| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB600-1384SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | BC100-494SS | |||
| 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 | |||
| Conjugate | Catalog # | Availability | Size | Price |
|---|---|---|---|---|
| Atto594 | NBP3-14765-100ug | |||
| Conjugate | Catalog # | Availability | Size | Price |
|---|---|---|---|---|
| Atto488 | NBP3-14785-100ug | |||
![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: PINK1 Antibody - BSA Free [BC100-494] - PPM1H does not dephosphorylate Ser111 of Rab8A or key phosphorylation sites of AMPK & Akt signaling pathways.(A) HEK293 cells were transiently transfected with constructs expressing the indicated components. 24 hr post-transfection, cells were treated ±10 µM CCCP (Carbonyl cyanide m-chlorophenyl hydrazine) for 3 hr to induce activation of the PINK1 kinase & trigger Rab8A phosphorylation at Ser111 (Lai et al., 2015). (B) As in (A) except cells were immunoblotted with the indicated antibodies that recognize key phosphorylation sites of AMPK & Akt signaling pathways. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31663853), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-31020241534312.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - PINK1 & Parkin are phosphorylated after a decrease in delta Ψm in mouse primary neurons. Neurons were infected with lentivirus encoding PINK1-Flag (A), wild-type HA-Parkin (B) or HA-Parkin with either the S65A or S65E mutation (C). Cells were treated with the mitochondrial uncoupler CCCP (30 μm) for 1–3 h & subjected to SDS-PAGE in the absence or presence of 50 μm phos-tag. Note that mobility does not reflect the molecular weight of proteins in phos-tag PAGE (Kinoshita et al. 15), & thus, molecular weight markers are not shown in the bottom gels. The red & black asterisks in (C) indicate phosphorylation of Parkin at Ser65 & an additional minor phosphorylation site, respectively. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23751051), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415384188.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - PINK1 translation is critical for the accumulation of PINK1 upon mitochondrial damage. aPINK1 mRNA levels were not altered by mitochondrial damage. HeLa cells were incubated with 10 μM CCCP or combination of 10 μM oligomycin & 4 μM antimycin for 2 h & then, PINK1 mRNA levels were measured by qRT-PCR. PINK1 mRNA level was normalized to the corresponding GAPDH levels & quantified as a percentage of control (n = 8, t-test). b, c Translation is involved in PINK1 accumulation upon CCCP treatment. HeLa cells were first pre-incubated with 100 μM cycloheximide (CHX) for 2 h & then washed. Cells were further incubated with 10 μM CCCP with or without CHX for 2 h (n = 4, two-way ANOVA). Values are mean ± SEM (n.s. = non-significant, ***p 1000 cells) & are shown as a percentage of control. Values are mean ± SEM (*p < 0.05, **p < 0.01, ***p < 0.001) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27456084), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415483619.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - Inhibition of endogenous miR-27a/b function increases human PINK1 expression. a Schematic diagram of sequence alignment of miR-27a/b & anti-miR-27a/b. Asterisks (*) indicate conserved nucleotides. b Inhibition of endogenous miR-27a/b function increased luciferase activities in HeLa cells. Cells were transfected with the reporter constructs containing the full-length 3′UTR of human PINK1 mRNA with wild-type (WT) or mutated (Mut) seed match sites downstream of Renilla luciferase gene. 48 h post-transfection, luciferase activities were measured (n = 4, t-test). c-f Inhibition of endogenous miR-27a/b increased PINK1 protein levels in HeLa (C-D) & M17 cells (E-F). Cells were transfected with 150 nM of anti-miR-27a/b or anti-control (anti-Ctl). 48 h post-transfection, cells were harvested for Western blot. PINK1 protein level was normalized to corresponding GAPDH level & quantified as a percentage of control (n = 4, t-test). Data are shown as a percentage of control. Values are mean ± SEM (n.s. = non-significant, **p < 0.01, ***p < 0.00) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27456084), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415482287.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - Regulation of PINK1 by miRNA. a Schematic diagram of AGO-specific RNA immunoprecipitation assay. b, cPINK1 mRNAs are associated with miRNA/RISC complex. HeLa cells were transfected with 50 nM of AGO2 siRNA or negative control. 48 h post-transfection, AGO2-bound mRNAs were pulled down from cell lysates with 2A8 anti-AGO2 antibody or non-specific IgG antibody. PINK1 mRNA levels were then measured by qRT-PCR. siRNA against AGO2 served as a quality control for AGO-specific RNA immunoprecipitation assay. PINK1 mRNA levels were quantified as a percentage of group 1 (n = 6, two-way ANOVA). d, e Knock-down of DICER1 increased PINK1 protein levels. HeLa cells were transfected with 50 nM DICER1 siRNA (DICER1 KD) or negative control (Ctl). 48 h post-transfection, cells were harvested for Western blot. The arrowhead indicates a full-length PINK1 band & the asterisk indicates a non-specific band. Each protein level was normalized to corresponding GAPDH level & quantified as a percentage of control (n = 4, t-test). Values are mean ± SEM (n.s. = non-significant, **p < 0.01, ***p < 0.001) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27456084), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415482296.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - The expression levels of microtubule protein light chain 3 (LC3B), PTEN inducing putative kinase 1 (PINK1), Parkin, mitofusin 1 (Mfn1), toll-like receptor (TLR) 9, cytochrome c oxidase 4 (COX4), myeloid differentiation factor 88 (MyD88), & nuclear factor (NF)-kappa B in lung tissues from animals with spontaneous breathing (CON) or mechanical ventilation at high tidal volume (HTV) with saline, antimycin A (AmA) or cyclosporine A (CsA). (A) Levels of PINK1, Parkin, & Mfn1 mRNA. (B) Levels of LC3B, PINK1, Parkin, & Mfn1 protein by Western blot. (C) Relative expression of LC3B-II/LC3B-I & PINK1 protein. (D) Relative expression of Parkin & Mfn1 protein. (E) Levels of TLR9 & COX4 mRNA. (F) Levels of MyD88 & nuclear factor-kappa B (NF-kappa B) mRNA. (G) Levels of TLR9, COX4, MyD88, & NF-kappa B protein by Western blot. (H) Relative expression of TLR9 & COX4 protein. (I) Relative expression of MyD88 & NF-kappa B protein. Fold expression for target genes was normalized to that measured for the beta -actin gene. Both of these experiments were in triplicate. aP < 0.05 vs. CON group;bP < 0.05 vs. HTV group; & cP < 0.05 vs. AmA group. Image collected & cropped by CiteAb from the following publication (//www.frontiersin.org/article/10.3389/fimmu.2018.01477/full), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415485118.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - Mitophagy contributes to removal of excess mitochondrial fragments in preeclampsia.