OSI for another 24 h. The protein levels of LC3, phosphorylated AMPK, phosphorylated LKB1 & MCT1 were analyzed by immunoblotting. f CRC cells were treated as in (e), the endogenous LC3 puncta were analyzed by immunofluorescence. Scale bar, 10 μm. g The number of LC3 puncta in (f). h CRC cells were transfected with empty vector or Flag-MCT1 plasmid for 48 h, the protein levels of MCT1 & phosphorylated AMPK were analyzed by immunoblotting. i CRC cells were treated as in (h), the endogenous LC3 puncta were analyzed by immunofluorescence. Scale bar, 10 μm. j The number of LC3 puncta in (i). k Immunoblotting analysis of LC3, MCT1 & phosphorylated AMPK levels in CRC cells co-transfected with Flag-MCT1 & DN-AMPK plasmids for 48 h. l CRC cells were treated as in (k), the endogenous LC3 puncta were analyzed by immunofluorescence. Scale bar, 10 μm. m The number of LC3 puncta per cell in (l). Data are presented as mean SEM, Student’s t-test, & are representative of three independent experiments. *P < 0.05; ***P < 0.001 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31409796), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-310202415541982.jpg)
![Immunocytochemistry/ Immunofluorescence: LC3B Antibody - BSA Free [NB100-2220] - Screening of potent NAPIs in HepG2. a Immunoblots for autophagy-related proteins LC3-II, p62 (left); semi-quantified analysis (n = 3) in various nanoparticles treated cells (right). CQ & Rapamycin (Rapa) were used as positive controls for autophagy inhibition & autophagy activation, respectively. Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) was used as the loading control. Normalized band densities were shown below each band. b Fluorescence images of mCherry-GFP-LC3 cells after incubation with CQ or NDs for 48 h (autophagosomes: mCherry+/GFP+ yellow puncta; autolysosomes: mCherry+/GFP) & quantification of the number of LC3 puncta per cell in cells (10 cells per group). Scale bar: 10 μm. c Immunoblots for autophagy-related proteins LC3-II, p62 (left); semi-quantified analysis (n = 3) in CQ, NDs, or CQ–NDs-treated cells (right). &P < 0.05, significantly different from NDs. GAPDH was used as the loading control. Normalized band densities were shown below each band. d Left: Cell viability after incubation with ATO or various NAPIs–ATO mixture for 48 h (n = 3). ##P < 0.01 by t-test, significantly different from ATO. Right: Cell viability after 48 h NDs–ATO treatment with RNAi of autophagy proteins ATG5 & ATG7 (n = 3). e, f Immunoblots for autophagy-related protein LC3-II & autolysosomal process-related protein NUPR1, SNAP25, VAMP8 in NDs-treated cells. g Immunoblots for autolysosomal process-related protein NUPR1 after NDs treatment with RNAi of autophagy proteins ATG5 & ATG7. GAPDH was used as the loading control. Error bars are s.d. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30341298), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-310202415532088.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB100-2220] - Screening of potent NAPIs in HepG2. a Immunoblots for autophagy-related proteins LC3-II, p62 (left); semi-quantified analysis (n = 3) in various nanoparticles treated cells (right). CQ & Rapamycin (Rapa) were used as positive controls for autophagy inhibition & autophagy activation, respectively. Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) was used as the loading control. Normalized band densities were shown below each band. b Fluorescence images of mCherry-GFP-LC3 cells after incubation with CQ or NDs for 48 h (autophagosomes: mCherry+/GFP+ yellow puncta; autolysosomes: mCherry+/GFP) & quantification of the number of LC3 puncta per cell in cells (10 cells per group). Scale bar: 10 μm. c Immunoblots for autophagy-related proteins LC3-II, p62 (left); semi-quantified analysis (n = 3) in CQ, NDs, or CQ–NDs-treated cells (right). &P < 0.05, significantly different from NDs. GAPDH was used as the loading control. Normalized band densities were shown below each band. d Left: Cell viability after incubation with ATO or various NAPIs–ATO mixture for 48 h (n = 3). ##P < 0.01 by t-test, significantly different from ATO. Right: Cell viability after 48 h NDs–ATO treatment with RNAi of autophagy proteins ATG5 & ATG7 (n = 3). e, f Immunoblots for autophagy-related protein LC3-II & autolysosomal process-related protein NUPR1, SNAP25, VAMP8 in NDs-treated cells. g Immunoblots for autolysosomal process-related protein NUPR1 after NDs treatment with RNAi of autophagy proteins ATG5 & ATG7. GAPDH was used as the loading control. Error bars are s.d. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30341298), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-310202415523913.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB100-2220] - OSI induces autophagy in CRC cells in vitro & in vivo.a Immunoblotting analysis of LC3, Atg5, & p62/SQSTM1 expression in CRC cells treated with indicated concentrations of OSI for 24 h. b The formation of endogenous LC3 puncta in cells treated with DMSO or 5 μM OSI for 24 h. c Total number of endogenous LC3 puncta per cell in (b). d, e LC3 expression in xenograft tissues was examined by IHC. Representative images were provided as indicated in (d) & relative intensity of LC3 staining was quantified in (e). f Immunoblotting analysis of LC3 & p62/SQSTM1 expression in tumor xenografts (Each protein of interest from each group was electrophoretically transferred onto a PVDF membrane, incubated with indicated primary & secondary antibodies, & developed as a digital image.) g Relative intensity of LC3 in (f). h Co-immunoprecipitation analysis of the interaction between Beclin 1 & Bcl-2 in CRC cells treated with or without 5 μM OSI for 24 h. i Immunoblotting analysis of LC3 expression in CRC cells treated with or without 5 μM OSI in the presence or absence of 5 mM 3-MA for 24 h. j CRC cells were treated as in (i), the LC3 puncta were analyzed by immunofluorescence. Scale bar, 10 μm. k, l Immunoblotting analysis of LC3 expression in CRC cells transfected with siScramble, siATG5 (k), or siBECN1 (l) for 24 h, followed by treatment with or without 5 μM OSI for another 24 h. m CRC cells were treated as in (k, l). The LC3 puncta were analyzed by immunofluorescence. Scale bar, 10 μm. Data are presented as mean SEM, Student’s t-test, & are representative of 3 independent experiments. **P < 0.01; ***P < 0.001 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31409796), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-310202415523911.jpg)
![Immunohistochemistry: LC3B Antibody - BSA Free [NB100-2220] - OSI induces autophagy in CRC cells in vitro & in vivo.a Immunoblotting analysis of LC3, Atg5, & p62/SQSTM1 expression in CRC cells treated with indicated concentrations of OSI for 24 h. b The formation of endogenous LC3 puncta in cells treated with DMSO or 5 μM OSI for 24 h. c Total number of endogenous LC3 puncta per cell in (b). d, e LC3 expression in xenograft tissues was examined by IHC. Representative images were provided as indicated in (d) & relative intensity of LC3 staining was quantified in (e). f Immunoblotting analysis of LC3 & p62/SQSTM1 expression in tumor xenografts (Each protein of interest from each group was electrophoretically transferred onto a PVDF membrane, incubated with indicated primary & secondary antibodies, & developed as a digital image.) g Relative intensity of LC3 in (f). h Co-immunoprecipitation analysis of the interaction between Beclin 1 & Bcl-2 in CRC cells treated with or without 5 μM OSI for 24 h. i Immunoblotting analysis of LC3 expression in CRC cells treated with or without 5 μM OSI in the presence or absence of 5 mM 3-MA for 24 h. j CRC cells were treated as in (i), the LC3 puncta were analyzed by immunofluorescence. Scale bar, 10 μm. k, l Immunoblotting analysis of LC3 expression in CRC cells transfected with siScramble, siATG5 (k), or siBECN1 (l) for 24 h, followed by treatment with or without 5 μM OSI for another 24 h. m CRC cells were treated as in (k, l). The LC3 puncta were analyzed by immunofluorescence. Scale bar, 10 μm. Data are presented as mean SEM, Student’s t-test, & are representative of 3 independent experiments. **P < 0.01; ***P < 0.001 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31409796), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-31020241553713.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB100-2220] - Growth retardation & shortened lifespan of the mice with deletion of an autophagy-essential gene Atg7 in hematopoietic system. (A) Three genotypes for wild-type, heterozygote, & homozygote for Atg 7 deletion in hematopoietic system with representative images of the mice. The images were taken at age of 10 weeks. (B) PCR Genotyping analysis of the offsprings from Atg7f/f mice crossing Vav-iCre mice to screen Atg7f/f;Vav-iCre mice. The sequences for the primers used in PCR are given in the method section, & their PCR amplified bands representing specific genotypes were indicated in the agarose gel electrophoresis films. (C) Examination of Atg7 expression in wild-type & the Atg7-deleted mice. Upper panel, quantitative PCR analysis of Atg7 transcription normalized to Gapdh transcript in different organs; lower panel, western blotting analysis of autophagy-essential protein ATG7 & lipidation of LC3 in different organs. GAPDH used as a loading control. (D) Growth comparison between wild-type & Atg7-deleted mice. Wild-type mice progressively gain weight before age of 60 weeks (left panel), but Atg7-deleted mice cease weight gain at about age of 6 weeks (right panel). (E) Measurement of lifespan of wild-type & Atg7-deleted mice. (F) Immunohistological examination of heart, liver, lung & thymus from 10 weeks old wild-type & Atg7-deleted mice by HE staining. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31327762), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-310202415535185.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB100-2220] - Overexpression of wild-type MAGEA6, but not mutant MAGEA6, suppresses autophagy in PDAC cell lines.(A) Immunoblot analysis of autophagy signaling in HPDE-iKRAS cells expressing GFP (Vec) & MAGEA6 variants. (B) Immunofluorescence staining of LC3B puncta in the transduced HPDE-iKRAS cells. Representative photos (left) & statistical analysis (mean ± standard deviation of counted cells, N=~100 per cohort) are shown. *p=0.002; two-tailed unpaired t-test. (C) Immunoblot analysis of autophagy substrate SQSTM1/p62 in the transduced HPDE-iKRAS cells treated with BafA1 for the indicated time points., Immunoblot analysis of (D) autophagy signaling & (E) SQSTM1/p62 accumulation in wild-type MAGEA6 expressing & (F) autophagy signaling in MAGEA6H305fs* expressing HPDE-iKRAS cells under nutrient-deficient conditions. (G) Immunoblot analysis of autophagy signaling in wild-type MAGEA6 expressing cells under prolonged nutrient-deficient conditions.Immunoblot analysis of autophagy signaling of transduced AsPC-1 & MIA PaCa-2.Immunoblot analysis of the accumulation of autophagy substrate SQSTM/p62 in the transduced HPDE-iKRAS cells under BafA1 for the indicated time points.Immunoblot analysis of autophagy activity in transduced HPDE-iKRAS cells under nutrient-depleted conditions as indicated. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32270762), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-310202415535165.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB100-2220] - Inhibition of LRRK2 alters the autophagy/lysosomal pathway in H4 neuroglioma cells. A) LC3-II levels increase upon LRRK2-in1 inhibitor treatment (1 μM, overnight treatment; quantification from 3 independent replicates, the plot shows mean & SD, * indicates significance (p < 0.05)). B) Dose dependent increase in LC3-II upon overnight treatment with LRRK2-in1. C) MTT assay showing no alteration of cell viability upon over night treatment with LRRK2-in1 from 1 to 5 μM. A small toxic effect appeared with the higher dose (10 μM). The plot shows mean & SD, * indicates significance (p < 0.05). D) LRRK2 knockdown cells display reduced response to LRRK2-in1. LRRK2 protein levels are decreased in shRNA stable line compared to wild type cells (right panel), & knockdown of LRRK2 reduces response to 1 μM LRRK2-in1 treatment compared to wild type or scrambled shRNA cells (left panel). E) Western blot analysis of H4 cells treated with DMSO & LRRK2-in1 (5 μM, 2.5 hours treatment) in the presence & absence of 40 nM bafilomycin added at the same time as the inhibitor. Quantification of three replicates is shown in the right hand panel, the plot shows mean & SD, * indicates significance (p < 0.05). F) LRRK2-in1 increases LC3-II levels independent of mTORC1 activity. P70S6K & phoshoThr389-P70S6K; S6 & phosphoSer235/236-S6 levels are shown in control, starvation & amino-acid stimulated conditions. LRRK2-in1 (1 μM over night) treatment does not alter phosphorylation of P70S6K & S6 in conditions that show increased levels of LC3-II. G) Neutral red staining. The plot shows mean & SEM. * indicates significance (p < 0.05). Image collected & cropped by CiteAb from the following publication (//linkinghub.elsevier.com/retrieve/pii/S0167488913002954), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-31020241553728.jpg)
![Immunocytochemistry/ Immunofluorescence: LC3B Antibody - BSA Free [NB100-2220] - SQSTM1 recruited ARHGAP5-AS1 for autophagic degradation.a ARHGAP5-AS1 expression in resistant cells after transfecting siNC or SQSTM1 siRNAs was assessed using qRT-PCR. **p < 0.01. b ARHGAP5-AS1 expression in sensitive cells after SQSTM1 overexpression was detected by qRT-PCR. c The interaction of ARHGAP5-AS1 with SQSTM1 in SGC-R cells was analyzed by RIP assay followed with qRT-PCR. IgG was served as the negative control. d RNA pull down assay was performed to verify the binding of SQSTM1 to ARHGAP5-AS1 in SGC7901 or SGC-R cells. beta -actin was served as negative control. NC: no probe. The interaction of ARHGAP5-AS1 with SQSTM1 in SGC-R cells before & after EBSS treatment (4 h) were analyzed using RIP assay (e) & RNA pull down assay (f). g The interaction of various SQSTM1 constructs with ARHGAP5-AS1 were analyzed using RIP assay. h The interaction of various ARHGAP5-AS1 fragments with SQSTM1 was analyzed by RNA pull down assay. i Half-life of ARHGAP5-AS1 in SGC7901 & SGC-R cells with different SQSTM1 expression status were determined by qRT-PCR. The colocalization of ARHGAP5-AS with SQSTM1 (j) & LC3B (k) in SGC-R cells treated as indicated were analyzed by combined FISH & IFC assay (original magnification, ×100). Scale bar: 100 μm (j) & 10 μm (k) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31097692), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-31020241553716.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB100-2220] - Effects of autophagy & caspase inhibitors on survival of neurons after glucose reperfusion (GR).After 3 h GD, neuro2a cells were replaced by 20-Methyladenine (3MA); Bafilomycin A1 (BA1) & z-VAD-FMK (z-VAD) were added at final concentrations of 5 mM, 5 nM & 20 uM, respectively. (A) Cell viability was assessed using the MTT assay after treatment of autophagy & pan-caspase inhibitors. MTT mitochondrial reduction was shown as a relative percentage of the MTT values at the indicated time point (3 h GD/48 h GR) from three independent experiments ± SD (*p<0.05, **p<0.001). (B) Changes in protein levels by inhibitors of autophagy or caspase activation were analyzed by immunoblot. Proteins were blotted with anti-LC3, p62, cleaved-caspase 3 & PARP antibodies. Tubulin was used as loading control. (C) Quantification of immunoblot data in (B). The amount of each protein was normalized against the amount of tubulin. Data represent the mean ± SD (*p<0.05, n = 3). (D) Cells transiently expressing GFP-LC3 (green) were treated with 3MA, BA1 or z-VAD for 48 h of GR after 3h GD. Nuclei were stained with DAPI (blue). Scale bar represents 5 µm. Quantification shown on the right graph represents mean GFP-LC3 puncta per cell (n = 10 cells per condition) from three independent experiments ± SD. The asterisks (*) indicate significant differences in the values.*p<0.05, **p<0.001. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0076466), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-31020241553717.jpg)