(a, left panel) Representative TEM image of a cytotrophoblast from PTC & PE placenta collected at 29 weeks. Mitochondrial proximity to ER (MAM) is indicated by white arrows, mitochondrial fission events are depicted by white stars (scale bar: 500 nm; n = 8 separate PE placentae). (a, right panel) percentage of mitochondrial tethering to the ER in in PE vs. PTC (PE placentae, n = 8; PTC placentae, n = 7; unpaired Student’s t-test *P < 0.05). b Representative western blots for MFN2 & calreticulin in ER isolated from PE & PTC placentae (PE & PTC, n = 3 separate samples). c WB & associated densitometry of ASAH2 (normalized to TOM20) in mitochondria from PTC & PE placentae. d Representative TEM depicting mitophagy (white arrow) in cytotrophoblast cell from PE placenta (scale bar: 500 nm, n = 8 separate PE placentae). e Western blot & associated densitometry of PINK1 & Parkin in PE vs. PTC mitochondrial isolates. Densitometry for PINK1 blot was used to calculate the ratio of full-length PINK63kDa to cleaved PINK153kDa (PE & PTC, n = 4 separate placentae, *P < 0.05) Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41419-018-0360-0), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415482279.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - Deficiency or mutant PINK1 reduces phosphorylation of LETM1 at Thr192. a, b Proteins extracted from PINK1 WT or KO MEFs (a) or mouse brain (b) were subjected to IP with anti-LETM1, probed with pT192 & reprobed with anti-LETM1 by WB. c Proteins extracted from human fibroblast of control (Con) or a PINK1-Q456X patient (Q456X) were subjected to IP with anti-LETM1, probed with pT192 & reprobed with anti-LETM1 by WB. d HEK293 cells were transfected with Adtrack GFP control, AdPINK1-WT, & AdPINK1-Q456X mutant for 1 day. Endogenous LETM1 protein was isolated by IP with anti-LETM1, probed with pT192 & reprobed with anti-LETM1 by WB. e SH-SY5Y cells were treated with 25 µM rotenone for 8 or 16 h. Total cell lysates were either analyzed by WB with anti-PINK1, or subjected to IP with anti-LETM1, probed with pT192 & reprobed with anti-LETM1 antibodies by WB. All above experiments were replicated three times, respectively Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29123128), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415482299.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - Polyphyllin I suppressed, & PINK1 knockdown further suppressed, tumor growth in a MDA-MB-231 xenograft modelA. Tumor volumes were measured every week & differed at the end of the treatment period (*P < 0.01 compared to shCon cells treated with PPI, ##P< 0.01 compared to shPINK1 cells treated with PPI). B. Representative image of tumors from each group. C. Body weight changes in mice during the 6 weeks of PPI treatment. There were no differences in body weights between the PPI-treated shCon & vehicle-treated shCon groups or between the PPI-treated shPINK1 group & shCon groups. D. Representative tumor tissues were sectioned & subjected to H&E staining, TUNEL assay, & immunohistochemistry staining for C-CASP3. Scale bars: 50 μm. E. Representative tumor tissues from each group were prepared & subjected to western blot using anti-DRP1, -PARK2, -LC3B, -PINK1, & -C-CASP3 antibodies. Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.14413), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415483648.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - Corticosterone affects NIX-dependent mitophagy through decreasing PGC1 alpha in vivo.a–f Mice exposed to vehicle, corticosterone (10 mg/kg), corticosterone w/ phorbol 12-myristate 13-acetate (PMA pretreatment, 200 μg/kg), or PMA alone for 7 days. a Slide samples for IHC immunostained w/ LAMP1 (green), TOMM20 (red), & DAPI (blue). Scale bars, 100 μm (magnification, ×200). n = 5. b The expressions of NIX, PTEN-induced kinase 1 (PINK1), & BCL2 interacting protein 3 (BNIP3) detected w/ WB where beta -actin used as a loading control. n = 5. c Slide samples for IHC immunostained w/ synpatophysin (green), PSD95 (red), & DAPI (blue). Scale bars, 100 μm (magnification, ×200). n = 5. d Synaptophysin & PSD95 detected by WB. Loading control is beta -actin. n = 5. e The mice subjected to Y-maze test to evaluate spatial memory function. n = 6. f The mice subjected to forced swim test to evaluate depression-like behavior. n = 5. g Vehicle or RU 486 (5 mg/kg) injected mice presented w//w/out corticosterone (10 mg/kg) for 3 days. The expressions of peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC1 alpha ) & NIX visualized via WB. Loading control is beta -actin. n = 5. h The schematic model for mechanisms of inhibition in NIX-dependent mitophagy by glucocorticoid shown. All blots & IF images representative. n = 5 or 6 from each animal w/ two technical replicates each in results of IHC & WB. Quantitative data presented as a mean ± S.E.M. The representative images acquired by SRRF imaging system. Two-sided two-way ANOVA conducted except Fig. 8b, data of which analyzed by two-sided unpaired student’s t test. ** indicates p < 0.01 versus control & ## indicates p < 0.01 versus corticosterone, respectively. Data provided as a Source data file. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33473105), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415482218.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - G-TPP activity is conserved in primary fibroblasts(A, C) Fibroblasts were treated with 15 µM G-TPP for the indicated time points. Cells were harvested & western blots were probed with antibodies against (A) PINK1, pS65-Ub & total Ub or (C) autophagy adapter proteins. GAPDH & Vinculin served as loading control. G-TPP treatment led to PINK1 stabilization & pS65-Ub induction in primary skin fibroblasts. p62 levels were induced upon G-TPP treatment, while other adapters seemed decreased. (B, D) Human fibroblasts were treated with 15 µM G-TPP for 16 h & fixed & stained with antibodies against (B) pS65-Ub (green) or (D) the autophagy adapters NBR1, NDP52, p62, OPTN & TAX1BP1 (green). Mitochondria were stained with antibodies against TOM20 (red), nuclei were visualized with Hoechst (blue). Scale bars indicate 10 µM. A magnified image of the boxed region, the fluorescence profile along the arrow & the Pearson’s correlation coefficient of adapter protein & mitochondrial stainingare shown to the right. Shown is the mean ± SEM of at least five randomly selected images (unpaired, two-sided t-test, ***p < 0.0005). Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.22287), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415482286.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - Polyphyllin I triggers PINK1/PARK2-dependent mitophagyA. MDA-MB-231 cells were treated with 8 μM PPI for different periods of time as indicated, & PARK2, P62, & ubiquitin (UB) levels in mitochondrial fractions were determined by western blot. B. Cells were cotransfected with GFP-UB & RFP-mito & treated with 8 μM PPI for 9 h, after which PARK2 (Alexa Fluor 405, pink) & P62 (Alexa Fluor 647, blue) immunostaining was detected using confocal microscopy. C. Cells cotransfected with GFP-UB & RFP-LC3 were treated with 8 μM PPI for 9 h, after which PARK2 (Alexa Fluor 405, pink) & TOMM20 (Alexa Fluor 647, blue) immunostaining was detected using confocal microscopy. Scale bars: 10 μm. D-E. MDA-MB-231 cells were treated with 8 μM PPI for different periods of time as indicated; whole-cell lysates were then separated on 8% SDS-PAGE gels & analyzed by western blot using the anti-PINK1 antibody. Relative full-length (∼63 kDa) & cleaved (∼52 kDa) PINK1 levels were quantified by densitometry & normalized to Tubulin. The results were expressed as a percentage of control, which was set at 100%. Data are presented as mean ± SD (*P< 0.01 vs. the control). F. Cells were treated with 8 μM PPI for different periods of time as indicated, & whole-cell lysates were then subjected to western blot analysis. G. Cells were treated with 8 μM PPI for 9 h, after which mitochondrial fractions were prepared & subjected to immunoprecipitation using anti-PINK1 antibody; associated PARK2 was detected using immunoblotting. H. RFP-mito-expressing MDA-MB-231 cells were treated with 8 μM PPI for 9 h, & PINK1 (Alexa Fluor 488, green) & PARK2 (Alexa Fluor 405, pink) immunostaining were evaluated using confocal microscopy. Scale bars: 10 μm. Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.14413), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415482214.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - miR-27a/b suppress human PINK1 expression. a Schematic diagram of the conserved target sites of miR-27a/b in the 3′UTR of human PINK1 mRNA. Seed sequences were indicated in red. Asterisks (*) indicate the conserved nucleotides. b Schematic diagram of the luciferase reporter plasmids. The reporter constructs contain the full-length 3′UTR of human PINK1 mRNA with wild-type (WT) or mutated (Mut) seed match sites downstream of Renilla luciferase gene. c Overexpression of miR-27a/b decreased luciferase activities in HeLa cells. Cells were transfected with miR-27a/b or negative control (Ctl) along with reporter constructs as indicated. 48 h post-transfection, luciferase activities were measured (n = 4, one-way ANOVA). Renilla luciferase activity was normalized to the corresponding firefly luciferase activity. d-g Overexpression of miR-27a/b decreased PINK1 protein levels in HeLa (D-E) & M17 cells (F-G). Cells were transfected with miR-27a/b or negative control (Ctl). 48 h post-transfection, cells were harvested for Western blot (n = 4, t-test). PINK1 protein level was normalized to corresponding GAPDH level & quantified as a percentage of control. Data are shown as a percentage of control. Values are mean ± SEM (n.s. = non-significant, **p < 0.01, ***p < 0.001) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27456084), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415483618.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - Increased p62 expression is prevented in PINK1 knock‐down cells. (a) SH‐SY5Y cells expressing scrambled shRNA or PINK1 shRNA (117‐2, 118‐3, & 118‐4) were treated with 10 μM carbonyl cyanide m‐chlorophenylhydrazone (CCCP) for 24 h & full‐length (FL) PINK1 protein levels measured by western blot. No accumulation of FL PINK1 was observed in 118‐3 & 118‐4 PINK1 shRNA clones. (b) SH‐SY5Y cells constitutively expressing scrambled (scram) or PINK1 shRNA (clone 118‐3) were treated with vehicle or 10 μM CCCP for 24 h & p62 protein expression measured by western blotting. **p < 0.05 versus scram CCCP; n = 9. (c) SH‐SY5Y cells were incubated in serum‐free culture media for up to 24 h to induce starvation‐mediated macroautophagy. p62 protein levels were measured by western blotting. *p < 0.05 versus 0 h; **p < 0.01 versus 0 h; n = 4. (d) SH‐SY5Y cells were transfected with scrambled (scram) or p62 siRNA for 72 h. For the last 24 h, cells were treated with vehicle (ethanol) or 10 μM CCCP. p62 protein expression was then measured by western blotting. p62 protein was significantly decreased in p62 siRNA cells under basal conditions & following CCCP treatment, when compared to scram cells. **p < 0.01 versus scram vehicle or scram CCCP; n = 3. (e) Mitochondrial content was measured in SH‐SY5Y cells treated with scram or p62 siRNA for 72 h by measuring citrate synthase (CS) activity. For the last 24 h, cells were treated with vehicle or 10 μM CCCP & data are expressed as % of vehicle. *p < 0.05 versus scram CCCP treatment; n = 5. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26509433), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415482278.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - NF kappa B upregulates human PINK1 gene expression. (A) NF kappa B increases the endogenous human PINK1 mRNA level. HEK293 cells were transfected with either the NF kappa B expression vector or empty vector pMTF. RT-PCRs were performed using either primers specific to the human PINK1 coding sequence or the human beta -actin coding sequence. (B) NF kappa B increases the endogenous human PINK1 protein levels. HEK293 cells transfected with NF kappa B were harvested 48 h after transfection for protein detection. Cell lysates were run on 10% glycine gel & images were collected by Licor. A significant increase of endogenous PINK1 was observed. (C) The endogenous human PINK1 protein level was dramatically increased by NF kappa B in SH-SY5Y cells. SH-SY5Y cells were transfected with NF kappa B p65 plasmids or the control vector pMTF & then harvested for protein detections. The human PINK1 protein & its proteolysis products ∆1-PINK1 (55kD) & ∆2-PINK1 (45kD) were all increased. beta -actin acted as the internal control. (D) LPS treatment facilitated PINK1 expression in SH-SY5Y cells. Cells were harvested after being treated for 16 h & then subjected to Western blot. The human beta -actin level was served as a control. Quantification was performed by Image J software. Values indicate means ± SEM. n = 3, *p <0.01 by Student’s t-test. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25108683), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415485116.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - G-TPP induces PINK1 stabilization & kinase activity in HeLa cells(A) G-TPP treatment leads to PINK1 stabilization & pS65-Ub induction in HeLa cells. HeLa cells stably expressing untagged Parkin were treated with 10 µM G-TPP for the indicated times. Western blots were prepared with cell lysates & probed with antibodies against PINK1 & pS65-Ub. GAPDH served as a loading control. (B) pS65-Ub is induced in G-TPP treated cells & co-localizes with EGFP-Parkin & mitochondria. HeLa cells stably expressing EGFP-Parkin (green) were treated with 10 µM G-TPP for the indicated times & fixed. Cells were stained with antibodies against pS65-Ub (red) & the mitochondrial marker TOM20 (cyan). Scale bars correspond to 10 µM. (C) Quantification of Parkin translocation using High Content Imaging. HeLa EGFP-Parkin cells were treated for 4 or 8 h with or without 10 µM G-TPP. CCCP treatment (10 µM for 2 h) was used as a positive control. Cells were fixed, counterstained with Hoechst dye to visualize nuclei, imaged & analyzed using the ratio of cytoplasmic to nuclear EGFP signal [21]. Data was normalized to positive (2 h 10 µM CCCP treatment) & negative (2 h DMSO) controls. G-TPP significantly induced Parkin re-localization to levels similar to or beyond 2 h CCCP treatment. Shown are the mean values of three independent experiments with triplicate wells each ± SEM (one-way ANOVA with Tukey’s posthoc, ***p < 0.0005). Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.22287), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-31020241548369.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - NF kappa B upregulates human PINK1 gene expression. (A) NF kappa B increases the endogenous human PINK1 mRNA level. HEK293 cells were transfected with either the NF kappa B expression vector or empty vector pMTF. RT-PCRs were performed using either primers specific to the human PINK1 coding sequence or the human beta -actin coding sequence. (B) NF kappa B increases the endogenous human PINK1 protein levels. HEK293 cells transfected with NF kappa B were harvested 48 h after transfection for protein detection. Cell lysates were run on 10% glycine gel & images were collected by Licor. A significant increase of endogenous PINK1 was observed. (C) The endogenous human PINK1 protein level was dramatically increased by NF kappa B in SH-SY5Y cells. SH-SY5Y cells were transfected with NF kappa B p65 plasmids or the control vector pMTF & then harvested for protein detections. The human PINK1 protein & its proteolysis products ∆1-PINK1 (55kD) & ∆2-PINK1 (45kD) were all increased. beta -actin acted as the internal control. (D) LPS treatment facilitated PINK1 expression in SH-SY5Y cells. Cells were harvested after being treated for 16 h & then subjected to Western blot. The human beta -actin level was served as a control. Quantification was performed by Image J software. Values indicate means ± SEM. n = 3, *p <0.01 by Student’s t-test. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25108683), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415482277.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - NF kappa B upregulates human PINK1 gene expression. (A) NF kappa B increases the endogenous human PINK1 mRNA level. HEK293 cells were transfected with either the NF kappa B expression vector or empty vector pMTF. RT-PCRs were performed using either primers specific to the human PINK1 coding sequence or the human beta -actin coding sequence. (B) NF kappa B increases the endogenous human PINK1 protein levels. HEK293 cells transfected with NF kappa B were harvested 48 h after transfection for protein detection. Cell lysates were run on 10% glycine gel & images were collected by Licor. A significant increase of endogenous PINK1 was observed. (C) The endogenous human PINK1 protein level was dramatically increased by NF kappa B in SH-SY5Y cells. SH-SY5Y cells were transfected with NF kappa B p65 plasmids or the control vector pMTF & then harvested for protein detections. The human PINK1 protein & its proteolysis products ∆1-PINK1 (55kD) & ∆2-PINK1 (45kD) were all increased. beta -actin acted as the internal control. (D) LPS treatment facilitated PINK1 expression in SH-SY5Y cells. Cells were harvested after being treated for 16 h & then subjected to Western blot. The human beta -actin level was served as a control. Quantification was performed by Image J software. Values indicate means ± SEM. n = 3, *p <0.01 by Student’s t-test. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25108683), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-31020241548363.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - G-TPP leads to recruitment of autophagy adapters & degradation of mitochondria(A) HeLa cells stably expressing untagged Parkin were treated with 10 µM G-TPP for 8 h. Western blots were prepared from cell lysates & probed with antibodies against LC3, phospho-TBK1 (Ser172) & TBK1. GAPDH was used as a loading control. Upon 8 h the levels of LC3-I & LC3-II were both increased. At 8 h after treatment with G-TPP but not at 4 or 24 h, TBK1 was phosphorylated. (B) HeLa cells stably expressing EGFP-Parkin were treated with 10 µM G-TPP & fixed 8 h after treatment. Cells were stained with antibodies against the autophagy adapter proteins NBR1, NDP52, OPTN, p62, & TAX1BP1 (red). Mitochondria were counterstained with TOM20 antibodies (cyan), nuclei with Hoechst (blue). EGFP-Parkin epifluorescence is shown in green. Scale bar corresponds to 10 µM. (C) HeLa cells stably expressing EGFP-Parkin & the reporter protein mitoKeima were treated with 10 µM CCCP or G-TPP & imaged over time. The ratio of ‘neutral’ mitoKeima to ‘acidic’ mitoKeima was calculated as readout for mitophagy. Parkin translocation was monitored at the same time. Values for Parkin translocation & mitophagy were normalized to 12 h treatment with 10 µM CCCP as positive control & DMSO as negative control (two-way ANOVA with Tukey’s post-hoc test, **p < 0.005, ***p < 0.0005). Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.22287), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415482225.jpg)
![Western Blot: Rabbit Polyclonal PINK1 Antibody [BC100-494] - PINK1 detection in mouse and postmortem human cortex samples. 1:1000 dilution at 4 degrees overnight to detect endogenous PINK1 from mouse and postmortem human cortex samples (10 ug total protein). Image from a verified customer review.](http://images.novusbio.com/fullsize/antibody/bc100-494_rabbit-polyclonal-pink1-antibody-western-blot-231202510057..jpg)
![Western Blot: FPRL1/FPR2 Antibody - BSA Free [NLS1878] - Immunoblot of FPR2 protein in various parts of the rat brain including olfactory bulb (OB), prefrontal cortex (PFC), primary somatosensory cortex (CTX1), parietal association cortex and secondary auditory cortex (CTX2), striatum (STR), thalamus and hypothalamus (THA), hippocampus (HPC), cerebellum (CB), brainstem (BS), cervical spinal cord [SC(C)], thoracic spinal cord [SC(T)], and lumbar spinal cord [SC(L)]. Blots incubated with antigen-absorbed antibody i. e. peptide competition, show reduced band intensities. Image collected and cropped by Citeab from the following publication (Localisation of Formyl-Peptide Receptor 2 in the Rat Central Nervous System and Its Role in Axonal and Dendritic Outgrowth. Neurochem Res (2018)) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/FPRL1-FPR2-Antibody---BSA-Free-Western-Blot-NLS1878-img0012.jpg "Western Blot: FPRL1/FPR2 Antibody - BSA Free [NLS1878] - Immunoblot of FPR2 protein in various parts of the rat brain including olfactory bulb (OB), prefrontal cortex (PFC), primary somatosensory cortex (CTX1), parietal association cortex and secondary auditory cortex (CTX2), striatum (STR), thalamus and hypothalamus (THA), hippocampus (HPC), cerebellum (CB), brainstem (BS), cervical spinal cord [SC(C)], thoracic spinal cord [SC(T)], and lumbar spinal cord [SC(L)]. Blots incubated with antigen-absorbed antibody i. e. peptide competition, show reduced band intensities. Image collected and cropped by Citeab from the following publication (Localisation of Formyl-Peptide Receptor 2 in the Rat Central Nervous System and Its Role in Axonal and Dendritic Outgrowth. Neurochem Res (2018)) licensed under a CC-BY license.")
![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)
![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)
![<b>Biological Strategies Validation. </b>Western Blot: FPRL1/FPR2 Antibody - BSA Free [NLS1878] - Murine neutrophils were extracted from the bone marrow of C57BL/6 mice and exposed to normal glucose (90 mg/dl) or high glucose (300 mg/dl) and the expression of FPR2 was assessed by western blotting after 1, 2, or 3 hr exposure to glucose. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35112667/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/FPRL1-FPR2 Antibody - BSA Free-Western Blot-NLS1878-img0013.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)
![Electron Microscopy: FPRL1/FPR2 Antibody - BSA Free [NLS1878] - Electron micrographs of FPR2 immunostained sections from the prefrontal cortex. Immunostaining is mostly present in axon pre-terminals (PrT) that did not form synapses with postsynaptic structures. Occasional labelled dendrites (DE) are also found, that formed asymmetrical synapses (S) with unlabelled axon terminals (AT). Scale: a, b, c=50A nm, e=100A nm. Image collected and cropped by Citeab from the following publication (Localisation of Formyl-Peptide Receptor 2 in the Rat Central Nervous System and Its Role in Axonal and Dendritic Outgrowth. Neurochem Res (2018)) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/FPRL1-FPR2-Antibody---BSA-Free-Electron-Microscopy-NLS1878-img0010.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)
![Western Blot: Recombinant Human alpha-Synuclein Active, Pre-formed Fibrils, (Type 1) Protein [NBP2-54789] - Lane 1: Molecular Weight Ladder (MW). Lane 2: Active Alpha Synuclein Protein Aggregate.](http://images.novusbio.com/fullsize/Recombinant-Human-alpha-Synuclein-Active-Pre-formed-Fibrils-Type-1-Protein-Western-Blot-NBP2-54789-img0005.jpg "Western Blot: Recombinant Human alpha-Synuclein Active, Pre-formed Fibrils, (Type 1) Protein [NBP2-54789] - Lane 1: Molecular Weight Ladder (MW). Lane 2: Active Alpha Synuclein Protein Aggregate.")