![Immunocytochemistry/ Immunofluorescence: LC3B Antibody - BSA Free [NB100-2220] - Exposure of microglia to cART resulted in blockade of autophagosome–lysosome fusion. (A) rPMs were seeded into a 12-well plate followed by tandem fluorescent-tagged MAP1LC3B plasmid. Next, cells were exposed to cART (5 µM each of TDF, FTC, & DTG) for an additional 24 h & observed by confocal imaging. The results showed that cART exposure significantly increased the formation of autophagosomes (yellow puncta). (B) Representative bar graph showing the number of autophagosome (yellow puncta) per cell. (C) Representative bar graph showing the number of autolysosome (red puncta) per cell. (D) rPMs were seeded into 12-well plates followed with cART exposure for 24 h. Cells were then double immunostained with MAP1LC3B & LAMP2 antibody & observed by immunofluorescent microscopy. (E,F) Representative bar graphs showing cART-mediated decreased LAMP2 puncta & decreased colocalization of MAP1LC3B & LAMP2. BAF—autophagosome fusion inhibitor, & rapamycin (RAP—autophagy inducer) were used as controls for autophagy flux. Data is from three independent experiments & is expressed as means ± SEM & were analyzed using one-way ANOVA. *, p < 0.05 vs. control. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31569373), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-31020241683936.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB100-2220] - The cytoprotection of in vitro sIPC is diminished by autophagy inhibitors in RPTC cells. RPTC cells were subjected to: (1) control; (2) CCCP-R; (3) sIPC + CCCP-R in the absence or presence of chloroquine (20 μM) & 3-methyladenine (10 mM). Both inhibitors were used for 1-h pretreatment & during 2-h recovery from prolonged CCCP treatment. Cells were collected for morphological & immunoblot analyses. (a) Representative images of phase contrast & fluorescence microscopy showing cellular & nuclear morphology of apoptosis. Scale bar: 200 μm. (b) Quantification of cell apoptosis. Data are expressed as mean ± SD. *, P < 0.05, significantly different from the control group; #, P < 0.05, significantly different from CCCP-R group. (c) Analysis of apoptosis inhibitory efficiency by sIPC. Data are expressed as mean ± SD. *, P < 0.05, significantly different from the group without inhibitors. (d & e) Immunoblots of LC3B & cleaved CASP3. ACTB was used as a loading control. The molecular mass marker lanes were labelled as kDa. For densitometric analysis of cleaved CASP3, after normalization with ACTB, the protein signals of the control were arbitrarily set as 1, & the signals of other conditions were normalized to the control to calculate fold changes. Data are expressed as mean ± SD. *, P < 0.05, significantly different from the control group; #, P < 0.05, significantly different from CCCP-R group. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31066324), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-310202415541971.jpg)
![Immunocytochemistry/ Immunofluorescence: LC3B Antibody - BSA Free [NB100-2220] - ORP1L & VAP-A form cholesterol-dependent ER-AV contact sites(a) MelJuSo cells expressing GFP or GFP-tagged ORP1L mutants were fixed & stained for LC3 & Calnexin. Y477 & D478 in the FFAT motif were mutated to alanines (A) in the ORP1L ydaa mutant. Scale bar, 10 μm. Right: co-immunoprecipitation for ORP1L (mutants) with VAP-A. GFP-ORP1L mutants or GFP were isolated from lysates of HEK293T cells co-overexpressing HA-VAPA using GFP-Trap beads. Western blot filters were probed for isolated GFP-tagged proteins, the associated HA-VAP-A & the input HA-VAP-A, as indicated. (b) Cryo-immuno-EM on HeLa cells expressing HA-LC3 & GFP-ORP1L delta ORD, as detected by HA10 nm & GFP15 nm gold antibodies. Insets show ORP1L labelling in the membrane contact site between ER & autophagosome. The membranes of the ER are depicted in the bottom inset. Scale bar, 50 nm. (c) Three-colour super-resolution image of an autophagosomal vesicle labelled by LC3 (green), ORP1L (blue) & the ER protein VAP-A (red). Scale bar, 500 nm (d) MelJuSo cells cultured either in lipid depleted serum or control medium were fixed & stained for LC3 & ER marker Calnexin. Scale bar, 10 μm. Right panel: Manders coefficient for LC3 localization to the ER was calculated on at least 10 cells over three independent experiments. Bars indicate mean+s.d. Student's t-test statistical analysis (****P<0.0001). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27283760), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-310202415541949.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB100-2220] - Inhibition of LRRK2 alters the autophagy/lysosomal pathway in H4 neuroglioma cells. A) LC3-II levels increase upon LRRK2-in1 inhibitor treatment (1 μM, overnight treatment; quantification from 3 independent replicates, the plot shows mean & SD, * indicates significance (p < 0.05)). B) Dose dependent increase in LC3-II upon overnight treatment with LRRK2-in1. C) MTT assay showing no alteration of cell viability upon over night treatment with LRRK2-in1 from 1 to 5 μM. A small toxic effect appeared with the higher dose (10 μM). The plot shows mean & SD, * indicates significance (p < 0.05). D) LRRK2 knockdown cells display reduced response to LRRK2-in1. LRRK2 protein levels are decreased in shRNA stable line compared to wild type cells (right panel), & knockdown of LRRK2 reduces response to 1 μM LRRK2-in1 treatment compared to wild type or scrambled shRNA cells (left panel). E) Western blot analysis of H4 cells treated with DMSO & LRRK2-in1 (5 μM, 2.5 hours treatment) in the presence & absence of 40 nM bafilomycin added at the same time as the inhibitor. Quantification of three replicates is shown in the right hand panel, the plot shows mean & SD, * indicates significance (p < 0.05). F) LRRK2-in1 increases LC3-II levels independent of mTORC1 activity. P70S6K & phoshoThr389-P70S6K; S6 & phosphoSer235/236-S6 levels are shown in control, starvation & amino-acid stimulated conditions. LRRK2-in1 (1 μM over night) treatment does not alter phosphorylation of P70S6K & S6 in conditions that show increased levels of LC3-II. G) Neutral red staining. The plot shows mean & SEM. * indicates significance (p < 0.05). Image collected & cropped by CiteAb from the following publication (//linkinghub.elsevier.com/retrieve/pii/S0167488913002954), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-3102024165723.jpg)
![Immunocytochemistry/ Immunofluorescence: LC3B Antibody - BSA Free [NB100-2220] - TFEB overexpression in macrophages induces the autophagy markers LC3 & p62 & restores their co-localization in atherosclerotic aortic roots.(a,b) Representative immunofluorescence images of atherosclerotic aortic roots (2 months' western diet) from control & mφTFEB-TG mice (ApoE-null background) stained with antibodies against TFEB (a), TFEB & MOMA-2 (b; scale bar, 50 μm). (c) Quantification of the average TFEB intensity & co-localization with nuclear marker DAPI (n=4-5 mice per group). (d) Representative immunofluorescence images of atherosclerotic aortic roots from control & mφTFEB-TG mice stained with p62 & LC3 (scale bar, 50 μm). (e) Quantification of the p62 & LC3 average intensity from control & mφTFEB-TG-stained roots (n=13–14 mice per group). (f) Representative pseudocolour image of these p62/LC3 images (green represents co-localization) & graph depicting the increased p62/LC3 correlation seen in a representative mφTFEB-TG as compared to a control lesion (scale bar, 50 μm). (g) Quantification of the p62/LC3 co-localization from control & mφTFEB-TG-stained roots shown (n=13–14 mice per group). (h,i) FACS analysis of aortic macrophages isolated from atherosclerotic aortas of Control or mφTFEB-TG mice (western diet-fed ApoE-KO background, n=3–4 pooled aortas) & stained for either (h) p62 & LC3, or (i) Lamp2 & LC3 antibodies (per cent of macrophages expressing each marker is shown below plots). For all graphs, data are presented as mean±s.e.m. *P<0.05, ***P<0.001, two-tailed unpaired t-test. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/ncomms15750), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-31020241553207.jpg)
![Immunohistochemistry: LC3B Antibody - BSA Free [NB100-2220] - Keap1 co-localizes with SQSTM1-immunopositive sarcoplasmic aggregates in AVM muscle. a-c. Only focal & minimal co-localization of LC3 (a) & Keap1 immunofluorescence (b) is seen in a representative toxic AVM sample (colchicine-treated subject #31); merged panel is shown in (c) (LC3, red; Keap1, green). d-f. In the same specimen, there is extensive co-localization of SQSTM1 (d) & Keap1 immunofluorescence (e); merged panel is shown in (f) (SQSTM1, red; Keap1, green). g-i. Similar to toxic AVM specimens, essentially no co-localization of LC3 (g) & Keap1 immunofluorescence (h) is seen in a representative IBM muscle biopsy (subject #46); merged panel is shown in (i) (LC3, red; Keap1, green). j-l. In the same specimen, there is extensive co-localization of SQSTM1 (j) & Keap1 immunofluorescence (k); merged panel is shown in (l) (SQSTM1, red; Keap1, green). Scale bar, 25 μm Image collected & cropped by CiteAb from the following publication (//actaneurocomms.biomedcentral.com/articles/10.1186/s40478-016-0384-6), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-310202415535125.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB100-2220] - Glucose deprivation (GD) induces neuronal cell death.Time course of cell viability & cell death after GD was estimated by MTT & LDH assays, respectively. Bars depict rates of MTT reduction (A) & LDH release (B) time dependent manner after GD. MTT data represent relative percentages compared with controls (*p<0.05, **p<0.001, n = 3). LDH release from neuro2a cells was calculated as fold increase from the LDH release in controls (*p<0.01, **p<0.001, n = 3). (C) Levels of LC3 & p62 expression, cleaved-caspase 3 & PARP cleavage were determined at indicated times after GD by immunoblot analysis. Tubulin was used as loading control. (D) Quantitative analyses of the immunoblots are shown in (C). The amount of each protein was normalized against the amount of tubulin. Data represent the mean ± SD for each condition (*p<0.05, **p<0.001, n = 3). Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0076466), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-31020241552390.jpg)
![Immunohistochemistry: LC3B Antibody - BSA Free [NB100-2220] - OSI induces autophagy through upregulation of MCT1 in CRC cells.a Immunoblotting analysis of MCT1 expression in CRC cells treated with or without 5 μM OSI for 24 h. b Immunoblotting analysis of MCT1 & phosphorylated AMPK in tumor xenografts obtained from vehicle- or OSI-treated mice. (Each protein of interest from each group was electrophoretically transferred onto a PVDF membrane, incubated with indicated primary & secondary antibodies, & developed as a digital image.) c Immunohistochemical analysis of MCT1 expression in tumor xenografts. Scale bar, 50 μm. d Relative intensity of MCT1 staining in (c). e CRC cells were transfected with siScramble or siMCT1 for 24 h, followed by treatment with or without 5 μM OSI for another 24 h. The protein levels of LC3, phosphorylated AMPK, phosphorylated LKB1 & MCT1 were analyzed by immunoblotting. f CRC cells were treated as in (e), the endogenous LC3 puncta were analyzed by immunofluorescence. Scale bar, 10 μm. g The number of LC3 puncta in (f). h CRC cells were transfected with empty vector or Flag-MCT1 plasmid for 48 h, the protein levels of MCT1 & phosphorylated AMPK were analyzed by immunoblotting. i CRC cells were treated as in (h), the endogenous LC3 puncta were analyzed by immunofluorescence. Scale bar, 10 μm. j The number of LC3 puncta in (i). k Immunoblotting analysis of LC3, MCT1 & phosphorylated AMPK levels in CRC cells co-transfected with Flag-MCT1 & DN-AMPK plasmids for 48 h. l CRC cells were treated as in (k), the endogenous LC3 puncta were analyzed by immunofluorescence. Scale bar, 10 μm. m The number of LC3 puncta per cell in (l). Data are presented as mean SEM, Student’s t-test, & are representative of three independent experiments. *P < 0.05; ***P < 0.001 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31409796), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-310202415525226.jpg)
![Immunohistochemistry: LC3B Antibody - BSA Free [NB100-2220] - OSI induces autophagy in CRC cells in vitro & in vivo.a Immunoblotting analysis of LC3, Atg5, & p62/SQSTM1 expression in CRC cells treated with indicated concentrations of OSI for 24 h. b The formation of endogenous LC3 puncta in cells treated with DMSO or 5 μM OSI for 24 h. c Total number of endogenous LC3 puncta per cell in (b). d, e LC3 expression in xenograft tissues was examined by IHC. Representative images were provided as indicated in (d) & relative intensity of LC3 staining was quantified in (e). f Immunoblotting analysis of LC3 & p62/SQSTM1 expression in tumor xenografts (Each protein of interest from each group was electrophoretically transferred onto a PVDF membrane, incubated with indicated primary & secondary antibodies, & developed as a digital image.) g Relative intensity of LC3 in (f). h Co-immunoprecipitation analysis of the interaction between Beclin 1 & Bcl-2 in CRC cells treated with or without 5 μM OSI for 24 h. i Immunoblotting analysis of LC3 expression in CRC cells treated with or without 5 μM OSI in the presence or absence of 5 mM 3-MA for 24 h. j CRC cells were treated as in (i), the LC3 puncta were analyzed by immunofluorescence. Scale bar, 10 μm. k, l Immunoblotting analysis of LC3 expression in CRC cells transfected with siScramble, siATG5 (k), or siBECN1 (l) for 24 h, followed by treatment with or without 5 μM OSI for another 24 h. m CRC cells were treated as in (k, l). The LC3 puncta were analyzed by immunofluorescence. Scale bar, 10 μm. Data are presented as mean SEM, Student’s t-test, & are representative of 3 independent experiments. **P < 0.01; ***P < 0.001 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31409796), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-310202415535133.jpg)
![Immunocytochemistry/ Immunofluorescence: LC3B Antibody - BSA Free [NB100-2220] - Measurement of dysregulated autophagy by fluorescent microscopyOVCAR3 cells were treated with the indicated drugs for 24 hours & then fixed & immunostained for p62 (red) & LC3 (green), with a DAPI costain (blue). Confocal z-stacks were flattened for image analysis to capture all punctate area. A. Doses were: chloroquine (10 μM), nelfinavir (10 μM), rapamycin (10 nM), dasatinib (50 nM), & all were combined for Necramed. B. Similar immunostaining as in (A) Punctae were quantified for size & number per cell by ImageJ with at least 40 cells per condition. LC3 channel was analyzed for autophagosomes, & the p62 channel for sequestosomes. Doses were same as in (A), but with chloroquine & nelfinavir reduced to 5 μM. *p < 0.05, ***p < 0.001 by t-test. All error bars are s.e.m. C. OVCAR3 cells with a virally integrated mCherry-GFP-LC3 construct were studied by live microscopy, for the number of hours indicated following Necramed (doses as in (A)) or control treatment. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26418751), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-3102024165734.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB100-2220] - Rop-DPRL combined with CR inhibits tumor growth. (A) Fluorescent imaging of major organs & tumor. Tumor-bearing mice were injected with cy5-labeled liposome or unlabelled liposome. The tumor & major organs from control or drug-treated mice were excised at 12 h or 24 h. (B) Fluorescent image of tumor sections. Tumor from control or Rop-DPRL treated mice were excised at 12 h. Tumor frozen sections were observed under confocal microscope. Scale bar = 20 µm. (C) Immunofluorescence staining of tumor sections for the autophagosome marker LC3, P62 & LAMP1. (D) Image of representative tumors. (E) Change in tumor volume. (F) Tumor weight. (G) TUNEL staining of tumor sections. Nuclei were stained with Hoechst. Scale bar = 20µm. (H) Body weight changes of mice under different treatments. CR: Calorie restriction. Arrows: Enlarged lysosomes. Data are presented as the mean ± SEM, ** p < 0.01. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32308756), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-31020241555242.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB100-2220] - SsD & SsA inhibit autophagy in HeLa cells. a Structures of SsA, SsC, & SsD. b SsD (15 μM) & SsA (30 μM), but not SsC, significantly increased LC3-II yellow puncta formation but did not significantly affect LC3-II red-only puncta in RFP-GFP-LC3-expressing HeLa cells. Scale bar = 10 μm. Quantification of LC3 yellow puncta/red puncta (%) is presented as the mean ± S.E., n = ~80 cells from 3 independent experiments. c Treatment of HeLa cells with SsD for 6 h induced the accumulation of both LC3-II & SQSTM1 in a dose-dependent manner. d SsD (15 μM) induced the accumulation of both LC3-II & SQSTM1 in HeLa cells in a time-dependent manner. e SsA (30 μM) induced the accumulation of both LC3-II & SQSTM1 in HeLa cells in a time-dependent manner. f Treatment with different concentrations of SsC for 6 h failed to induce the accumulation of either LC3-II or SQSTM1 in HeLa cells. g SsD (15 μM) reversibly inhibited autophagy Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30820356), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-31020241553736.jpg)