![Immunocytochemistry/Immunofluorescence: Recombinant Human alpha-Synuclein Active, Pre-formed Fibrils, (Type 1) Protein [NBP2-54789] - Primary rat hippocampal neurons show lewy body inclusion formation when treated with active Alpha Synuclein Protein Aggregate at 4 ug/ml (D-F), but not when treated with control Alpha Synuclein Protein Aggregate at 4 ug/ml (A-C). Tissue: Primary hippocampal neurons. Species: Sprague-Dawley rat. Fixation: 4% formaldehyde from PFA. Primary Antibody: Mouse anti-pSer129 Antibody at 1:1000 24 hours at 4C. Secondary Antibody: FITC Goat Anti-Mouse (green) at 1:700 for 1 hours at RT. Counterstain: Hoechst (blue) nuclear stain at 1:4000 for 1 hour at RT. Localization: Lewy body incluscions. Magnification: 20x.](http://images.novusbio.com/fullsize/Recombinant-Human-alpha-Synuclein-Active-Pre-formed-Fibrils-Type-1-Protein-Immunocytochemistry-Immunofluorescence-NBP2-54789-img0004.jpg)
![Immunohistochemistry: Recombinant Human alpha-Synuclein Active, Pre-formed Fibrils, (Type 1) Protein [NBP2-54789] - Immunohistochemistry analysis of rat brain injected with Type 1 human alpha synuclein PFFs (NBP2-54789). Species: Female Sprague-Dawley Rat. Rat was injected with 16g Type 1 human alpha synuclein PFFs (NBP2-54789) in each of 2 injection sites: AP+1.6, ML+2.4, DV-4.2 from skull; and AP-1.4, ML+0.2, DV-2.8 from skull. 30-days post-injection. Fixation: Saline perfusion followed by 4% PFA fixation for 48 hrs. Primary antibody: rabbit monoclonal anti-pSer129 alpha synuclein. Secondary Antibody: Biotin-SP Donkey Anti-Rabbit IgG (H+L) at 1:500 for 2 hours in cold room with shaking. ABC signal amplification, DAB staining. Magnification: 20X. Alpha synuclein pathology is seen in the striatum close to an injection site.](http://images.novusbio.com/fullsize/Recombinant-Human-alpha-Synuclein-Active-Pre-formed-Fibrils-Type-1-Protein-Immunohistochemistry-NBP2-54789-img0007.jpg)
![In vitro assay: Recombinant Human alpha-Synuclein Active, Pre-formed Fibrils, (Type 1) Protein [NBP2-54789] - Thioflavin T emission curves show increased fluorescence (correlated to alpha Synuclein protein aggregation) over time when 10 nM of active alpha Synuclein aggregate (NBP2-54789) is combined with 100 uM of active alpha Synuclein monomer (NBP2-54788), as compared to active alpha Synuclein aggregate (NBP2-54789) and active alpha Synuclein monomer (NBP2-54788) alone. Thioflavin T ex = 450 nm, em = 485 nm.](http://images.novusbio.com/fullsize/Recombinant-Human-alpha-Synuclein-Active-Pre-formed-Fibrils-Type-1-Protein-In-vitro-assay-NBP2-54789-img0006.jpg)
![Electron Microscopy: Recombinant Human alpha-Synuclein Active, Pre-formed Fibrils, (Type 1) Protein [NBP2-54789] - TEM of Type 1 alpha-Synuclein Pre-formed Fibrils (PFFs) (NBP2-54789)](http://images.novusbio.com/fullsize/Recombinant-Human-alpha-Synuclein-Active-Pre-formed-Fibrils-Type-1-Protein-Electron-Microscopy-NBP2-54789-img0008.jpg)
![Product Image: Recombinant Human alpha-Synuclein Active, Pre-formed Fibrils, (Type 1) Protein [NBP2-54789] - Toxicity results comparing Active Human Recombinant alpha-Synuclein Pre-formed Fibrils (Type 2) and Active Human Recombinant alpha-Synuclein Pre-formed Fibrils (Type 1) (Catalog No. NBP2-54789). Data was graphed after live cell imaging results were obtained using the following procedure: After 8 days in vitro, primary rat mixed cortical neuron cells were washed with 1X PBS and treated with 500 g/ml of Type 1 and Type 2 alpha-Synuclein Proteins for 20 hours at 37C. Following treatements, cells were washed with 2X PBS and incubated with a staining solution (2.0 M Cell Event + 2.5 M Ethidium homodimer + 2.5 g/ml Hoechst 33342 in sterile HBSS) for 30 minutes at 37C. The addition of the Type 2 alpha-Synuclein Proteins resulted in a significant increase in cell death.](http://images.novusbio.com/fullsize/Recombinant-Human-alpha-Synuclein-Active-Pre-formed-Fibrils-Type-1-Protein-Product-Image-NBP2-54789-img0010.jpg)
![Electron Microscopy: Recombinant Human alpha-Synuclein Active, Pre-formed Fibrils, (Type 1) Protein [NBP2-54789] - TEM of Type 1 alpha-Synuclein Pre-formed Fibrils (PFFs) (NBP2-54789)](http://images.novusbio.com/fullsize/Recombinant-Human-alpha-Synuclein-Active-Pre-formed-Fibrils-Type-1-Protein-Electron-Microscopy-NBP2-54789-img0009.jpg)
![Western Blot: Recombinant Human alpha-Synuclein Active, Pre-formed Fibrils, (Type 2) Protein [NBP2-54787] - Lane 1: Molecular Weight Ladder (MW). Lane 2: Alpha Synuclein Protein Aggregate](http://images.novusbio.com/fullsize/Recombinant-Human-alpha-Synuclein-Active-Pre-formed-Fibrils-Type-2-Protein-Western-Blot-NBP2-54787-img0005.jpg "Western Blot: Recombinant Human alpha-Synuclein Active, Pre-formed Fibrils, (Type 2) Protein [NBP2-54787] - Lane 1: Molecular Weight Ladder (MW). Lane 2: Alpha Synuclein Protein Aggregate")