![Immunocytochemistry/ Immunofluorescence: LC3B Antibody - BSA Free [NB100-2220] - PERK pathway-independent induction of prosurvival autophagy in KG1 LSC-like cells upon G9a inhibition. a, LC3-I/II & p62 expression, analyzed by western blotting, after cell treatment with BIX-01294 (15 μmol/L) in the absence or presence of bafilomycin A1 (BafA1) for 24 h. b, Confocal microscopy images of GFP-LC3-transfected cells after treatment with BIX-01294 (5 μmol/L). c, Apoptotic fractions, measured using flow cytometry, after cell treatment with BIX-01294 (15 μmol/L) in the absence or presence of the autophagy inhibitor 3-MA (5 mmol/L) or BafA1 (2 nmol/L) for 48 h. d, Protein expression, analyzed by western blotting with the indicated antibodies, after treatment of PERK siRNA-transfected & non-transfected cells with BIX-01294 (15 μmol/L) for 48 h. e, Protein expression, analyzed by western blotting with the indicated antibodies, after cell treatment with BIX-01294 (10 μmol/L) in the absence or presence of GSK2606414 (20 μmol/L) for 48 h. f, Protein expression, analyzed by western blotting with the indicated antibodies, after treatment of NRF2 siRNA-transfected & non-transfected cells with BIX-01294 (10 μmol/L) for 48 h. g, Levels of apoptosis, evaluated by flow cytometry, after cell treatment for 48 h with BIX-01294 (10 μmol/L) in the absence or presence of the PERK inhibitor GSK2606414 (10 μmol/L) or the autophagy inhibitor 3-MA (5 mmol/L), or BafA1 (2 nmol/L). h, Levels of apoptosis, evaluated by flow cytometry, after treatment of PERK siRNA- or control siRNA-transfected cells with BIX-01294 (10 μmol/L) in the absence or presence of 3-MA (5 mmol/L) or BafA1 (2 nmol/L) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32293500), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-31020241682153.jpg)
![Immunohistochemistry: LC3B Antibody - BSA Free [NB100-2220] - OSI induces autophagy in CRC cells in vitro & in vivo.a Immunoblotting analysis of LC3, Atg5, & p62/SQSTM1 expression in CRC cells treated with indicated concentrations of OSI for 24 h. b The formation of endogenous LC3 puncta in cells treated with DMSO or 5 μM OSI for 24 h. c Total number of endogenous LC3 puncta per cell in (b). d, e LC3 expression in xenograft tissues was examined by IHC. Representative images were provided as indicated in (d) & relative intensity of LC3 staining was quantified in (e). f Immunoblotting analysis of LC3 & p62/SQSTM1 expression in tumor xenografts (Each protein of interest from each group was electrophoretically transferred onto a PVDF membrane, incubated with indicated primary & secondary antibodies, & developed as a digital image.) g Relative intensity of LC3 in (f). h Co-immunoprecipitation analysis of the interaction between Beclin 1 & Bcl-2 in CRC cells treated with or without 5 μM OSI for 24 h. i Immunoblotting analysis of LC3 expression in CRC cells treated with or without 5 μM OSI in the presence or absence of 5 mM 3-MA for 24 h. j CRC cells were treated as in (i), the LC3 puncta were analyzed by immunofluorescence. Scale bar, 10 μm. k, l Immunoblotting analysis of LC3 expression in CRC cells transfected with siScramble, siATG5 (k), or siBECN1 (l) for 24 h, followed by treatment with or without 5 μM OSI for another 24 h. m CRC cells were treated as in (k, l). The LC3 puncta were analyzed by immunofluorescence. Scale bar, 10 μm. Data are presented as mean SEM, Student’s t-test, & are representative of 3 independent experiments. **P < 0.01; ***P < 0.001 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31409796), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-31020241555224.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB100-2220] - Metabolic profiling & biochemical assay. (A) Relative abundance of the substrates in the glycolytic pathway & TCA cycle in ORP compared to OCL by targeted metabolic profiling. When compared with OCL heart, ORP hearts have significantly lower glucose-6-phosphate & fructose-6-phosphate (both are glycolytic metabolites), & significantly higher a-ketoglutarate, fumarate, malate, & citrate (all are TCA cycle metabolites). *P < 0.05 compared with OCL. See Table S6 for numerical data. (B) A schematic diagram summarizing the changes in metabolism by rapamycin in old heart. (C) Western blots of autophagic markers show no significant change of LC3 II/I, p62, or beclin-1 in cardiac aging. However, OCR has significantly lower p62 than that in OCL. #P < 0.05 compared with OCL. (D) Both CR & RP significantly reduce the age-dependent increase in protein carbonyls (nmol mL−1). #P < 0.05 compared with OCL. (E). Both CR & RP significantly reduce the age-dependent increase in protein ubiquitination.*P < 0.05 compared with YCL & #P < 0.05 compared with OCL. n = 3–8. G6P: glucose 6-phosphate; G1P: glucose 1-phosphate; F6P: fructose 6-phosphate; F1P: fructose 1-phosphate; F16BP: fructose 1,6-bisphosphate; F26BP: fructose 2,6-biphosphate; G3P: glyceraldehyde 3-phosphate; DHAP:dihydroxyacetone phosphate; 2(3)-PGA: 2- or 3-phosphoglycerate; & PEP: phosphoenolpyruvate. Isomers of same molecular weight, that is, G6P versus G1P, F6P versus F1P, & F16BP versus F26BP, were not distinguishable by the LC-MS/MS-based metabolic profiling method. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/24612461), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-310202415535191.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB100-2220] - iNOS level is regulated by autophagy during LPS-stimulated condition. (A) Raw 264.7 cells were treated with LPS (200 ng/mL) for 12 h first, followed by removing the LPS & added CQ (30 µM), SAR (1 µM), Torin (1 µM), Rap (1 µM) for another 12 h. CTRL is blank control group with DMSO treatment. (B) Western blot analysis of iNOS in Raw 264.7 cells under LPS treatment. (C) Western blot analysis of p62 in Raw 264.7 cells under LPS treatment. (D) Raw 264.7 cells were treated LPS (200 ng/mL) for 12 h, then removed LPS added CHX (1 µg/mL) & autophagy related drugs for another 12 h. (E) Level of iNOS in Raw 264.7 cell after CHX treatment. (B–E) Values were analyzed from three individual experiments by GraphPad Prism, each experiment conducted three times. * p < 0.05, ** p < 0.01, *** p < 0.001. Error bars (mean ± SEM). One-way ANOVA with Turkeys as post hoc tests. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31618870), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-31020241682195.jpg)
![Immunocytochemistry/ Immunofluorescence: LC3B Antibody - BSA Free [NB100-2220] - Autophagic pathway regulates inflammasome activation in blood-derived monocytes stimulated with M. leprae. (A–C) Monocytes were purified from healthy donors’ peripheral blood mononuclear cells by 2-h adherence & stimulated with 10 µg/mL M. leprae (ML) in the presence or absence of autophagy regulators for 18 h. Autophagy was triggered with 200 ng/mL rapamycin (RP), & inhibited with 100 µM chloroquine (CQ, autophagic flux blocker) & 10 µM 3-methyladenine (3-MA). (A) Monocytes stimulated with M. leprae, RP, CQ, & 3-MA were fixed & stained with anti-NLRP3 (red), anti-LC3B (green) antibodies & DAPI (blue). Monocytes stimulated with M. leprae increase the number of LC3-II-decorated autophagosomes (puncta) per cell, which is reforced by RP addition, & reverted by 3-MA. Autophagy blocking with CQ & 3-MA was able to increase NLRP3 specks numbers per cell in relation to the well stimulated with M. leprae & RP. Immunofluorescence images were quantified & bars represent the mean values of the number of LC3 puncta & NLRP3 specks per cell ± SEM (n = 3). *(in relation to NS) or #(indicated by the dashes) p < 0.05. Scale bar: 10 µm. (B) Purified mRNAs from monocyte cultures stimulated with M. leprae, the autophagy blocker 3-MA, & RP, as a control of autophagy activation, were analyzed by RT-qPCR for LC3B & IL1B. Bars represent the mean of the fold change values in relation to the non-stimulated controls of three independent experiments with similar results. (C) The IL-1 beta , IL-6, & TNF levels in the monocyte cultures supernatants were assessed by ELISA. Bars represent the fold change values in relation to the non-stimulated controls ± SEM (n = 3). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29915584), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-31020241554517.jpg)
![Immunocytochemistry/ Immunofluorescence: LC3B Antibody - BSA Free [NB100-2220] - Melatonin induced LC3 aggregation & conversion. a GFP-LC3 aggregation & conversion in U87MG cells stably expressing an exogenous fusion protein, green fluorescent protein (GFP) & microtubule-associated light chain 3 (LC3) (U87-GFP-LC3), after treatment with DMSO (control), rapamycin (RAP 200 nM), melatonin (MEL 1 mM) or agomelatine (AGO 2 μM) for 24 h (×40); b U87MG cells & c A172 cells treated with DMSO (control), rapamycin (RAP 200 nM), melatonin (MEL 1 mM), agomelatine (AGO 2 μM) & luzindole (LUZ 5 μM/L) for 24 h were fixed & analyzed for endogenous LC3 dots by immunofluorescence using anti-LC3 antibodies (green), DAPI (blue) staining shows the nuclei (×40). d Stable U87-GFP-LC3 cell lines & GFP in vector control. U87MG cells stably expressing an exogenous fusion protein, green fluorescent protein (GFP) & microtubule-associated light chain 3 (LC3) (U87-GFP-LC3) (×40) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31870319), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-31020241612627.jpg)
![Immunocytochemistry/ Immunofluorescence: LC3B Antibody - BSA Free [NB100-2220] - Autophagy induction by atorvastatin in T24 human bladder cancer cells. (A) Immunocytochemistry for the co-localization of LC3 puncta (green) & Lysotracker (red, demarcation for the lysosome) after atorvastatin treatments (30 μM) for 24 h in T24 cells. Rapamycin treated T24 cells were the positive control of autophagy induction. 4′,6-diamidino-2-phenylindole (DAPI) was used for nucleus staining. Scale bar = 100 μm; (B) High magnification view of immunocytochemistry for the co-localization LC3 puncta (green) & Lysotracker after atorvastatin treatments (30 μM) for 24 h in T24 cells at the single-cell level. Scale bar = 50 μm; (C) Western blot analysis of autophagosome formation markers p62/SQSTM1, LC3-I & LC3-II in untreated (control) & atorvastatin (30 μM) treated T24 cells. Image collected & cropped by CiteAb from the following publication (//www.mdpi.com/1422-0067/15/5/8106), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-310202415541929.jpg)
![Immunocytochemistry/ Immunofluorescence: LC3B Antibody - BSA Free [NB100-2220] - Increased LC3B-positive puncta correlated positively with vascular remodeling during AngII-induced hypertension. (A) Western blot analysis of LC3B-II expression in aortas from sham or AngII-infused mice at different time points after operation. **P < 0.01 vs. the corresponding sham group, Student's t-test. n = 10 mice/group. (B) Representative immunofluorescence staining of LC3B (green) & alpha -SMA (red) in thoracic aorta section. Nuclei were stained with DAPI. Scale bars, 20 µm. (C) Quantification of LC3B puncta. Five random fields (2,500 µm2/filed) were measured in one section. Statistical significance was determined by one-way ANOVA. **P < 0.01 vs. sham, n = 12 sections from six mice per group. (D-G) Structural parameters of mouse aorta from sham & hypertensive mice. WD, wall diameter; LD, lumen diameter; CSA, cross-sectional area. *P < 0.05, **P < 0.01 vs. the corresponding sham group, Student's t-test. n = 10 mice/group. (H) Correlation between changes in LC3B puncta & CSA values. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32226533), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-31020241555241.jpg)
![Immunohistochemistry: LC3B Antibody - BSA Free [NB100-2220] - Representative images of the variation of LC3 staining associated with cavities in SDH activity & mitochondrial COX-1 staining in PAD gastrocnemius muscle sections. First column shows succinate dehydrogenase (SDH) activity (dark fibers are type I, intermediate fibers are type IIa, & light fibers are type IIa/x), second column shows mitochondrial COX-1 protein (green), third column shows LC3 (red) & fourth column shows COX-1 & LC3 merged. Examples of normal fibers with no LC3 staining or COX-1 cavities (rowA), punctate LC3 staining where a COX-1 cavitiy is forming (row B), elevated LC3 staining with low COX-1 staining (rowC), LC3 accumulation in areas lacking COX-1 staining (row D), & LC3 plaque in the center of an SDH/COX1 cavity (COX-1; rowE). Arrows within the same row point to areas of LC3 accumulation in same fiber. Scale bar = 100 µM Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27687713), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-3102024168218.jpg)
![Immunocytochemistry/ Immunofluorescence: LC3B Antibody - BSA Free [NB100-2220] - Vps34 inhibition blocks autophagy initiation & causes accumulation of ubiquitin-positive & p62-positive structures. a Representative confocal images of cortical neurons treated with vehicle, Bafilomycin A1 (BafA1) at 50 nM, VPS34IN1 at 3 µM or cotreated for 3 h. Arrows highlight LC3 & p62 structures. Right panel, bar graphs denote average object intensity, per cell (mean ± SEM, N = 49-60 cells, from three independent experiments). Scale bar, 10 µm. ***p < 0.001 in one-way ANOVA, Holm–Sidak’s multiple comparisons test. b Representative confocal images of cortical neurons treated as in a & immunostained for LAMP-1, LC3, & p62. Airyscan insets highlight position of LC3 & p62 structures relative to LAMP-1-positive membranes. Scale bar, 10 µm. c Representative confocal images of cultured cortical neurons treated with vehicle or VPS34IN1 at 3 µM for 24 h. Arrows highlight p62 & ubiquitin colocalization. Scale bar, 10 µm Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41467-017-02533-w), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-3102024155521.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB100-2220] - Mechanistic analysis of autophagic inhibition in ATO-treated HepG2. a The viability of HepG2 & NB4 cells after incubation with ATO at various concentrations for 48 h (n = 3; error bars are s.d.). Upper: Confocal images of NB4 or HepG2 cells after being stained with calcein AM. Scale bars: 10 μm. b The viability of HepG2 & NB4 cells after incubation with CQ, ATO, or CQ–ATO mixture for 48 h (n = 3). ##P < 0.01 by t-test, significantly different from ATO. ns not significant. c Immunoblots of autophagy-related proteins LC3-II, p62 (left); semi-quantified analysis (n = 3) in NDs, ATO, or NDs–ATO mixture-treated cells (right). GAPDH was used as the loading control. Normalized band densities were shown below each band. d Cell viability & Caspase-3 activity after incubation with ATO or NDs–ATO mixture for 48 h (n = 3). ##P < 0.01 by t-test, significantly different from ATO. e Immunostaining of LC3 in NDs, ATO, or NDs–ATO mixture-treated cells (left). Scale bar: 20 μm. TEM images of ATO or NDs–ATO mixture-treated cells (right). Scale bars: 1 μm. Typical structures of autophagosomes induced by ATO & autolysosome containing NDs induced by NDs–ATO mixture are indicated with green or blue arrows, respectively (magnification). Vacuoles inside cells are indicated with red arrows (magnification). Scale bars: 500 nm. Error bars are s.d. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30341298), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-310202415525276.jpg)
![Immunocytochemistry/ Immunofluorescence: LC3B Antibody - BSA Free [NB100-2220] - Rop-DPRL impairs autophagy. (A) Fluorescent images of GFP-LC3-HeLa cells treated with 1.5 mM ropivacaine for 0-24 h, or starvation for 0-24 h, & stained with 75 nM LysoTracker Red. Scale bar = 5 µm. (B) Western blot & (C) statistical results of P62, immature & mature cathepsin D (CathD), LC3I, LC3II, & beta -actin. HeLa cells were treated with ropivacaine or starvation for 0-24 h. (D) Western blot & (E) statistical results of P62, LC3I, LC3II, & beta -actin. HeLa cells were treated with PBS, CQ (50 µM), ropivacaine, or CQ+Rop for 24 h. (F) Fluorescent images of GFP-LC3-HeLa cells treated with empty liposome or Rop-DPRL for 24 h & stained with 75 nM LysoTracker Red. Scale bar = 5 μm. (G,I, K & M) Western blot & (H,J,L & N) statistical results for P62, LC3I, LC3II & beta -actin. Cells were treated with empty liposome, CQ, Rop-DPRL, starvation or indicated combination for 24 h. Data are presented as the mean ± SEM, *p < 0.05, ** p < 0.01, *** p < 0.001, ns = no significant difference, Rop: ropivacaine, starv: starvation. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32308756), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-31020241682123.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB100-2220] - PERK pathway-independent induction of prosurvival autophagy in KG1 LSC-like cells upon G9a inhibition. a, LC3-I/II & p62 expression, analyzed by western blotting, after cell treatment with BIX-01294 (15 μmol/L) in the absence or presence of bafilomycin A1 (BafA1) for 24 h. b, Confocal microscopy images of GFP-LC3-transfected cells after treatment with BIX-01294 (5 μmol/L). c, Apoptotic fractions, measured using flow cytometry, after cell treatment with BIX-01294 (15 μmol/L) in the absence or presence of the autophagy inhibitor 3-MA (5 mmol/L) or BafA1 (2 nmol/L) for 48 h. d, Protein expression, analyzed by western blotting with the indicated antibodies, after treatment of PERK siRNA-transfected & non-transfected cells with BIX-01294 (15 μmol/L) for 48 h. e, Protein expression, analyzed by western blotting with the indicated antibodies, after cell treatment with BIX-01294 (10 μmol/L) in the absence or presence of GSK2606414 (20 μmol/L) for 48 h. f, Protein expression, analyzed by western blotting with the indicated antibodies, after treatment of NRF2 siRNA-transfected & non-transfected cells with BIX-01294 (10 μmol/L) for 48 h. g, Levels of apoptosis, evaluated by flow cytometry, after cell treatment for 48 h with BIX-01294 (10 μmol/L) in the absence or presence of the PERK inhibitor GSK2606414 (10 μmol/L) or the autophagy inhibitor 3-MA (5 mmol/L), or BafA1 (2 nmol/L). h, Levels of apoptosis, evaluated by flow cytometry, after treatment of PERK siRNA- or control siRNA-transfected cells with BIX-01294 (10 μmol/L) in the absence or presence of 3-MA (5 mmol/L) or BafA1 (2 nmol/L) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32293500), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-310202415525287.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB100-2220] - TLR4 mediates Hsp70/Hsp90-induced catabolic response in myotubes. a Hsp70 & Hsp90-induced catabolic response in myotubes is dependent on TLR4. C2C12 myoblasts were transfected with siRNA as indicated. After differentiation, myotubes were treated with rHsp70 & rHsp90 & analyzed for catabolic response as described above. b LLC-released EVs induce muscle catabolism in C2C12 myotubes through TLR4. C2C12 myotubes with either TLR2 or TLR4 knockdown were treated with EVs isolated from LCM (AchE 6 mU) & analyzed for catabolic response. c CD9-positive EVs activate TLR4 in reporter cells. EVs isolated from LCM were subjected to immunoprecipitation (IP) using an antibody against CD9 with pre-immune IgG as control. Resulting pellet & supernatant were used to treat TLR4 reporter cell line HEK-Blue hTLR4 for 24 h, & compared with original EVs. TLR4 activation was measured as SEAP activity. Data (n = 3) were analyzed by analysis of variance. * denotes a difference (P < 0.05) Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41467-017-00726-x), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-310202415533814.jpg)
![Immunocytochemistry/ Immunofluorescence: LC3B Antibody - BSA Free [NB100-2220] - cIAP2 & XIAP regulate autophagosome fusion, but not cIAP1.a MEFs expressing mCherry-GFP-LC3b were transfected with siRNA against either cIAP1, cIAP2 or XIAP. Cells were analysed with the microscope & the number of mCherry+, & GFP + puncta/cell were calculated & the ratio of GFP + /mCherry + puncta is indicated. Shown are the means & the error bars represent the SEM of at least three independent experiments. Westerns show efficient knockdown of cIAP1 & XIAP expression. cIAP2 siRNA efficiency was determined by real time PCR as shown in the graph below the westerns. b Wild type & cIAP2−/− XIAP−/− dermal fibroblasts expressing mCherry-GFP-LC3b were treated analysed on the microscope & mCherry+, & GFP + puncta/cell were calculated. The ratio of GFP+/mCherry + puncta is indicated. c Wild type & cIAP2−/− XIAP−/− dermal fibroblasts were left in complete media (CM) or starved for 2 h in EBSS. Cells were lysed & proteins analysed by western blot for XIAP, LC3, & Actin. cIAP2−/− was confirmed by PCR due to lack of effective antibodies for mouse cIAP2 (see supplemental Fig. 2). d Immunofluoresence showing accumulation of LC3 in starved cIAP2−/− XIAP−/− dermal fibroblasts. Wild type & cIAP2−/− XIAP−/− dermal fibroblasts were incubated in complete media or starved in EBSS for 2 h, then fixed & stained for LC3 (green channel) & LAMP2 (red channel). Nuclei are stained blue with Hoechst. Shown in upper panels are overviews. Lower panels show zoomed in regions indicated in the upper panels Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29743550), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-310202415541921.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB100-2220] - Enhanced mTORC2 signaling is sufficient to protect MSC from calcification. Flag-tagged rictor or green fluorescent protein (GFP) as a control were introduced into MSC by lentiviral transfer. Cells were cultured for 21 days under control conditions, with osteoblast induction medium (OM) & vehicle, or OM & 20 nM Rapa as indicated. (A) Western blot analyses of rictor & flag confirming overexpression of rictor due to gene transfer, downstream targets of the two mTOR complexes (mTORC1: pp70-S6KSer389; mTORC2: pAKTSer473), inhibition of autophagy (LC3B II, p62), cellular senescence (p16INK4a), & apoptosis-related proteins (Bcl-2: negative regulator of apoptosis; cleaved caspase 3 (cl casp 3): executioner caspase). Representative western blots from six independent experiments are shown. For densitometric quantification, band intensities were normalized to GAPDH as a loading control. Control (no OM) was set to 1. (B) Lactate dehydrogenase (LDH) activity in cell culture supernatants normalized to total protein concentrations was determined to quantify cell death. Control was set to 1. (C) Alkaline phosphatase (ALP) activity normalized to total protein concentrations was measured after 7 days of incubation. (D) Calcium deposition was quantified with the ortho-cresolphthalein method & normalized to total protein concentrations. Bars represent mean + SEM, *P < 0.05, **P < 0.01, ***P < 0.001. Numbers of independent experiments are indicated at the bottom of each graph. (E) Alizarin red S staining of calcium deposits. Representative experiment out of six, phase contrast microscopy, original magnification x200, scale bar = 100 µm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31882658), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-310202415523919.jpg)
![Immunocytochemistry/ Immunofluorescence: LC3B Antibody - BSA Free [NB100-2220] - Autophagy induction by atorvastatin in T24 human bladder cancer cells. (A) Immunocytochemistry for the co-localization of LC3 puncta (green) & Lysotracker (red, demarcation for the lysosome) after atorvastatin treatments (30 μM) for 24 h in T24 cells. Rapamycin treated T24 cells were the positive control of autophagy induction. 4′,6-diamidino-2-phenylindole (DAPI) was used for nucleus staining. Scale bar = 100 μm; (B) High magnification view of immunocytochemistry for the co-localization LC3 puncta (green) & Lysotracker after atorvastatin treatments (30 μM) for 24 h in T24 cells at the single-cell level. Scale bar = 50 μm; (C) Western blot analysis of autophagosome formation markers p62/SQSTM1, LC3-I & LC3-II in untreated (control) & atorvastatin (30 μM) treated T24 cells. Image collected & cropped by CiteAb from the following publication (//www.mdpi.com/1422-0067/15/5/8106), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-310202415532040.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB100-2220] - OSI induces autophagy by activating LKB1/AMPK signaling in CRC cells.a Immunoblotting analysis of AMPK, phosphorylated AMPK (Thr172) & LC3 levels in CRC cells treated with indicated concentration of OSI for 24 h. b Immunohistochemistry analysis of AMPK phosphorylation levels in xenograft tissues. Scale bar, 50 μm. c Relative intensity of phosphorylated AMPK staining in (b). d CRC cells were transfected with siScramble or siAMPK for 24 h & followed by treatment with or without 5 μM for another 24 h. LC3 & phosphorylated AMPK (Thr172) levels were detected by immunoblotting. e CRC cells were transfected with empty vector or DN-AMPK plasmid for 24 h, followed by treatment with or without 5 μM OSI for another 24 h. LC3 & AMPK phosphorylation levels were determined by immunoblotting. f CRC cells were treated as in (d), the endogenous LC3 puncta in CRC cells were assessed by immunofluorescence. Scale bar, 10 μm. g The number of LC3 puncta per cell in (f). h CRC cells were treated as in (e), the endogenous LC3 puncta in CRC cells were assessed by immunofluorescence, Scale bar, 10 μm. i The number of LC3 puncta per cell in (h). j Immunoblotting analysis of phosphorylated LKB1 & phosphorylated CaMKK beta levels in CRC cells treated with or without 5 μM OSI. Data are presented as mean SEM, Student’s t-test, & are representative of three independent experiments. ***P < 0.001 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31409796), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-310202415532067.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB100-2220] - Cathepsin inhibitors promote neuronal survival after glucose reperfusion (GR).After 3 h GD, neuro2a cells were replaced by 20; pepstatin A (PA, 10 uM), leupeptin (Leu, 10 uM) or both (PA+Leu). (A) Cell viability was assessed using the MTT assay. MTT mitochondrial reduction was shown as a relative percentage of the MTT values at the indicated time point (3 h GD/48 h GR) from three independent experiments ± SD (*p<0.05, **p<0.001). (B) Changes of protein level by cathepsin inhibitors were analyzed by immunoblot analysis. Proteins from cell lysates were fractionated on SDS-PAGE; blots were probed with anti-LC3, anti-p62, anti-cleaved caspase-3, & anti-PARP antibodies. Tubulin was used as loading control. (C) The graphs represent relative band density of each protein shown in (B). The amount of each protein was normalized against the amount of tubulin. Data represent the mean ± SD (*p<0.05, n = 3). Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0076466), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2220_rabbit-polyclonal-lc3b-antibody-31020241553712.jpg)
![Analysis of LC3B in HeLa cells using anti-LC3B antibody (red) [Catalog # NB600-1384]. Nuclei were counterstained with DAPI (blue).](http://images.novusbio.com/fullsize/LC3B-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NB600-1384-img0033.jpg)
![Analysis of LC3B in treated U87-MG (human glioblastoma astrocytoma) lysates using anti- [Catalog # NB600-1384].](http://images.novusbio.com/fullsize/LC3B-Antibody---BSA-Free-Western-Blot-NB600-1384-img0027.jpg)
![Staining of treated U373-MG (human glioblastoma) cells using anti- [Catalog # NB600-1384].](http://images.novusbio.com/fullsize/LC3B-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NB600-1384-img0030.jpg)
![Analysis of U87MG glioma xenografts using anti- [Catalog # NB600-1384]. Image from verified customer review.](http://images.novusbio.com/fullsize/LC3B-Antibody---BSA-Free-Immunohistochemistry-Paraffin-NB600-1384-img0023.jpg)
![Immunocytochemistry/ Immunofluorescence: LC3B Antibody - BSA Free [NB600-1384] - Assesment of functional basal autophagy in vitro(A) Immunoblotting of LC3B & p62 upon pharmacological autophagy inhibition. A dose-dependent increase of LC3B & p62 was observed with increasing concentrations of chloroquine. (B) Immunofluorescence of LC3B & p62 upon pharmacological autophagy inhibition. I. In CC cell lines HT-29 & II. LoVo a dose-dependent increase of LC3B & p62 was observed with increasing concentrations of chloroquine. (C) Electron microscopy of CC cell lines pharmacological autophagy inhibition. I-III. In CC cell line HT-29 a dose-dependent increase of cytoplasmic vesicles was observed with increasing concentrations of CQ. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28903368), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-310202415384116.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB600-1384] - Phosphorylation of AKT & mTOR decreases after treatment with gemcitabine (GCB)A LM7, CCH-OS-D, & K7M3 osteosarcoma cells were treated with 1μM GCB & cell lysates were analyzed by immunoblotting with specific antibodies for AKT, mTOR, p-AKT, & p-mTOR. beta -actin was used as a loading control. Densitometry was performed using ImageJ. B. & C. Following treatment with GCB, lysates were analyzed using the Human Phospho Kinase Antibody Array. The phosphorylation levels of AKT, mTOR, PRAS40, p70S6K, JNK, AMPK, & ERK were evaluated. Densitometry was performed using Image J. Values were graphed as relative fold change. Means ± standard deviation of three independent experiments are shown. Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.20308), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-310202415304227.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB600-1384] - Autophagy decreases during striatal development. (A) Representative Western blot images for LC3B, p62, DARPP32, & actin. Quantification of (B) LC3B-ii relative to actin, (C) LC3B-ii relative to LC3B-i, (D) p62 relative to actin normalized to P120 values. Data analyzed with one-way ANOVA; (B) Age: F(4,21) = 6.526, p = 0.0014; (C) Age: F(4,22) = 3.797, p = 0.0171; (D) Age: F(4,15) = 3.762, p = 0.0260. *p 0.01); (b) FTC-133/TPC-1 cells transfected with HMGB1 shRNA & control shRNA were starved by HBSS for 3 h & then treated with rapamycin (1 μM) for 12 h. Flow cytometry was performed for measuring the ROS level by a DCFH-DA probe in indicated cells. Rap, rapamycin. (n = 3, *P 0.01); (c) FTC-133/TPC-1 cells were transfected with HMGB1 shRNA & control shRNA & then starved by HBSS for 3 h. ATP levels were detected by ATP Assay Kit (n = 3, *P > 0.01); (d) FTC-133/TPC-1 cells were pretreated with NAC (2 mM) & then starved by HBSS for 3 h. LC3-I/II, NIS, p-AMPK, AMPK, p-mTOR, mTOR, p-p70S6K & p70S6K levels were assayed by Western blot; (e) FTC-133/TPC-1 cells transfected with HMGB1 shRNA & control shRNA were starved by HBSS for 3 h & then treated with rapamycin (1 μM) for 12 h. LC3-I/II, NIS, p-mTOR & mTOR levels were assayed by Western blot. Rap, rapamycin Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31331356), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-31020241617143.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB600-1384] - Serum starvation induces autophagy & apoptosis in endothelial cells.A Evaluation by Hoechst 33342 & propidium iodide (HO/PI) staining of apoptosis & necrosis in HUVECs exposed to normal medium (N) or serum-starved (SS) for 4 h. P values obtained by unpaired t test. n = 10 for each condition. Scale bar = 25 μm. B Quantification of caspase-3 activity in HUVECs exposed to N or SS HUVECs for 1, 2, 3, & 4 h. P values obtained by one-way ANOVA. n = 4 for each condition. C Immunoblot & densitometric analysis of PARP, LC3, & SQSTM1/p62 in HUVECs exposed to N or SS for 1, 2, or 4 h. beta -actin (ACTB) was used as a loading control. P values obtained by unpaired t test (*P 0.01, **P > 0.01); (d) Dynamic uptaking: FTC-133/TPC-1 cells were transfected with HMGB1 shRNA & control shRNA & starved by HBSS for 3 h. Indicated cells were cultured with 175 KBq 131I for 5, l0, 20, 30, 60, 90 & 120 min. The uptake of 131I in indicated cells was detected by a gamma counter; (e) Radionuclide uptaking: FTC-133/TPC-1 cells were transfected with HMGB1 shRNA & control shRNA in the presence or absence of 3-MA (10 mM) treatment for 1 h & then starved by HBSS for 3 h. After 1-h incubating with 131I, the uptake of 131I in indicated cells was detected by a gamma counter (n = 3, *P 0.01); (f) FTC-133/TPC-1 cells transfected with HMGB1 shRNA & control shRNA were starved by HBSS for 3 h & then treated with rapamycin (1 μM) for 12 h. After 1-h incubating with 131I, the uptake of 131I in indicated cells was detected by a gamma counter. Rap, rapamycin. (n = 3, *P 0.01) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31331356), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-310202416161815.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB600-1384] - ROS was sufficient for inducing HMGB1 translocation & enhancing autophagy (a) FTC-133/TPC-1 cells were pretreated with the antioxidant (NAC, 2 mM) for 1 h & then starved by HBSS for 3 h. ROS production was assessed by measuring the fluorescent intensity of DCF on a fluorescent plate reader. Incremental production of ROS was expressed as a percentage of control (n = 3, *P 0.01); (b) FTC-133/TPC-1 cells transfected with HMGB1 shRNA & control shRNA were starved by HBSS for 3 h & then treated with rapamycin (1 μM) for 12 h. Flow cytometry was performed for measuring the ROS level by a DCFH-DA probe in indicated cells. Rap, rapamycin. (n = 3, *P 0.01); (c) FTC-133/TPC-1 cells were transfected with HMGB1 shRNA & control shRNA & then starved by HBSS for 3 h. ATP levels were detected by ATP Assay Kit (n = 3, *P > 0.01); (d) FTC-133/TPC-1 cells were pretreated with NAC (2 mM) & then starved by HBSS for 3 h. LC3-I/II, NIS, p-AMPK, AMPK, p-mTOR, mTOR, p-p70S6K & p70S6K levels were assayed by Western blot; (e) FTC-133/TPC-1 cells transfected with HMGB1 shRNA & control shRNA were starved by HBSS for 3 h & then treated with rapamycin (1 μM) for 12 h. LC3-I/II, NIS, p-mTOR & mTOR levels were assayed by Western blot. Rap, rapamycin Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31331356), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-310202416182641.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB600-1384] - Fucoxanthin activated autophagy after TBI.