![Immunocytochemistry/Immunofluorescence: Recombinant Human alpha-Synuclein Active, Pre-formed Fibrils, (Type 2) Protein [NBP2-54787] - Primary rat hippocampal neurons show lewy body inclusion formation when treated with active Alpha Synuclein Protein Aggregate at 4 ug/ml (D-F), but not when treated with control Alpha Synuclein Protein Aggregate at 4 ug/ml (A-C). Tissue: Primary hippocampal neurons. Species: Sprague-Dawley rat. Fixation: 4% formaldehyde made from PFA. Primary Antibody: Mouse anti-pSer129 Antibody at 1:1000 24 hours at 4C. Secondary Antibody: FITC Goat Anti-Mouse (green) at 1:700 for 1 hours at RT. Counterstain: Hoechst (blue) nuclear stain at 1:4000 for 1 hour at RT. Localization: Lewy body incluscions. Magnification: 20x.](http://images.novusbio.com/fullsize/Recombinant-Human-alpha-Synuclein-Active-Pre-formed-Fibrils-Type-2-Protein-Immunocytochemistry-Immunofluorescence-NBP2-54787-img0006.jpg)
![In vitro assay: Recombinant Human alpha-Synuclein Active, Pre-formed Fibrils, (Type 2) Protein [NBP2-54787] - Thioflavin T is a fluorescent dye that binds to beta sheet-rich structures, such as those in alpha Synuclein aggregates. Upon binding, the emission spectrum of the dye experiences a red-shift, and increased fluorescence intensity. Thioflavin T emission curves show increased fluorescence (correlated to alpha Synuclein protein aggregation) over time when 10 nM of active alpha Synuclein aggregate (NBP2-54789) is combined with 100 uM of active alpha Synuclein monomer (NBP2-54788), as compared to when 100 uM of active alpha Synuclein monomer (NBP2-54788) is combined with 10 nM of control alpha Synuclein aggregate (NBP2-54787), or 100 uM of control alpha Synuclein monomer (NBP2-54786) is combined with 10 nM of control alpha Synuclein aggregate (NBP2-54787). Thioflavin T ex = 450 nm, em = 485 nm.](http://images.novusbio.com/fullsize/Recombinant-Human-alpha-Synuclein-Active-Pre-formed-Fibrils-Type-2-Protein-In-vitro-assay-NBP2-54787-img0007.jpg)
![Product Image: Recombinant Human alpha-Synuclein Active, Pre-formed Fibrils, (Type 2) Protein [NBP2-54787] - Toxicity results comparing Active Human Recombinant alpha-Synuclein Pre-formed Fibrils (Type 2) (Catalog No. NBP2-54787) and Active Human Recombinant alpha-Synuclein Pre-formed Fibrils (Type 1). Data was graphed after live cell imaging results were obtained using the following procedure: After 8 days in vitro, primary rat mixed cortical neuron cells were washed with 1X PBS and treated with 500 g/ml of Type 1 and Type 2 alpha-Synuclein Proteins for 20 hours at 37C. Following treatements, cells were washed with 2X PBS and incubated with a staining solution (2.0 M Cell Event + 2.5 M Ethidium homodimer + 2.5 g/ml Hoechst 33342 in sterile HBSS) for 30 minutes at 37C. The addition of the Type 2 alpha-Synuclein Proteins resulted in a significant increase in cell death.](http://images.novusbio.com/fullsize/Recombinant-Human-alpha-Synuclein-Active-Pre-formed-Fibrils-Type-2-Protein-Product-Image-NBP2-54787-img0009.jpg)
![Electron Microscopy: Recombinant Human alpha-Synuclein Active, Pre-formed Fibrils, (Type 2) Protein [NBP2-54787] - TEM of Type 2 alpha-Synuclein Pre-formed Fibrils (PFFs) (NBP2-54787)](http://images.novusbio.com/fullsize/Recombinant-Human-alpha-Synuclein-Active-Pre-formed-Fibrils-Type-2-Protein-Electron-Microscopy-NBP2-54787-img0008.jpg)
![Immunohistochemistry: Recombinant Mouse alpha-Synuclein Active, Pre-formed Fibrils, (Type 1) Protein [NBP2-61596] - Immunohistochemistry analysis of rat brain injected with Type 1 mouse alpha synuclein PFFs (NBP2-61596). Species: Female Sprague-Dawley Rat. Rat was injected with 16g Type 1 mouse alpha synuclein PFFs (NBP2-61596) in each of 2 injection sites: AP+1.6, ML+2.4, DV-4.2 from skull; and AP-1.4, ML+0.2, DV-2.8 from skull. 30 days post-injection. Fixation: Saline perfusion followed by 4% PFA fixation for 48 hrs. Primary antibody: rabbit monoclonal anti-pSer129 alpha synuclein. Secondary Antibody: Biotin-SP Donkey Anti-Rabbit IgG (H+L) at 1:500 for 2 hours in cold room with shaking. ABC signal amplification, DAB staining. Magnification: 20X. Alpha synuclein pathology is seen in the periform/insular cortex and the cingulate cortex on both the same (ipsi) and opposite (contra) sides as the injection sites.](http://images.novusbio.com/fullsize/Recombinant-Mouse-alpha-Synuclein-Active-Pre-formed-Fibrils-Type-1-Protein-Immunohistochemistry-NBP2-61596-img0003.jpg "Immunohistochemistry: Recombinant Mouse alpha-Synuclein Active, Pre-formed Fibrils, (Type 1) Protein [NBP2-61596] - Immunohistochemistry analysis of rat brain injected with Type 1 mouse alpha synuclein PFFs (NBP2-61596). Species: Female Sprague-Dawley Rat. Rat was injected with 16g Type 1 mouse alpha synuclein PFFs (NBP2-61596) in each of 2 injection sites: AP+1.6, ML+2.4, DV-4.2 from skull; and AP-1.4, ML+0.2, DV-2.8 from skull. 30 days post-injection. Fixation: Saline perfusion followed by 4% PFA fixation for 48 hrs. Primary antibody: rabbit monoclonal anti-pSer129 alpha synuclein. Secondary Antibody: Biotin-SP Donkey Anti-Rabbit IgG (H+L) at 1:500 for 2 hours in cold room with shaking. ABC signal amplification, DAB staining. Magnification: 20X. Alpha synuclein pathology is seen in the periform/insular cortex and the cingulate cortex on both the same (ipsi) and opposite (contra) sides as the injection sites.")