(A) Representative images of immunofluorescence for LC3 surrounding the injured cortex. LC3 punctate dots were observed in the cytoplasm by immunofluorescent staining of LC3 (red). Neuron cells & nuclei are labeled with NeuN (green) & DAPI (blue), respectively. Magnification: 40 x. Scale bar: 50 mm. (B) Mice brain tissues were collected 1 day after TBI in different groups, & the expression of LC3, Beclin-1 & p62 was measured by western blot. Fucoxanthin treatment significantly increased the level of LC3-II & Beclin-1 while decreasing the level of p62 after TBI. (C) 3-MA (400 nM) was injected i.c.v. 30 min before TBI. Mice were then subjected to TBI & treatment of fucoxanthin 30 min after TBI. Pretreatment with 3-MA significantly attenuated fucoxanthin-induced activation of autophagy & suppression of apoptosis & oxidative stress in the ipsilateral cortex. Data are presented as mean ± SEM, n = 6 per group; **p 0.01, **P > 0.01); (d) Dynamic uptaking: FTC-133/TPC-1 cells were transfected with HMGB1 shRNA & control shRNA & starved by HBSS for 3 h. Indicated cells were cultured with 175 KBq 131I for 5, l0, 20, 30, 60, 90 & 120 min. The uptake of 131I in indicated cells was detected by a gamma counter; (e) Radionuclide uptaking: FTC-133/TPC-1 cells were transfected with HMGB1 shRNA & control shRNA in the presence or absence of 3-MA (10 mM) treatment for 1 h & then starved by HBSS for 3 h. After 1-h incubating with 131I, the uptake of 131I in indicated cells was detected by a gamma counter (n = 3, *P 0.01); (f) FTC-133/TPC-1 cells transfected with HMGB1 shRNA & control shRNA were starved by HBSS for 3 h & then treated with rapamycin (1 μM) for 12 h. After 1-h incubating with 131I, the uptake of 131I in indicated cells was detected by a gamma counter. Rap, rapamycin. (n = 3, *P 0.01) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31331356), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-31020241616376.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB600-1384] - Metformin treatment increases cisplatin effects; (A) MDA-MB-231 & Ca Ski cells were either left untreated or treated with metformin or cisplatin alone or metformin in combination with cisplatin for 15 days. At the end of the treatment, cells were processed to obtain whole cell lysates. MAP1LC3B, pPRKAA2Thr172, PRKAA2 & CASP3 (cleaved) expression was determined by Western blot. ACTB was used as loading control. Densitometric analysis of the gels was performed as described under Materials & Methods; (B) MDA-MB-231 & Ca Ski cells were either left untreated or treated with metformin or cisplatin alone or metformin in combination with cisplatin for 15 days. Ammonia level in the culture medium was measured as indicated in the Material & Methods section. # Significantly different from treatment with metformin alone. All experiments in this figure were repeated three times. * Significantly different from control untreated cells. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30646605), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-31020241618938.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB600-1384] - Autophagy & the proteasome regulate CagA stability. (A) Wild-type (WT) & autophagy-deficient (Atg5−/−) MEFs were infected with a CagA+ vacA− isogenic mutant strain (MOI 100) for 8 hours using a gentamycin protection assay. The autophagy marker LC3-II was used to confirm that Atg5−/− MEFs are autophagy-deficient. CagA protein levels were measured by Western blotting using beta -actin as loading control. Graph shows fold change of CagA normalized to beta -actin relative to WT MEFs (mean + SEM; n = 4). (B) AGS cells were infected with a CagA+ vacA− isogenic mutant strain (MOI 50) for 19 hours using a gentamycin protection assay. MG132 (5 μM) was added during the 14-hour low-dose gentamycin incubation. DMSO was used as a vehicle control. CagA protein levels were measured by Western blotting using beta -actin as loading control. Graph shows fold change of CagA normalized to beta -actin relative to vehicle control (mean + SEM; n = 6). (C) AGS cells were infected with a CagA+ vacA− isogenic mutant strain (MOI 50) for 24 hours using a gentamycin protection assay. Lactacystin (10 μM) was added during the 19-hour low-dose gentamycin incubation. Water was used as a vehicle control. CagA protein levels were measured by Western blotting using beta -actin as loading control. Graph shows fold change of CagA normalized to beta -actin relative to vehicle control (mean + SEM; n = 5). Relevant gel bands were cropped from the original blots. Dotted line indicates slicing of two regions together from the same blot. Statistical analysis was performed using Student’s t-test. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30631092), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-310202416173533.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB600-1384] - Vps34 activity is required for maintaining LC3B-ii levels at P10 & mTOR inhibition increases p-Beclin-1 & LC3B-ii levels at P28. (A) Representative Western blot images for actin, DARPP32 & LC3B-i & -ii in striatal slices obtained from P10 or P28 mice, treated with SAR405 (1 μM) or vehicle (Veh; DMSO, 0.1%). (B,C) Quantification of LC3B-ii relative to actin, normalized to vehicle condition at each age. (B) P10: unpaired, two-tailed t-test, t11 = 2.985, p = 0.0124; P28: unpaired, two-tailed t-test, t24 = 1.807, p = 0.0922. P10: Veh: n = 6 slices, SAR405 n = 7 slices from 3 to 4 mice/age. (C) P28: Veh: n = 9 slices, Baf n = 7 slices from 3 to 4 mice/age. *p 0.05 versus untreated group). C. Morphological features of NB4 cells that were treated with ATRA (1 μM) or HMGB1 (1 μg/ml) was determined by Wright-Giemsa staining & visualized by light microscopy (100X magnification). D. Differentiation of NB4 cells treated with ATRA (1 μM) or HMGB1 (10 μg/ml) for 6-48 h was examined by NBT reduction & surface CD11b expression in comparison to the control (DMSO) (n=3, *P<0.05 versus ATRA group). E. Expression of PML-RAR alpha , P62 & LC3-I/II in NB4 cells treated with ATRA (1 μM) or HMGB1 (10 μg/ml) for 48 h was assayed by western blotting & co-immunoprecipitation in comparison to control (DMSO). Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.15432), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-310202416171499.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB600-1384] - Zearalenone (ZEN) induced endoplasmic reticulum (ER) stress & autophagy in HepG2 cells. mRNA level & protein expression were determined by quantitative real-time polymerase chain reaction (qRT-PCR) & Western blot analysis, respectively. (A) The protein expression level of GRP78 was measured in cells treated with ZEN for 1 h. (B) The phosphorylation of eIF2 alpha was evaluated in cells treated with ZEN for 2 h. (C) CHOP mRNA levels, (D) Beclin1 mRNA levels, & (E) LC3-II mRNA levels were determined in cells treated with ZEN for 4 h. (F) The protein expression level of LC3-II/LC3-I was examined in cells treated with ZEN for 24 h. Data represent mean ± SEM of three independent experiments. * indicates significant difference vs. the control (** p < 0.01, & *** p < 0.001). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31861425), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-310202416154612.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB600-1384] - ATRA induces autophagy in SKBR3 cells. (a) SKBR3 & MDA-MB-453 breast cancer cells were treated either with 0.1 or 1 μM ATRA for 2 & 4 days, respectively. beta -Catenin & LC3B levels were measured by western blotting. GAPDH was used as a loading control. (b) LC3B-II quantification from at least three independent experiments. LC3B-II expression was normalized to GAPDH & to vehicle-treated SKBR3 cells. (c) beta -Catenin staining of SKBR3 & MDA-MB453 cells. Cells were control or ATRA (1 μM) treated for 2 days. beta -Catenin FITC (fluorescein isothiocyanate) & nuclear DAPI (4',6-diamidino-2-phenylindole) staining as analyzed by confocal microscopy are shown. (d) Quantification of endogenous LC3B puncta. LC3B in SKBR3 & MDA-MB453 cells treated with 1 μM ATRA for 2 days. (e) LC3B-II western blotting & quantification of the autophagic activation upon treatment with 1 μM ATRA for 2 days in the presence or absence of BafA for 2 h at 200 nM. LC3B-II levels were normalized to GAPDH & to vehicle-treated SKBR3 cells. Standard deviations for five independent experiments are shown. (f) Long-lived protein degradation assay of SKBR3 & MDA-MB453 cells treated as in (e). Radioactivity was determined by liquid scintillation counting of at least three independent experiments. Absolute proteolysis is shown. (g) Long-lived protein degradation assay of SKBR3 treated as in (e) & including treatment with the macroautophagy-specific inhibitor 3-MA (10 mM). Analysis as in (f). Mann–Whitney U-test: *P<0.05, **P<0.01, ***P<0.001 & ****P<0.0001 Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/cddis2015236), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-31020241616052.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB600-1384] - CA1 Tg mice undergo mitochondrial stress. a WB analysis of extracts from 6-mo Wt & Tg mice CA1 (Wt, n = 6; Tg, n = 7), using antibodies against SIRT3, SOD2 & acetylated SOD2. b WB analysis of extracts from 12-mo Wt & Tg mice hippocampi (Wt, n = 5; Tg, n = 5). Data are presented as mean ± SEM (**P < 0.01; ***P < 0.001). WB analysis of extracts from 6-mo Wt & Tg mice CA1 (Wt, n = 6; Tg, n = 5) (c), & from 12-mo Wt & Tg mice hippocampi (Wt, n = 5; Tg, n = 5) (d) for PINK1 & LC-3. Data are presented as mean ± SEM, *P < 0.05. WB analysis of extracts from 6-mo WT & Tg mice CA1 (WT, n = 5; Tg, n = 6) (e), & from 12-mo WT & Tg mice hippocampi (WT, n = 5; Tg, n = 5) (f) for TFAM. Data are presented as mean ± SEM (*P < 0.05), **P < 0.01). Actin was used as loading control Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32131898), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-31020241616181.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB600-1384] - ATRA induces autophagy in SKBR3 cells. (a) SKBR3 & MDA-MB-453 breast cancer cells were treated either with 0.1 or 1 μM ATRA for 2 & 4 days, respectively. beta -Catenin & LC3B levels were measured by western blotting. GAPDH was used as a loading control. (b) LC3B-II quantification from at least three independent experiments. LC3B-II expression was normalized to GAPDH & to vehicle-treated SKBR3 cells. (c) beta -Catenin staining of SKBR3 & MDA-MB453 cells. Cells were control or ATRA (1 μM) treated for 2 days. beta -Catenin FITC (fluorescein isothiocyanate) & nuclear DAPI (4',6-diamidino-2-phenylindole) staining as analyzed by confocal microscopy are shown. (d) Quantification of endogenous LC3B puncta. LC3B in SKBR3 & MDA-MB453 cells treated with 1 μM ATRA for 2 days. (e) LC3B-II western blotting & quantification of the autophagic activation upon treatment with 1 μM ATRA for 2 days in the presence or absence of BafA for 2 h at 200 nM. LC3B-II levels were normalized to GAPDH & to vehicle-treated SKBR3 cells. Standard deviations for five independent experiments are shown. (f) Long-lived protein degradation assay of SKBR3 & MDA-MB453 cells treated as in (e). Radioactivity was determined by liquid scintillation counting of at least three independent experiments. Absolute proteolysis is shown. (g) Long-lived protein degradation assay of SKBR3 treated as in (e) & including treatment with the macroautophagy-specific inhibitor 3-MA (10 mM). Analysis as in (f). Mann–Whitney U-test: *P<0.05, **P<0.01, ***P<0.001 & ****P<0.0001 Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/cddis2015236), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-310202416182623.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB600-1384] - Bmi‐1 deficiency aggravates cardiac hypertrophy & decreases autophagic flux. (A) Representative micrographs of paraffin‐embedded heart ventricular wall sections of 6‐week‐old Bmi‐1–/– mice & WT mice stained for haematoxylin‐eosin (H&E), wheat germ agglutinin (WGA) & Masson's trichrome (Masson) staining. (B) Heart weight relative to body weight (HW/BW) & heart weight relative to tibia length (HW/TL). (C) The wall thickness of interventricular septum. (D) Myocyte cross‐sectional area from Bmi‐1–/– mice relative to WT mice. (E) Collagenous fibre area from Bmi‐1–/– mice relative to WT mice was counted with anterior wall staining for Masson. (F) Anp, Bnp, beta ‐MHC, c‐TnI & GATA4 mRNA levels in hearts by real‐time RT‐PCR, calculated as ratio to beta ‐actin mRNA & expressed relative to WT. (G) Western blots of cardiac tissue extracts & mouse embryonic cardiomyocytes (MECs) showing ANP, BNP, GATA4, LC3B & p16; beta ‐actin was the loading control. (H) Protein levels relative to beta ‐actin were assessed by densitometric analysis. (I) Representative micrographs of paraffin‐embedded heart sections immunohistochemical staining for ANP, BNP & GATA4. (J) The percentage of cells positive for ANP, BNP, GATA4 or positive area relative to total cells or area. (K) Representative micrographs of fluorescence with autophagy lentivirus transfection, with DAPI for nuclei. (L) Percentage of positive GFP dots or mRFP dots relative to total cells. (M) The number of autophagosomes & autolysosomes per cell. Six mice per group were used for experiments. Cell experiments were performed with three biological repetitions per group. Values are mean ± SEM from six determinations per group, *p < .05, **p < .01, ***p < .001 compared with WT group, unpaired Student's t‐test Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35390228), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-31020241618262.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB600-1384] - 8-Cl-Ado-induces autophagy. Immunoblot analysis of (A) phospho-ULK (Ser555) levels & (B) LC3B-I lipidation to form LC3B-II in MCF-7 & BT-474 cells treated with 10 μM of 8-Cl-Ado for the indicated times. (C) Fluorescent microscopy of MCF-7 & BT-474 cells transiently transfected with GFP-LC3B & treated with 10 μM of 8-Cl-Ado for 12-hours to assess aggregation of LC3B. (D) Immunoblot analysis of p62 levels in MCF-7 & BT-474 cells treated with 10 μM of 8-Cl-Ado for the indicated times. The normalized ratio of p62 to GAPDH relative to the untreated control is indicated beneath each lane. (E) Fluorescent microscopic imaging of autolysosomes. MCF-7 cells were untreated or treated for 2-days with 8-Cl-Ado or rapamycin. Cells were stained with MDC, blue, to visualize AVO & Syto 61 (DNA), red, for nuclei counterstaining. (F) Representative flow cytometery histograms of AVO stained with acridine orange in MCF-7 cells untreated or treated for 3 days with 50 nM rapamycin or 10 μM 8-Cl-Ado. Baf was added before 30 min prior to staining to neutralize AVO staining. (G) Quantification triplicate experiments of MCF-7 & BT-474 cells treated & analyzed as in E. Image collected & cropped by CiteAb from the following publication (//jhoonline.biomedcentral.com/articles/10.1186/1756-8722-7-23), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-31020241617525.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB600-1384] - PB induces autophagy but blocks autophagosome trafficking & autophagosome-lysosome fusion in Hep3B cells.(A) Hep3B cells, HepG2 cells, & primary mouse hepatocytes treated w/ increasing concentrations of PB (6–2000 μg/mL) for 24 h; viable cells quantified using the MTT assay. Data are presented as mean ± SD from at least 3 independent experiments. Bars = SD. *P < 0.05, **P < 0.01, ***P < 0.001, control versus PB-treated cells. (B) Hep3B cells treated for 6, 24 & 48 h w/ indicated concentrations of PB. Levels of protein expression analysed by WB using antibodies against LC3B, p62/SQSTM1, ATG12, BECN1 & Actin. Images cropped from different blots run under the same experimental conditions. The original blots attached as Supplementary Figure 3A. (C) Hep3B cells transfected w/ GFP-LC3B treated w/ 240 μg/mL PB for 24 h & then observed under a confocal microscope. (D) Hep3B cells treated for 24 h w/ indicated concentrations of PB. Levels of protein expression analysed by WB using antibodies against phosphorylated & total mTOR, 4EBP1, & p70S6K1 as well as actin. Images cropped from different blots run under the same experimental conditions. The original blots attached as Supplementary Figure 3B. (E) Hep3B cells serum-starved overnight, & incubated w/ or w/out PB (240 μg/mL) for 6 h before stimulating w/ 20 ng/mL EGF for 20 min. EGFR protein levels analysed by confocal microscope. (F) Hep3B cells treated PB for 12, 24 or 48 h w/ indicated concentrations. Levels of protein expression analysed by WB using antibodies against EGFR & Actin. Images cropped from different blots run under the same experimental conditions in each panel. The original blots attached as Supplementary Figure 3C. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/srep41437), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-31020241618948.jpg)
![Western Blot: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - TARDBP monoclonal antibody (M01), clone 2E2-D3 Analysis of TARDBP expression in A-431.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-2E2-D3-Western-Blot-H00023435-M01-img0025.jpg "Western Blot: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - TARDBP monoclonal antibody (M01), clone 2E2-D3 Analysis of TARDBP expression in A-431.")
![Immunohistochemistry-Paraffin: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - TARDBP in rat tissue samples. Image courtsey of product review by Daniel Pirici.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-2E2-D3-Immunohistochemistry-Paraffin-H00023435-M01-img0011.jpg)
![Immunocytochemistry/Immunofluorescence: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - Analysis of monoclonal antibody to TARDBP on HeLa cell. Antibody concentration 10 ug/ml.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-2E2-D3-Immunocytochemistry-Immunofluorescence-H00023435-M01-img0019.jpg)
![Immunohistochemistry-Paraffin: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - TARDBP on formalin-fixed paraffin-embedded human leiomyosarcoma. [antibody concentration 3 ug/ml]](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-2E2-D3-Immunohistochemistry-Paraffin-H00023435-M01-img0013.jpg)
![Western Blot: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - Analysis of TARDBP expression in transfected 293T cell line by TARDBP monoclonal antibody (M01), clone 2E2-D3.Lane 1: TARDBP transfected lysate(44.7 KDa).Lane 2: Non-transfected lysate.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-2E2-D3-Western-Blot-H00023435-M01-img0026.jpg)
![Immunohistochemistry-Paraffin: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - Analysis of monoclonal antibody to TARDBP on formalin-fixed paraffin-embedded human leiomyosarcoma tissue Antibody concentration 3 ug/ml.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-2E2-D3-Immunohistochemistry-Paraffin-H00023435-M01-img0021.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - Analysis of TARDBP over-expressed 293 cell line, cotransfected with TARDBP Validated Chimera RNAi ( Cat # H00023435-R01V ) (Lane 2) or non-transfected control (Lane 1). Blot probed with TARDBP monoclonal antibody (M01), clone 2E2-D3 (Cat # H00023435-M01 ). GAPDH ( 36.1 kDa ) used as specificity and loading control.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-2E2-D3-Western-Blot-H00023435-M01-img0023.jpg)
![ELISA: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - Detection limit for recombinant GST tagged TARDBP is 0.3 ng/ml as a capture antibody.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-2E2-D3-ELISA-H00023435-M01-img0027.jpg)
![Western Blot: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - PDI co-precipitates with TDP-43 & is increased in mutant TDP-43 transgenic mouse spinal cords.(A) Co-immunoprecipitation of wildtype & mutant Q331K TDP-43-mCherry from Neuro2a cell lysates using an anti-PDI antibody followed by TDP-43 immunoblot. Control immunoprecipitations performed using untransfected (Untrans) or mCherry expressing cell lysates, buffer only with coprecipitating antibodies or TDP-43 Q331K cell lysates using an irrelevant, isotype-matched control antibody (IgG). Input control (2%) shows expression of mCherry-TDP43 in wildtype & Q331K cell lysates. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0081170), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/h00023435-m01_mouse-monoclonal-tdp-43-tardbp-antibody-2e2-d3-310202415284521.jpg)
![Western Blot: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - CLIP shows that TDP-43 directly interacts with translational target mRNAs. (A) Schematic diagram of the CLIP experiment. (B) Immunoblot showing specific IP of TDP-43 from MN1 cells under CLIP conditions. A TDP-43 band is specifically observed in the input & TDP-43 IP lanes from both untreated & UV-treated cells, but not in the IgG or anti-RBP X control lanes. RBP X is an IP of a different RNA-binding protein, which serves as an additional specificity control here. (C and D) Plots showing percentage of input mRNA in the TDP-43 IP for the mRNAs indicated in three separate CLIP assays from MN1 cells. Performing CLIP from UV-treated cells leads to significant recovery & enrichment relative to Gapdh for all mRNAs examined (C). In the absence of UV treatment, much less mRNA is recovered & no significant enrichment relative to Gapdh mRNA is observed. Note that the Y-axis scale in D is 1000× smaller than in C, indicating strong crosslinking dependence of mRNA co-immunoprecipitation (n = 3, s.e.m. error bars, P-values indicated in the plot, unpaired two-tailed t-test). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30357366), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/h00023435-m01_mouse-monoclonal-tdp-43-tardbp-antibody-2e2-d3-310202415483647.jpg)
![Western Blot: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - SINE compounds partially rescue motor deficits in an animal model of ALS/FTD. (a) Schematic timeline for in vivo experiments. (b) Western blot demonstrating the expression of human TDP43 within the brains of AAV9-injected animals, which we have previously shown is largely restricted to neuronal cell types (Jackson et al.59). Full-length blots appear in Fig. S1. (c) The hang test measures the time it takes for animals to fall from grid-like scaffold when it is lifted & tilted. A single representative animal administered AAV9-TDP43 is shown; note the inability of the hind limbs to clasp the wire mesh. (d) TDP43 expression impaired motor performance on the hang test at 3 weeks, an effect that could be mitigated by 7.5 mg kg-1 KPT-350. (e) Rotarod testing at 4 weeks of age showed prominent deficits associated with TDP43 expression that were resistant to treatment with SINE compounds. n, number of animals per condition. ns, not significant, mean ± s.e.m. *p < 0.05, **p < 0.01, ***p < 0.001, one-way ANOVA with Bonferroni correction. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-018-22858-w), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/h00023435-m01_mouse-monoclonal-tdp-43-tardbp-antibody-2e2-d3-310202415482260.jpg)
![Immunocytochemistry/ Immunofluorescence: beta Amyloid Antibody (MOAB-2) - BSA Free [NBP2-13075] - No difference in A beta plaque load between propofol (n = 8) & vehicle (n = 6) treated APP/PS1 mice. a An example image of A beta plaque immunoreactivity in the cortex of an APP/PS1 mouse following repeated propofol exposure. b A representative image of A beta plaque immunolabeling the cortex of an APP/PS1 mouse following treatment with vehicle. c Bar graph showing the percentage of the cortex occupied by A beta plaques in propofol & vehicle treated APP/PS1 mice. d Bar graph showing the average size (μm2) of A beta plaques in the cortex of APP/PS1 in the propofol & vehicle treatment groups. e Bar graph showing the average density of A beta plaques (/μm2) in the cortex of propofol & vehicle exposed APP/PS1 mice. All data is shown as mean ± SEM. Scale bar = 500 μm Image collected & cropped by CiteAb from the following publication (//bmcanesthesiol.biomedcentral.com/articles/10.1186/s12871-018-0509-5), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp2-13075_mouse-monoclonal-beta-amyloid-antibody-moab-2-310202416114798.jpg)
![Immunocytochemistry/Immunofluorescence: GAPDH Antibody [NB300-327] - Analysis of HeLa cells stained with rabbit pAb to GAPDH, dilution 1:2000 in red. Blue is Hoescht staining of nuclear DNA. The GAPDH antibody produces diffuse cytoplasmic staining of cells.](http://images.novusbio.com/fullsize/GAPDH-Antibody-Immunocytochemistry-Immunofluorescence-NB300-327-img0007.jpg)
![Western Blot: GAPDH Antibody [NB300-327] - Theoretical molecular weight: 36 kDa. Detection of GAPDH in mouse liver.](http://images.novusbio.com/fullsize/GAPDH-Antibody-Western-Blot-NB300-327-img0002.jpg)
![Western Blot: GAPDH Antibody [NB300-327] - Western blot analysis of extracts from Jurkat and HeLa cells using NB300-327 at 1:1000. Theoretical molecular weight: 36 kDa.](http://images.novusbio.com/fullsize/GAPDH-Antibody-Western-Blot-NB300-327-img0003.jpg)
![Western Blot: GAPDH Antibody [NB300-327] - Analysis of different cell cytosolic or nuclear enriched fractions, GAPDH antibody, dilution 1:20,000 (Red): [1] protein standard, [2] NIH-3T3 cytosolic, [3] NIH-3T3 nuclear, [4] HeLa cytosolic, and [5] HeLa nuclear fractions. Strong band at 37kDa corresponds to GAPDH protein, mainly detected in the cytosolic fractions. The same blot was simultaneously probed with mouse mAb to the nuclear RNA binding protein SF3B4, dilution 1:1,000 (Green). In contrast to GAPDH, SF3B4 is exclusively expressed in the nuclear fraction.](http://images.novusbio.com/fullsize/GAPDH-Antibody-Western-Blot-NB300-327-img0008.jpg)
![Immunocytochemistry/Immunofluorescence: GAPDH Antibody [NB300-327] - The GAPDH antibody was tested in Hela cells at a 1:500 dilution against Dylight 488 (Green). Alpha-tubulin and nuclei were counterstained with Dylight 550 (Red) and DAPI (Blue), respectively.](http://images.novusbio.com/fullsize/GAPDH-Antibody-Immunocytochemistry-Immunofluorescence-NB300-327-img0001.jpg)
![Immunocytochemistry/Immunofluorescence: GAPDH Antibody [NB300-327] - Confocal immunofluorescence analysis of HeLa cells using GAPDH (NB300-327) antibody (green). Nuclei was counterstained with DAPI (blue).](http://images.novusbio.com/fullsize/GAPDH-Antibody-Immunocytochemistry-Immunofluorescence-NB300-327-img0004.jpg)
![Immunocytochemistry/Immunofluorescence: GAPDH Antibody [NB300-327] - IF Confocal analysis of C2C12 cells using GAPDH antibody (NB300-327, 1:20). An Alexa Fluor 488-conjugated Goat to rabbit IgG was used as secondary antibody (green). Actin filaments were labeled with Alexa Fluor 568 phalloidin (red). DAPI was used to stain the cell nuclei (blue).](http://images.novusbio.com/fullsize/GAPDH-Antibody-Immunocytochemistry-Immunofluorescence-NB300-327-img0005.jpg)
![Simple Western: GAPDH Antibody [NB300-327] - Simple Western lane view shows a specific band for GAPDH in 0.2 mg/ml of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system. Note: band observed higer than predicted 36 kDa molecular weight.](http://images.novusbio.com/fullsize/GAPDH-Antibody-Simple-Western-NB300-327-img0006.jpg)
![Western Blot: GAPDH Antibody [NB300-327] - Increased PIP expression in the lungs of PF‐PH compared to PF ratsA, BRelative expression of PIP mRNA (A) & protein (B) normalized to GAPDH.CRepresentative images & PIP quantification.Data information: Values are expressed as mean ± SEM. The number of samples per group for each experiment is included within each bar graph (t‐test; *P < 0.05, **P < 0.01). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31468711), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-327_rabbit-polyclonal-gapdh-antibody-3102024153562.jpg)
![Western Blot: GAPDH Antibody [NB300-327] - Effects of subchronic administration (7 & 14 days) of therapeutic relevant concentration of Brex (Brex: 300 nM) & interaction between Brex & 5-HT1A receptor (5-HT1AR) antagonist WAY100635 (WAY: 10 μM) on protein expression of 5-HT1A (panel A) & 5-HT7 (panel B) receptor in the plasma membrane fraction of cortical primary cultured astrocytes. In left side histograms, ordinate: mean ± SD (n = 6) of the relative protein level of 5-HT1AR & 5-HT7R per GAPDH. * p < 0.05, ** p < 0.01: relative to control (Brex-free) by one-way analysis of variance (ANOVA) with Tukey’s post-hoc test, & @ p < 0.05: relative to Brex for 14 days by Student’s T-test. Right side panels indicate their pseudo-gel images using capillary immunoblotting. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35743014), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-327_rabbit-polyclonal-gapdh-antibody-31020241534337.jpg)
![Western Blot: GAPDH Antibody [NB300-327] - Online lung microarray analysis revealed PIP as one of the Slug transcriptional targets mediating vascular cell proliferation in PF‐PHAHeatmap of the 20 genes upregulated in GSE24988 microarray & known to be Slug transcriptional target.BVenn diagram showing the overlap between Slug targets implicated in cell proliferation & known to be extracellular.CHeatmap of the seven transcriptional targets of Slug known to promote proliferation & to be extracellular.D, ERelative expression of prolactin‐induced protein (PIP) mRNA (D) & protein (E) expression normalized to GAPDH in PF & PF‐PH patients.FRepresentative images of PIP immunohistochemistry showing its extracellular localization & quantification.G–JProliferation assay on healthy fibroblast (G), pulmonary arterial EC (H), & healthy pulmonary arterial SMC (I & J) in the presence or absence of PIP.Data information: Values are expressed as mean ± SEM. The number of samples per group for each experiment is included within each bar graph. Statistical test: panels (D–F): t‐test; panels (G–J): ANOVA (*P < 0.05, **P < 0.01 ***P < 0.001). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31468711), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-327_rabbit-polyclonal-gapdh-antibody-310202416212393.jpg)
![Western Blot: GAPDH Antibody [NB300-327] - Growth of lactobacilli on IECs & their influence towards C. albicans cytotoxicity, adhesion, hyphal length & translocation. (A) LDH release of IECs colonized (Pre-Inc.) or simultaneously colonized (w/o Pre-Inc.) with L. rhamnosus (L.r.) at different MOI (5, 50 or 250) & infected or not with C. albicans (C.a.) (MOI 1) & measured at 24 h post-infection. (B) Growth of L. paracasei (L.p.), L. rhamnosus, L. salivarius (L.s.), L. fermentum (L.f.), & L. brevis (L.b.) on IECs. (C) Percentage of C. albicans adhered to IECs colonized with different Lactobacillus species (MOI 50) at 1 h post-infection. (D) C. albicans hyphal induction on IECs or on plastic colonized with L. rhamnosus or L. brevis (MOI 50) at 4 h post-infection. Results were normalized to C. albicans single infection. (E) Translocation of C. albicans (MOI 1) across IECs colonized with L. rhamnosus or L. brevis (MOI 50) at 24 h post-infection. (F) Assessment of epithelial barrier integrity measured as the loss of transepithelial electrical resistance (TEER) in response to L. rhamnosus or L. brevis (MOI 50) colonization & C. albicans infection in the presence or absence of Lactobacillus colonization at 24 h post-infection. Data are TEER loss in percentage of uninfected host cells (before pre-incubation). (G) E-Cadherin protein expression analyzed by western blot compared to GAPDH in IECs that were left uninfected or colonized with L. rhamnosus (MOI 50) & infected with C. albicans for 6, 12 & 24 h. Data are mean±s.e.m. *P<0.05, **P<0.01, ***P<0.005 (t-test). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31413153), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-327_rabbit-polyclonal-gapdh-antibody-31020241621819.jpg)
![Simple Western: CRISPR-Cas9 Antibody (7A9-3A3) - N-Terminus [NBP2-36440] - Image shows a specific band for Cas9 (observed molecular weight ~158 kDa) in HeLa Cas9 lysate but not in Hela WT lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/CRISPR-Cas9-Antibody-7A9-3A3-N-Terminus-Simple-Western-NBP2-36440-img0013.jpg "Simple Western: CRISPR-Cas9 Antibody (7A9-3A3) - N-Terminus [NBP2-36440] - Image shows a specific band for Cas9 (observed molecular weight ~158 kDa) in HeLa Cas9 lysate but not in Hela WT lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.")