![In vitro assay: Recombinant Mouse alpha-Synuclein Active, Pre-formed Fibrils, (Type 1) Protein [NBP2-61596] - Active alpha synuclein aggregate seeds the formation of new alpha Synuclein aggregates from the pool of active monomers. Thioflavin T is a fluorescent dye that binds to beta sheet-rich structures, such as those in alpha Synuclein aggregates. Upon binding, the emission spectrum of the dye experiences a red-shift, and increased fluorescence intensity. Thioflavin T emission curves show increased fluorescence (correlated to alpha Synuclein protein aggregation) over time when 10 nM of active alpha Synuclein aggregate is combined with 100 uM of active alpha Synuclein monomer, as compared to active alpha Synuclein aggregate and active alpha Synuclein monomer alone. Thioflavin T excitation maximum = 450 nm; emission maximum = 485 nm.](http://images.novusbio.com/fullsize/Recombinant-Mouse-alpha-Synuclein-Active-Pre-formed-Fibrils-Type-1-Protein-In-vitro-assay-NBP2-61596-img0002.jpg)
![Electron Microscopy: Recombinant Mouse alpha-Synuclein Active, Pre-formed Fibrils, (Type 1) Protein [NBP2-61596] - TEM of Type 1 mouse alpha synuclein Pre-formed Fibrils (NBP2-61596). Fibrils were sonicated and image was taken at 100kx magnification.](http://images.novusbio.com/fullsize/Recombinant-Mouse-alpha-Synuclein-Active-Pre-formed-Fibrils-Type-1-Protein-Electron-Microscopy-NBP2-61596-img0005.jpg)
![Electron Microscopy: Recombinant Mouse alpha-Synuclein Active, Pre-formed Fibrils, (Type 1) Protein [NBP2-61596] - TEM of Type 1 mouse alpha synuclein Pre-formed Fibrils (NBP2-61596). Image was taken at 100kx magnification.](http://images.novusbio.com/fullsize/Recombinant-Mouse-alpha-Synuclein-Active-Pre-formed-Fibrils-Type-1-Protein-Electron-Microscopy-NBP2-61596-img0004.jpg)
![Immunohistochemistry: Recombinant Mouse alpha-Synuclein Active, Pre-formed Fibrils, (Type 1) Protein [NBP2-61596] - TH fluorescence in mouse brain. Image from a verified customer review.](http://images.novusbio.com/fullsize/nbp2-61596_recombinant-mouse-alpha-synuclein-active-pre-formed-fibrils-type-1-protein-immunohistochemistry-205202512497..jpg)
![Western Blot: beta Amyloid 42 Peptide [NBP3-18318] - Western blot of amyloid beta 1-42 monomers (NBP3-18318, left), oligomers (middle) and fibrils (right) using anti-amyloid beta 6E10 antibody. Amyloid beta constructs at 160 pmol were run on 4-12% Bis-Tris SDS-PAGE, transferred to nitrocellulose in the presence of 0.02% v/v Tween-20, and blotted with 1:1000 mouse 6E10 primary antibody (Biolegend). Oligomers observed under TEM/AFM show distinct dimer/trimer bands as well as a signal from ~37-75 kDa (middle). Fibrils observed under TEM/AFM show a signal greater than 100 kDa and a distinct signal in the stacking gel (right).](http://images.novusbio.com/fullsize/beta-Amyloid-42-Peptide-Western-Blot-NBP3-18318-img0001.jpg "Western Blot: beta Amyloid 42 Peptide [NBP3-18318] - Western blot of amyloid beta 1-42 monomers (NBP3-18318, left), oligomers (middle) and fibrils (right) using anti-amyloid beta 6E10 antibody. Amyloid beta constructs at 160 pmol were run on 4-12% Bis-Tris SDS-PAGE, transferred to nitrocellulose in the presence of 0.02% v/v Tween-20, and blotted with 1:1000 mouse 6E10 primary antibody (Biolegend). Oligomers observed under TEM/AFM show distinct dimer/trimer bands as well as a signal from ~37-75 kDa (middle). Fibrils observed under TEM/AFM show a signal greater than 100 kDa and a distinct signal in the stacking gel (right).")
![In vitro assay: beta Amyloid 42 Peptide [NBP3-18318] - Amyloid beta 1-42 oligomers and fibrils show a dose-dependent toxicity to primary rat cortical neurons, but not monomers (NBP3-18318). Survival of rat primary cortical neurons 14 days after treatment with different concentrations of (A) monomers, (B) oligomers or (C) fibrils quantified by MAP2 positive neurons and expressed as a percentage of control. Fibrils and respective vehicle controls were initially sonicated in a Bioruptor. Test conditions were run in the same plate as untreated control and vehicle controls, which consisted of buffer without amyloid beta 1-42 protein. Data expressed as mean +/- s.e.m. (n=6). A global analysis of the data was performed using a one-way ANOVA followed by Dunnetts test; ** p<0.01 stats vs control; ## p<0.01, #### p<0.0001 stats vs vehicle control.](http://images.novusbio.com/fullsize/beta-Amyloid-42-Peptide-In-vitro-assay-NBP3-18318-img0002.jpg)
![Immunomicroscopy: beta Amyloid 42 Peptide [NBP3-18318] - AFM of amyloid beta 1-42 monomers (NBP3-18318, left), oligomers (middle) and fibrils (right). Atomic force microscopy analysis of 1.0 mg/mL samples diluted to 0.1 mg/mL in dH2O, mounted on freshly cleaved mica, washed, dried and analyzed with tapping mode. Representative images are 2.5 x 2.5 m x-y with a z-range of 10 nm.](http://images.novusbio.com/fullsize/beta Amyloid 42 Peptide-Immunomicroscopy-NBP3-18318-img0004.jpg)
![Electron Microscopy: beta Amyloid 42 Peptide [NBP3-18318] - TEM of amyloid beta 1-42 monomers (NBP3-18318, left), oligomers (middle) and fibrils (right). Negative stain transmission electron microscopy images acquired at 80 Kv on carbon coated 400 mesh copper grids using phosphotungstic acid and uranyl acetate stain. Scale bar = 100 nm.](http://images.novusbio.com/fullsize/beta-Amyloid-42-Peptide-Electron-Microscopy-NBP3-18318-img0003.jpg)
![Electron Microscopy: Recombinant Human alpha-Synuclein Oligomers, (Dopamine HCL Stabilized) Protein [NBP3-14771] - TEM of Human Recombinant alpha-Synuclein Oligomers (Dopamine HCL Stabilized) (NBP3-14771)](http://images.novusbio.com/fullsize/Recombinant-Human-alpha-Synuclein-Oligomers-Dopamine-HCL-Stabilized-Protein-Electron-Microscopy-NBP3-14771-img0001.jpg "Electron Microscopy: Recombinant Human alpha-Synuclein Oligomers, (Dopamine HCL Stabilized) Protein [NBP3-14771] - TEM of Human Recombinant alpha-Synuclein Oligomers (Dopamine HCL Stabilized) (NBP3-14771)")
![Electron Microscopy: Recombinant Human alpha-Synuclein Oligomers, (Dopamine HCL Stabilized) Protein [NBP3-14771] - TEM of Human Recombinant alpha-Synuclein Oligomers (Dopamine HCL Stabilized) (NBP3-14771)](http://images.novusbio.com/fullsize/Recombinant-Human-alpha-Synuclein-Oligomers-Dopamine-HCL-Stabilized-Protein-Electron-Microscopy-NBP3-14771-img0002.jpg)
![SDS-Page: Recombinant Human alpha-Synuclein Oligomers, (Dopamine HCL Stabilized) Protein [NBP3-14771] - Coomassie gel stain of human dopamine-stabilized alpha synuclein oligomers (NBP3-14771). Load: 2 ug.](http://images.novusbio.com/fullsize/Recombinant-Human-alpha-Synuclein-Oligomers-Dopamine-HCL-Stabilized-Protein-SDS-Page-NBP3-14771-img0004.jpg)