![Immunocytochemistry/Immunofluorescence: CRISPR-Cas9 Antibody (7A9-3A3) - N-Terminus [NBP2-36440] - Hela cells were transiently transfected with an N-terminally Flag-tagged S. pyogenes Cas9 expression vector. The cells were stained with the Cas9 antibody followed by anti mouse-AF488 coupled secondary antibody. Nuclei were counter-stained with Hoechst 33342.](http://images.novusbio.com/fullsize/CRISPR-Cas9-Antibody-7A9-3A3-N-Terminus-Immunocytochemistry-Immunofluorescence-NBP2-36440-img0002.jpg)
![Immunoprecipitation: CRISPR-Cas9 Antibody (7A9-3A3) - N-Terminus [NBP2-36440] - HEK293T expressing N-terminally Flag-tagged S.pyogenes Cas9 were lysed 72h post transfection by resuspending the cells in Hunt buffer and subjecting to 3 freeze-thaw cycles in liquid nitrogen/ice. Proteins were immunoprecipitated from 100ug of whole cell lysate for 1h at 4C with Cas9 supernatant followed by incubation for 1h at 4C with a 1:1 mixture of protein A/G sepharose beads, or for 2h at 4C with Cas9 ab crosslinked to a 1:1 mixture of protein A/G sepharose beads. Beads were washed 2x with Hunt buffer and 1x with TBS. Bound proteins were eluted by boiling in Laemmli, separated by SDS-PAGE and transferred to nitrocellulose. Membrane was blocked, incubated with Cas9 ab, incubated with HRP anti-mouse secondary. *IgG heavy chain](http://images.novusbio.com/fullsize/CRISPR-Cas9-Antibody-7A9-3A3-N-Terminus-Immunoprecipitation-NBP2-36440-img0011.jpg)
![Western Blot: CRISPR-Cas9 Antibody (7A9-3A3) - N-Terminus [NBP2-36440] - Analysis of lysate from Cas9 transfected HEK-293T cells using Cas9 antibody clone 7A9-3A3 at 2ug/ml concentration. The signal was developed using HRP-labelled anti-mouse secondary antibody and ECL based detection. Observed molecular weight is ~158 kDa.](http://images.novusbio.com/fullsize/CRISPR-Cas9-Antibody-7A9-3A3-N-Terminus-Western-Blot-NBP2-36440-img0008.jpg)
![Western Blot: CRISPR-Cas9 Antibody (7A9-3A3) - N-Terminus [NBP2-36440] - Human HEK293 cells were transfected with the indicated CRISPR-Cas9 plasmids, T2 guide RNA, and GFP transgene donor with homology arms to the AAVS1 targeted locus. HDR-mediated transgene integration was measured by FACS analysis of GFP-positive cells, resulting from targeted GFP transgene integration. Indels at the cleavage site were measured by the T7E1 assay. Asterisks indicate that the difference is statistically significant when comparing Cas9-HE, Cas9-HE-Geminin, and Cas9-Geminin to CRISPR-Cas9 in t-test (*P<0.05 or **P<0.005). Relative expression levels of and other fusions were analyzed by western blot with CRISPR-Cas9 and control anti-tubulin antibodies. Protein extracts were obtained with lysis buffer containing 150 mM NaCl. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/s41467-018-03475-7) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/CRISPR-Cas9-Antibody-7A9-3A3-N-Terminus-Western-Blot-NBP2-36440-img0016.jpg)
![Immunocytochemistry/Immunofluorescence: CRISPR-Cas9 Antibody (7A9-3A3) - N-Terminus [NBP2-36440] - DF-1 stable cell line (chicken fibroblast) expressing Cas9 (left )or wildtype DF-1 cells (right) stained with Cas9 antibody NBP2-36440 and phalloidin and DAPI to visualise F-actin and DNA respectively. Cells fixed with 4% PFA. Antibody at 1:500 overnight at 4C. ICC/IF image submitted by a verified customer review.](http://images.novusbio.com/fullsize/CRISPR-Cas9-Antibody-7A9-3A3-N-Terminus-Immunocytochemistry-Immunofluorescence-NBP2-36440-img0014.jpg)
![Immunohistochemistry-Frozen: CRISPR-Cas9 Antibody (7A9-3A3) - N-Terminus [NBP2-36440] - Analysis of a formalin fixed 20um thick frozen section of mouse brain with GBM xenograft tumor areas (GBM cells over expressing SpyCas9 through lentivirus infection). CRISPR-Cas9 antibody (clone 7A9-3A3) was used at 1:50 dilution. The signal was detected using immunofluoresence labeled secondary antibody via Confocal microscopy. Image submitted via verified customer review.](http://images.novusbio.com/fullsize/CRISPR-Cas9-Antibody-7A9-3A3-N-Terminus-Immunohistochemistry-Frozen-NBP2-36440-img0010.jpg)
![Western Blot: CRISPR-Cas9 Antibody (7A9-3A3) - N-Terminus [NBP2-36440] - 20 ug whole cell lysates from control MEF (MEF-WT) and MEF-Cas9 stable cell line. CRISPR-Cas9 antibody (clone 7A9-3A3) was used at 1:1000 dilution. Observed molecular weight is ~158 kDa. Image submitted via verified customer review.](http://images.novusbio.com/fullsize/CRISPR-Cas9-Antibody-7A9-3A3-N-Terminus-Western-Blot-NBP2-36440-img0012.jpg)
![Western Blot: CRISPR-Cas9 Antibody (7A9-3A3) - N-Terminus [NBP2-36440] - Chicken fibroblasts DF-1 cells stably expressing Cas9 in lanes 2 and 4, wild type fibroblasts in lanes 1 and 3 blot, probed with Cas9 antibody. WB image submitted by a verified customer review.](http://images.novusbio.com/fullsize/CRISPR-Cas9-Antibody-7A9-3A3-N-Terminus-Western-Blot-NBP2-36440-img0015.jpg)
![Immunocytochemistry/Immunofluorescence: CRISPR-Cas9 Antibody (7A9-3A3) - N-Terminus [NBP2-36440] - Analysis of Crispr-Cas9 transfected HEK293 cells using CRISPR-Cas9 antibody (clone 7A9-3A3). Red staining represents CRISPR-Cas9 positivity while DAPI stained nuclei are visible in blue color. Image submitted via verified customer review.](http://images.novusbio.com/fullsize/CRISPR-Cas9-Antibody-7A9-3A3-N-Terminus-Immunocytochemistry-Immunofluorescence-NBP2-36440-img0007.jpg)
![Immunoprecipitation: Mouse Monoclonal CRISPR-Cas9 Antibody (7A9-3A3) - N-Terminus [NBP2-36440] - LC-MS/MS signals of a surrogate peptide from Cas9 and a Cas9 variant after immunoprecipitation using CRISPR-Cas9 Antibody (7A9-3A3) [Biotin] (NBP2-36440B). Image from a verified customer review.](http://images.novusbio.com/fullsize/antibody/nbp2-36440_mouse-monoclonal-crispr-cas9-antibody-7a9-3a3-n-terminus-immunoprecipitation-1582024135956..png)
![Western Blot: CRISPR-Cas9 Antibody (7A9-3A3) - N-Terminus - BSA Free [NBP2-36440] - Identification of “HDR-enhancer” (HE) domain of CtIP. a Schematic diagram of CtIP protein showing different truncated CtIP proteins have been fused to Cas9 & tested for their ability to stimulate HDR. Various sequence features of CtIP, including tetramerization & dimerization domains, & CDK phosphorylation sites S233, T245, & S276, are indicated. b Identification of a domain of CtIP, called HE, spanning aa 1 to 296, which is able to stimulate HDR when fused to Cas9. Human RG37 fibroblasts transfected w/ indicated plasmids expressing Cas9 or Cas9–CtIP derivatives, T2 guide RNA plasmid, & GFP transgene donor w/ homology arms to targeted AAVS1 locus. Expression of fusion proteins examined by WB (Supplementary Fig. 1). Data are from four independent experiments. Error bars indicate standard deviation. c Functional analysis of HE domain. HEK293 cells transfected w/ indicated Cas9 plasmids, T2 guide RNA, & GFP transgene donor w/ homology arms to AAVS1 targeted locus. HDR-mediated transgene integration measured by FACS analysis of GFP-positive cells, resulting from targeted GFP transgene integration. Indels at cleavage site measured by T7E1 assay. Results are expressed as mean of relative HDR or indel frequencies calculated by normalizing every HDR or indel frequency by induced by Cas9, respectively. Asterisks indicate difference is statistically significant when comparing Cas9–CtIP or Cas9–HE derivatives to Cas9 in nonparametric t-test (*P<0.05, **P<0.005, or ***P<0.0005). Data are from four independent experiments. Error bars indicate standard deviation. The relative expression levels of Cas9 & Cas9–HE derivatives analyzed by WB using anti-Cas9 & control anti-tubulin antibodies Image collected & cropped by CiteAb from following publication (//pubmed.ncbi.nlm.nih.gov/29556040), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp2-36440_mouse-monoclonal-crispr-cas9-antibody-7a9-3a3-n-terminus-310202416114788.jpg)
![Western Blot: CRISPR-Cas9 Antibody (7A9-3A3) - N-Terminus - BSA Free [NBP2-36440] - Stimulation of transgene integration by Cas9–HE & Cas9–Geminin. Relative frequencies of HDR & indels induced by Cas9 or fusion of Cas9 to HE domain, Geminin degron, or both. Human HEK293 cells were transfected with the indicated Cas9 plasmids, T2 guide RNA, & GFP transgene donor with homology arms to the AAVS1 targeted locus. HDR-mediated transgene integration was measured by FACS analysis of GFP-positive cells, resulting from targeted GFP transgene integration. Indels at the cleavage site were measured by the T7E1 assay. The results are expressed as the mean of relative HDR or indel frequency calculated by normalizing every HDR or indel frequency by that induced by Cas9. Asterisks indicate that the difference is statistically significant when comparing Cas9–HE, Cas9–HE–Geminin, & Cas9–Geminin to Cas9 in t-test (*P<0.05 or **P<0.005). Data are from three independent experiments. Error bars indicate standard deviation. Relative expression levels of Cas9 & other fusions were analyzed by western blot with anti-Cas9 & control anti-tubulin antibodies. Protein extracts were obtained with lysis buffer containing 150 mM NaCl, which resulted in inefficient solubilization of Cas9 fusions with the HE domain compared to those of Cas9 & Cas9–Geminin Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29556040), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp2-36440_mouse-monoclonal-crispr-cas9-antibody-7a9-3a3-n-terminus-3102024161361.jpg)
![Immunocytochemistry/Immunofluorescence: FPRL1/FPR2 Antibody - BSA Free [NLS1878] - Mouse J774A.1, mouse reticulum cell sarcoma macrophage cell line. Left panel is + Anti-Rabbit FITC; middle panel indicates the cell nuclei stained with Hoechst; the right panel is a merged image. ICC/IF image submitted by a verified customer review.](http://images.novusbio.com/fullsize/FPRL1-FPR2-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NLS1878-img0008.jpg)
![<b>Biological Strategies Validation. </b>Immunohistochemistry-Paraffin: FPRL1/FPR2 Antibody - BSA Free [NLS1878] - SPM receptors differentially expressed on endothelium and infiltrating leukocytes AE](http://images.novusbio.com/fullsize/FPRL1-FPR2-Antibody---BSA-Free-Immunohistochemistry-Paraffin-NLS1878-img0011.jpg)
![Flow Cytometry: FPRL1/FPR2 Antibody - BSA Free [NLS1878] - Flow Cytometry: [Alexa Fluor® 700] [NLS1878AF700] - Mouse splenocytes. Cells were pre-gated with live/dead and FSC-A/W to exclude dead cells and cell doublets. Image from verified customer review. Image using the Alexa Fluor 700 form of this antibody.](http://images.novusbio.com/fullsize/FPRL1-FPR2-Antibody---BSA-Free-Flow-Cytometry-NLS1878-img0007.jpg)
![Western Blot: FPRL1/FPR2 Antibody - BSA Free [NLS1878] - Analysis in HL-60 cell lysate.](http://images.novusbio.com/fullsize/FPRL1-FPR2-Antibody---BSA-Free-Western-Blot-NLS1878-img0004.jpg)
![Immunocytochemistry/Immunofluorescence: FPRL1/FPR2 Antibody - BSA Free [NLS1878] - Antibody was tested in Raw264.7 cells with DyLight 488 (green). Nuclei were counterstained with DAPI (blue).](http://images.novusbio.com/fullsize/FPRL1-FPR2-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NLS1878-img0005.jpg)
![Immunohistochemistry: FPRL1/FPR2 Antibody - BSA Free [NLS1878] - Analysis in human kidney cancer using DAB with hematoxylin counterstain.](http://images.novusbio.com/fullsize/FPRL1-FPR2-Antibody---BSA-Free-Immunohistochemistry-NLS1878-img0006.jpg)
![Immunohistochemistry: FPRL1/FPR2 Antibody - BSA Free [NLS1878] - Electron micrographs of FPR2 immunostained sections from the prefrontal cortex. a, b Immunostaining is mostly present in axon pre-terminals (PrT) that did not form synapses with postsynaptic structures. c Occasional axon terminals (AT) are observed to form asymmetrical, putatively glutamatergic synapses (S) with unlabelled dendrites (DE). d Occasional labelled dendrites (DE) are also found, that formed asymmetrical synapses (S) with unlabelled axon terminals (AT). Scale: a, b, c = 50 nm, e = 100 nm Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29948727), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nls1878_rabbit-polyclonal-fprl1-fpr2-antibody-310202415382420.jpg)
![Immunohistochemistry: FPRL1/FPR2 Antibody - BSA Free [NLS1878] - Electron micrographs of FPR2 immunostained sections from the prefrontal cortex. a, b Immunostaining is mostly present in axon pre-terminals (PrT) that did not form synapses with postsynaptic structures. c Occasional axon terminals (AT) are observed to form asymmetrical, putatively glutamatergic synapses (S) with unlabelled dendrites (DE). d Occasional labelled dendrites (DE) are also found, that formed asymmetrical synapses (S) with unlabelled axon terminals (AT). Scale: a, b, c = 50 nm, e = 100 nm Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29948727), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nls1878_rabbit-polyclonal-fprl1-fpr2-antibody-31020241534335.jpg)
![Immunohistochemistry: FPRL1/FPR2 Antibody - BSA Free [NLS1878] - Electron micrographs of FPR2 immunostained sections from the prefrontal cortex. a, b Immunostaining is mostly present in axon pre-terminals (PrT) that did not form synapses with postsynaptic structures. c Occasional axon terminals (AT) are observed to form asymmetrical, putatively glutamatergic synapses (S) with unlabelled dendrites (DE). d Occasional labelled dendrites (DE) are also found, that formed asymmetrical synapses (S) with unlabelled axon terminals (AT). Scale: a, b, c = 50 nm, e = 100 nm Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29948727), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nls1878_rabbit-polyclonal-fprl1-fpr2-antibody-31020241534380.jpg)
![Immunohistochemistry: FPRL1/FPR2 Antibody - BSA Free [NLS1878] - Electron micrographs of FPR2 immunostained sections from the prefrontal cortex. a, b Immunostaining is mostly present in axon pre-terminals (PrT) that did not form synapses with postsynaptic structures. c Occasional axon terminals (AT) are observed to form asymmetrical, putatively glutamatergic synapses (S) with unlabelled dendrites (DE). d Occasional labelled dendrites (DE) are also found, that formed asymmetrical synapses (S) with unlabelled axon terminals (AT). Scale: a, b, c = 50 nm, e = 100 nm Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29948727), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nls1878_rabbit-polyclonal-fprl1-fpr2-antibody-310202415382435.jpg)
![Immunocytochemistry/ Immunofluorescence: FPRL1/FPR2 Antibody - BSA Free [NLS1878] - Lipoxin A4, along with its precursors & ligand, were altered by hAECs. (A): Expression of the lipoxin A4 precursor genes ALOX‐5, ‐12, & ‐15 was increased at days 5 & 7 compared with saline controls (ALOX‐5: 0.393 ± 0.114 vs. 3.777 ± 1.98; ALOX‐12: 0.484 ± 0.248 vs. 1.520 ± 0.203; ALOX‐15: 0.020 ± 0.007 vs. 1.998 ± 0.983). ∗, p < .05. (B): Lipoxin A4 protein levels were elevated in lung lysates at day 7 in animals treated with hAECs compared with controls (0.103 ± 0.021 ng/ml vs. 0.249 ± 0.072 ng/ml, respectively). ∗, p < .05. (C): At day 7, bleomycin challenge resulted in positively stained F4/80/FPR2 cells, which were was elevated in mice treated with hAECs compared with control mice (5.720% ± 0.587% vs. 8.795% ± 0.687%, respectively). ∗, p < .05. (D): Representative images of F4/80‐ & FPR2‐positive‐stained lung sections from hAEC‐treated animals. Magnification: ×200. Scale bar =100 μm. Abbreviations: DAPI, 4′,6‐diamidino‐2‐phenylindole; FPR2, N‐formyl peptide receptor 2; hAEC, human amnion epithelial cell. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28371562), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nls1878_rabbit-polyclonal-fprl1-fpr2-antibody-310202416114742.jpg)
![Western Blot: FPRL1/FPR2 Antibody - BSA Free [NLS1878] - Higher expression of Fpr2 in the livers of female mice is related with hepatocyte protection.a qRT-PCP analysis for Fpr2 expression in primary hepatocytes (pHEPs) from WT (male n = 2, female n = 2) & KO mice (male n = 2, female n = 2). Total eight mice were employed in each hepatocyte isolation, & the experiments were replicated at least three times & the mean ± S.E.M. results are graphed (*p < 0.05, **p < 0.005 vs WT male-pHEPs). b Western blot analysis & c double immunofluorescent images of Fpr2 (red) with albumin (green) in these cells. Gapdh was used as internal control. DAPI (blue) was used as nuclear counterstaining. Data shown represent one of three experiments with similar results (Scale bar, 20 μm). d qRT-PCR analysis for Fpr2 & glucose-6-phosphatase (G6pc) in, e cell viability of, & f western blot analysis of cleaved Caspase-3 & pro Caspase-3 in WT & KO female mice-isolated pHEPs treated with vehicle (Veh) or 250 μM of palmitate (PA). The data shown represent one of three experiments with similar results. The mean ± S.E.M. results obtained from three repetitive experiments are graphed (*p < 0.05, **p < 0.005 vs WT-Veh). Gray circles represent individual data points. See Supplementary Data for statistical details. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35102146), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nls1878_rabbit-polyclonal-fprl1-fpr2-antibody-3102024161228.jpg)
![Immunocytochemistry/Immunofluorescence: rRNA Antibody (Y10b) [NB100-662] - HeLa cells were fixed and permeabilized for 10 minutes with -20C MeOH. The cells were incubated with rRNA Antibody [Y10b] conjugated to Biotin (NB100-662B) at 5ug/ml overnight at 4C and detected with Streptavidin conjugated to DyLight 550. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 100X objective and digitally deconvolved.](http://images.novusbio.com/fullsize/rRNA-Antibody-Y10b-Immunocytochemistry-Immunofluorescence-NB100-662-img0015.jpg "Immunocytochemistry/Immunofluorescence: rRNA Antibody (Y10b) [NB100-662] - HeLa cells were fixed and permeabilized for 10 minutes with -20C MeOH. The cells were incubated with rRNA Antibody [Y10b] conjugated to Biotin (NB100-662B) at 5ug/ml overnight at 4C and detected with Streptavidin conjugated to DyLight 550. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 100X objective and digitally deconvolved.")
![Flow Cytometry: rRNA Antibody (Y10b) [NB100-662] - An intracellular stain was performed on HeLa cells with rRNA Antibody [Y10b] NB100-662B (blue) and a matched isotype control (orange). Both antibodies were conjugated to Biotin. Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature, followed by Streptavidin - R-Phycoerythrin Protein (2012-1000, Novus Biologicals).](http://images.novusbio.com/fullsize/rRNA-Antibody-Y10b-Flow-Cytometry-NB100-662-img0013.jpg)
![Immunocytochemistry/Immunofluorescence: rRNA Antibody (Y10b) [NB100-662] - rRNA antibody was tested in Ntera-2 cells with DyLight 488 (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and DyLight 550 (red).](http://images.novusbio.com/fullsize/rRNA-Antibody-Y10b-Immunocytochemistry-Immunofluorescence-NB100-662-img0004.jpg)
![Immunocytochemistry/Immunofluorescence: rRNA Antibody (Y10b) [NB100-662] - Staining of rRNA in vero cells.](http://images.novusbio.com/fullsize/rRNA-Antibody-Y10b-Immunocytochemistry-Immunofluorescence-NB100-662-img0003.jpg)
![Immunocytochemistry/Immunofluorescence: rRNA Antibody (Y10b) [NB100-662] - HeLa cells were fixed and permeabilized for 10 minutes using -20C MeOH. The cells were incubated with anti-rRNA (Y10b) conjugated to DyLight 488 [NB100-662G] at 5ug/ml for 1 hour at room temperature. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/rRNA-Antibody-Y10b-Immunocytochemistry-Immunofluorescence-NB100-662-img0009.jpg)
![Immunocytochemistry: rRNA Antibody (Y10b) [NB100-662] - Immunohistochemical staining of mouse neuronal progenitor culture using rRNA antibody (green). Image from verified customer review.](http://images.novusbio.com/fullsize/rRNA-Antibody-Y10b-Immunocytochemistry-NB100-662-img0005.jpg)
![Flow (Intracellular): rRNA Antibody (Y10b) [NB100-662] - Analysis using Alexa Fluor (R) 488 conjugate of NB100-662. An intracellular stain was performed on HeLa cells with rRNA antibody (Y10b) NB100-662 (blue) and an isotype control (orange). Cells were fixed with 4% PFA and then permeablized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 488.](http://images.novusbio.com/fullsize/rRNA-Antibody-Y10b-Flow-Intracellular-NB100-662-img0006.jpg)
![Flow (Intracellular): rRNA Antibody (Y10b) [NB100-662] - Analysis of Alexa Fluor (R) 647 conjugate of NB100-662. An intracellular stain was performed on HeLa cells with rRNA (Y10b) antibody NB100-662AF647 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeablized with 0.1%](http://images.novusbio.com/fullsize/rRNA-Antibody-Y10b-Flow-Intracellular-NB100-662-img0007.jpg)
![Flow (Intracellular): rRNA Antibody (Y10b) [NB100-662] - An intracellular stain was performed on RAW 246.7 cells with rRNA Antibody (Y10b) NB100-662APC (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeablized with 0.1% saponin. Cells were incubated in an antibody dilution of 1 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Allophycocyanin.](http://images.novusbio.com/fullsize/rRNA-Antibody-Y10b-Flow-Intracellular-NB100-662-img0008.jpg)
![Flow (Intracellular): rRNA Antibody (Y10b) [NB100-662] - An intracellular stain was performed on A549 cells with NB100-662AF488 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeablized with 0.1% saponin. Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 488.](http://images.novusbio.com/fullsize/rRNA-Antibody-Y10b-Flow-Intracellular-NB100-662-img0011.jpg)
![Flow (Intracellular): rRNA Antibody (Y10b) [NB100-662] - An intracellular stain was performed on SH-SY5Y cells with rRNA (Y10b) antibody NB100-662AF647 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeablized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 647.](http://images.novusbio.com/fullsize/rRNA-Antibody-Y10b-Flow-Intracellular-NB100-662-img0012.jpg)
![CyTOF-reported: rRNA Antibody (Y10b) [NB100-662] - Human bone marrow after RBC lysis, stained with anti-CD16, fixed, permeabilized with methanol, stained with anti-lactoferrin 1C6 NB120-10109 and anti-rRNA Y10b NB100-662, and gated on myeloid cells per Nat Med. 2020. 26:408-417. CyTOF image submitted by a verified customer review.](http://images.novusbio.com/fullsize/rRNA-Antibody-Y10b-CyTOF-reported-NB100-662-img0014.jpg)
![Immunocytochemistry/Immunofluorescence: Histone H3 [Citrulline 2, Citrulline 8, Citrulline 17] Antibody [NB100-57135] - HL60 cells treated with DMSO and Calcimycin Green: (at 1:1000 Blue Hoechst)](http://images.novusbio.com/fullsize/Histone-H3-Antibody-Immunocytochemistry-Immunofluorescence-NB100-57135-img0004.jpg "<b>Biological Strategies Validation. </b>Immunocytochemistry/Immunofluorescence: Histone H3 [Citrulline 2, Citrulline 8, Citrulline 17] Antibody [NB100-57135] - HL60 cells treated with DMSO and Calcimycin Green: (at 1:1000 Blue Hoechst)")
![<b>Biological Strategies Validation. </b>Western Blot: Histone H3 [Citrulline 2, Citrulline 8, Citrulline 17] Antibody [NB100-57135] - Histone H3/Citrulline (R2,R8,R17) at 1:10000 dilution. Observed molecular weight is ~15 kDa.](http://images.novusbio.com/fullsize/Histone-H3-[Citrulline-2-Citrulline-8-Citrulline-17]-Antibody-Western-Blot-NB100-57135-img0003.jpg)
![Immunohistochemistry: Rabbit Polyclonal Histone H3 [Citrulline Arg17, Citrulline Arg2, Citrulline Arg8] Antibody [NB100-57135] - Analysis of Histone H3 on mouse brain tissue. Nucleus (Blue, DAPI) ; H3cit (green). Hemorrhagic stroke model FxFr ; 10 µm thickness 1:400 Secondary antibody AF488. Image from a verified customer review.](http://images.novusbio.com/fullsize/antibody/nb100-57135_rabbit-polyclonal-histone-h3-antibody-immunohistochemistry-20320259417..png)
![Immunocytochemistry/ Immunofluorescence: Clostridium Difficile Toxin A Antibody (PCG4.1) - BSA Free [NB600-1066] - PACSIN2 is required for TcdA uptake & toxin-induced rounding in wildtype MEF cells. (C), (D) & (E). Depletion of PACSIN2 reduces TcdA uptake in MEF cells. Wildtype MEF cells expressing luciferase (luc) or PACSIN2 siRNA incubated with 50 nM TcdA-546 at 10°C for 45 min. Cells allowed to warm up to 37°C for 2 min & then washed to remove unbound toxins & incubated with fresh media prewarmed to 37°C. Bound toxins allowed to internalize for 9 min at 37°C. Cells then fixed, stained for PACSIN2 & imaged by confocal microscopy. PACSIN2 & TcdA-546 staining from each condition shown in (C). Scale bars, 10 μm. The images shown representative of multiple fields imaged from two independent experiments. (D) Comparison of mean fluorescence intensities of PACSIN2 between luc & PACSIN2 siRNA transfected cells. Data represent mean & SD of 101 individual cells. Student’s t test ***p<0.0001. (E) Comparison of mean fluorescence intensities of TcdA-546 between luc & PACSIN2 siRNA transfected cells. Data represent mean & SD of 101 individual cells. Student’s t test ***p<0.0001. Cells chosen at random for intensity analyses. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.ppat.1006070), licensed under a CC0-1.0 license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1066_mouse-monoclonal-clostridium-difficile-toxin-a-antibody-pcg4-1-310202416173511.jpg)
![Immunocytochemistry/ Immunofluorescence: Clostridium Difficile Toxin A Antibody (PCG4.1) - BSA Free [NB600-1066] - TcdA colocalizes with PACSIN2 in wildtype MEF cells.(A) Wildtype MEFs on glass coverslips were allowed to bind 50 nM TcdA-546 for 45 min at 10°C, & cells were shifted to 37°C to allow internalization of toxin for 3 min. Cells were fixed, stained for PACSIN2, & analyzed by confocal microscopy. Merged images show PACSIN2 in red, toxin in green, & colocalization in yellow. Scale bars, 10 μm. The images shown are representative of multiple fields imaged from two independent experiments. (B) Immunofluorescence assays were performed as described in (A), but cells were stained for cav1 in addition to PACSIN2. Merged images show PACSIN2 in red, toxin in green, & cav1 in blue. Yellow puncta in merged images denote TcdA- & PACSIN2-positive structures. Pink punta denote caveolae-associated PACSIN2. Scale bars, 10 μm. (C) Pearson’s correlation coefficient to assess the extent of colocalization between PACSIN2, cav1 & TcdA-546 after 3 min toxin uptake. Data represent mean & SD of 31 individual cells chosen at random. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.ppat.1006070), licensed under a CC0-1.0 license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1066_mouse-monoclonal-clostridium-difficile-toxin-a-antibody-pcg4-1-310202416182624.jpg)
![Immunocytochemistry/ Immunofluorescence: Clostridium Difficile Toxin A Antibody (PCG4.1) - BSA Free [NB600-1066] - TcdA colocalizes with PACSIN2 in wildtype MEF cells.(A) Wildtype MEFs on glass coverslips were allowed to bind 50 nM TcdA-546 for 45 min at 10°C, & cells were shifted to 37°C to allow internalization of toxin for 3 min. Cells were fixed, stained for PACSIN2, & analyzed by confocal microscopy. Merged images show PACSIN2 in red, toxin in green, & colocalization in yellow. Scale bars, 10 μm. The images shown are representative of multiple fields imaged from two independent experiments. (B) Immunofluorescence assays were performed as described in (A), but cells were stained for cav1 in addition to PACSIN2. Merged images show PACSIN2 in red, toxin in green, & cav1 in blue. Yellow puncta in merged images denote TcdA- & PACSIN2-positive structures. Pink punta denote caveolae-associated PACSIN2. Scale bars, 10 μm. (C) Pearson’s correlation coefficient to assess the extent of colocalization between PACSIN2, cav1 & TcdA-546 after 3 min toxin uptake. Data represent mean & SD of 31 individual cells chosen at random. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.ppat.1006070), licensed under a CC0-1.0 license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1066_mouse-monoclonal-clostridium-difficile-toxin-a-antibody-pcg4-1-310202416175252.jpg)
![Western Blot: Rad51 Antibody [H00005888-B01P] - Analysis of RAD51 expression in human colon.](http://images.novusbio.com/fullsize/Rad51-Antibody-Western-Blot-H00005888-B01P-img0015.jpg "Western Blot: Rad51 Antibody [H00005888-B01P] - Analysis of RAD51 expression in human colon.")
![Immunocytochemistry/Immunofluorescence: Rad51 Antibody [H00005888-B01P] - Immunofluorescence of purified MaxPab antibody to RAD51 on HeLa cell. [antibody concentration 10 ug/ml]](http://images.novusbio.com/fullsize/Rad51-Antibody-Immunocytochemistry-Immunofluorescence-H00005888-B01P-img0008.jpg)
![Immunohistochemistry-Paraffin: Rad51 Antibody [H00005888-B01P] - Analysis of purified antibody to RAD51 on formalin-fixed paraffin-embedded human testis. (antibody concentration 3 ug/ml)](http://images.novusbio.com/fullsize/Rad51-Antibody-Immunohistochemistry-Paraffin-H00005888-B01P-img0010.jpg)
![Western Blot: Rad51 Antibody [H00005888-B01P] - expression in transfected 293T cell line. Lane 1: RAD51 transfected lysate(37.29 KDa). Lane 2: Non-transfected lysate.](http://images.novusbio.com/fullsize/Rad51-Antibody-Western-Blot-H00005888-B01P-img0009.jpg)
![Western Blot: Rad51 Antibody [H00005888-B01P] - Analysis of RAD51 expression in PC-12.](http://images.novusbio.com/fullsize/Rad51-Antibody-Western-Blot-H00005888-B01P-img0011.jpg)
![Western Blot: Rad51 Antibody [H00005888-B01P] - Analysis of RAD51 expression in Raw 264.7.](http://images.novusbio.com/fullsize/Rad51-Antibody-Western-Blot-H00005888-B01P-img0012.jpg)
![Western Blot: Rad51 Antibody [H00005888-B01P] - Analysis of RAD51 expression in Jurkat.](http://images.novusbio.com/fullsize/Rad51-Antibody-Western-Blot-H00005888-B01P-img0013.jpg)
![Western Blot: Rad51 Antibody [H00005888-B01P] - Analysis of RAD51 expression in NIH/3T3.](http://images.novusbio.com/fullsize/Rad51-Antibody-Western-Blot-H00005888-B01P-img0014.jpg)
![Western Blot: Rad51 Antibody [H00005888-B01P] - Analysis of RAD51 expression in transfected 293T cell line by RAD51 polyclonal antibody. Lane 1: RAD51 transfected lysate(37.29 KDa). Lane 2: Non-transfected lysate.](http://images.novusbio.com/fullsize/Rad51-Antibody-Western-Blot-H00005888-B01P-img0016.jpg)
![Western Blot: ARF5 Antibody (1B4) [H00000381-M01] - Analysis of ARF5 expression in transfected 293T cell line by ARF5 monoclonal antibody (M01), clone 1B4.Lane 1: ARF5 transfected lysate(20.5 KDa).Lane 2: Non-transfected lysate.](http://images.novusbio.com/fullsize/ARF5-Antibody-1B4-Western-Blot-H00000381-M01-img0015.jpg "Western Blot: ARF5 Antibody (1B4) [H00000381-M01] - Analysis of ARF5 expression in transfected 293T cell line by ARF5 monoclonal antibody (M01), clone 1B4.Lane 1: ARF5 transfected lysate(20.5 KDa).Lane 2: Non-transfected lysate.")
![Immunocytochemistry/Immunofluorescence: ARF5 Antibody (1B4) [H00000381-M01] - Analysis of monoclonal antibody to ARF5 on HeLa cell. Antibody concentration 15 ug/ml.](http://images.novusbio.com/fullsize/ARF5-Antibody-1B4-Immunocytochemistry-Immunofluorescence-H00000381-M01-img0009.jpg)
![Western Blot: ARF5 Antibody (1B4) [H00000381-M01] - ARF5 monoclonal antibody (M01), clone 1B4. Analysis of ARF5 expression in HeLa.](http://images.novusbio.com/fullsize/ARF5-Antibody-1B4-Western-Blot-H00000381-M01-img0011.jpg)
![Western Blot: ARF5 Antibody (1B4) [H00000381-M01] - ARF5 monoclonal antibody (M01), clone 1B4. Analysis of ARF5 expression in PC-12.](http://images.novusbio.com/fullsize/ARF5-Antibody-1B4-Western-Blot-H00000381-M01-img0012.jpg)
![Western Blot: ARF5 Antibody (1B4) [H00000381-M01] - ARF5 monoclonal antibody (M01), clone 1B4. Analysis of ARF5 expression in Raw 264.7.](http://images.novusbio.com/fullsize/ARF5-Antibody-1B4-Western-Blot-H00000381-M01-img0013.jpg)
![Western Blot: ARF5 Antibody (1B4) [H00000381-M01] - ARF5 monoclonal antibody (M01), clone 1B4 Analysis of ARF5 expression in A-431.](http://images.novusbio.com/fullsize/ARF5-Antibody-1B4-Western-Blot-H00000381-M01-img0014.jpg)
![ELISA: ARF5 Antibody (1B4) [H00000381-M01] - Detection limit for recombinant GST tagged ARF5 is approximately 0.3ng/ml as a capture antibody.](http://images.novusbio.com/fullsize/ARF5-Antibody-1B4-ELISA-H00000381-M01-img0010.jpg)