![Product Image: Recombinant Human alpha-Synuclein Oligomers, (Dopamine HCL Stabilized) Protein [NBP3-14771] - HPLC of alpha-Synuclein Protein Oligomers (NBP3-14771) ran down a size exclusion column. Wavelength: 280 nm.](http://images.novusbio.com/fullsize/Recombinant-Human-alpha-Synuclein-Oligomers-Dopamine-HCL-Stabilized-Protein-Product-Image-NBP3-14771-img0003.jpg)
![SDS-Page: Recombinant Human Tau 441 Active, P301S Mutant, Pre-formed Fibrils Protein [NBP2-76794] - DS-PAGE of ~67 kDa Human Tau Protein 2N4R P301S Preformed Fibrils (NBP2-76794). Lane 1: MW Ladder. Lane 2: Tau Protein Preformed Fibrils (NBP2-76794)](http://images.novusbio.com/fullsize/Recombinant-Human-Tau-441-Active--P301S-Mutant--Pre-formed-Fibrils-Protein-SDS-Page-NBP2-76794-img0001.jpg "SDS-Page: Recombinant Human Tau 441 Active, P301S Mutant, Pre-formed Fibrils Protein [NBP2-76794] - DS-PAGE of ~67 kDa Human Tau Protein 2N4R P301S Preformed Fibrils (NBP2-76794). Lane 1: MW Ladder. Lane 2: Tau Protein Preformed Fibrils (NBP2-76794)")
![In vitro assay: Recombinant Human Tau 441 Active, P301S Mutant, Pre-formed Fibrils Protein [NBP2-76794] - Thioflavin T is a fluorescent dye that binds to beta sheet-rich structures such as those in tau fibrils. Upon binding, the emission spectrum of the dye experiences a red-shift, and increased fluorescence intensity. Thioflavin T emission curves show increased fluorescence (correlated to tau aggregation) when tau Pre-formed Fibrils (NBP2-76794) are combined with tau monomers . The Pre-formed Fibrils seed the formation of new fibrils from a pool of monomers. Thioflavin T ex = 450 nm, em = 485 nm. 10 uM heparin was added to each well.](http://images.novusbio.com/fullsize/Recombinant-Human-Tau-441-Active--P301S-Mutant--Pre-formed-Fibrils-Protein-In-vitro-assay-NBP2-76794-img0002.jpg)
![Electron Microscopy: Recombinant Human Tau 441 Active, P301S Mutant, Pre-formed Fibrils Protein [NBP2-76794] - TEM of recombinant Tau 441441 (2N4R), P301S mutant Pre-formed Fibrils (PFFs). Fibrils were sonicated and stained with uranyl acetate.](http://images.novusbio.com/fullsize/Recombinant Human Tau 441 Active- P301S Mutant- Pre-formed Fibrils Protein-Electron Microscopy-NBP2-76794-img0004.jpg)
![Electron Microscopy: Recombinant Human Tau 441 Active, P301S Mutant, Pre-formed Fibrils Protein [NBP2-76794] - TEM of recombinant Tau 441441 (2N4R), P301S mutant Pre-formed Fibrils (PFFs) at 150kx magnification. HV = 80kV. Fibrils were sonicated and stained with uranyl acetate.](http://images.novusbio.com/fullsize/Recombinant-Human-Tau-441-Active--P301S-Mutant--Pre-formed-Fibrils-Protein-Electron-Microscopy-NBP2-76794-img0003.jpg)
![In vitro assay: Recombinant Human alpha-Synuclein Active, Pre-formed Fibrils, (Type 1) Acetyl (N-Term) Protein [NBP3-14769] - Thioflavin T assay for N-terminal acetylated alpha synuclein monomers and pre-formed fibrils (PFFs) (NBP3-14769). Increased fluorescence, indicative of beta-sheet formation, was seen when 50 ug N-acetylated monomer and 5 ug N-acetylated fibril were combined, compared to monomer or fibril alone.](http://images.novusbio.com/fullsize/Recombinant-Human-alpha-Synuclein-Active-Pre-formed-Fibrils-Type-1-Acetyl-N-Term-Protein-In-vitro-assay-NBP3-14769-img0001.jpg "In vitro assay: Recombinant Human alpha-Synuclein Active, Pre-formed Fibrils, (Type 1) Acetyl (N-Term) Protein [NBP3-14769] - Thioflavin T assay for N-terminal acetylated alpha synuclein monomers and pre-formed fibrils (PFFs) (NBP3-14769). Increased fluorescence, indicative of beta-sheet formation, was seen when 50 ug N-acetylated monomer and 5 ug N-acetylated fibril were combined, compared to monomer or fibril alone.")
![Electron Microscopy: Recombinant Human alpha-Synuclein Active, Pre-formed Fibrils, (Type 1) Acetyl (N-Term) Protein [NBP3-14769] - TEM of N-terminal acetylated alpha synuclein pre-formed fibirls (PFFs) (NBP3-14769)](http://images.novusbio.com/fullsize/Recombinant-Human-alpha-Synuclein-Active-Pre-formed-Fibrils-Type-1-Acetyl-N-Term-Protein-Electron-Microscopy-NBP3-14769-img0003.jpg)
![Electron Microscopy: Recombinant Human alpha-Synuclein Active, Pre-formed Fibrils, (Type 1) Acetyl (N-Term) Protein [NBP3-14769] - TEM of N-terminal acetylated alpha synuclein pre-formed fibirls (PFFs) (NBP3-14769)](http://images.novusbio.com/fullsize/Recombinant-Human-alpha-Synuclein-Active-Pre-formed-Fibrils-Type-1-Acetyl-N-Term-Protein-Electron-Microscopy-NBP3-14769-img0002.jpg)
![In vitro assay: Recombinant Rat alpha-Synuclein Active, Pre-formed Fibrils Protein [NBP3-14774] - Thioflavin T is a fluorescent dye that binds to beta sheet-rich structures, such as those in alpha synuclein monomers and fibrils. Upon binding, the emission spectrum of the dye experiences a red-shift, and increased fluorescence intensity. The Rat alpha-Synuclein monomer is very active and was able to form more beta-sheet structure alone than with the combination of monomer and fibril. In combination, the fibril (NBP3-14774) is the majority of the seed.](http://images.novusbio.com/fullsize/Recombinant-Rat-alpha-Synuclein-Active--Pre-formed-Fibrils-Protein-In-vitro-assay-NBP3-14774-img0001.jpg "In vitro assay: Recombinant Rat alpha-Synuclein Active, Pre-formed Fibrils Protein [NBP3-14774] - Thioflavin T is a fluorescent dye that binds to beta sheet-rich structures, such as those in alpha synuclein monomers and fibrils. Upon binding, the emission spectrum of the dye experiences a red-shift, and increased fluorescence intensity. The Rat alpha-Synuclein monomer is very active and was able to form more beta-sheet structure alone than with the combination of monomer and fibril. In combination, the fibril (NBP3-14774) is the majority of the seed.")
![Electron Microscopy: Recombinant Rat alpha-Synuclein Active, Pre-formed Fibrils Protein [NBP3-14774] - TEM of Rat alpha-Synuclein Pre-formed Fibrils (PFFS) (NBP3-14774). 500nm](http://images.novusbio.com/fullsize/Recombinant Rat alpha-Synuclein Active- Pre-formed Fibrils Protein-Electron Microscopy-NBP3-14774-img0003.jpg)
![Electron Microscopy: Recombinant Rat alpha-Synuclein Active, Pre-formed Fibrils Protein [NBP3-14774] - TEM of Rat alpha-Synuclein Pre-formed Fibrils (PFFS) (NBP3-14774). 200nm](http://images.novusbio.com/fullsize/Recombinant-Rat-alpha-Synuclein-Active--Pre-formed-Fibrils-Protein-Electron-Microscopy-NBP3-14774-img0002.jpg)
![In vitro assay: Recombinant Human SOD1/Cu-Zn SOD Pre-formed Fibrils Protein [NBP3-14783] - Thioflavin T assay of SOD1 pre-formed fibrils (PFFs) (NBP3-14783) combined with SOD1 monomers . Pre-formed fibrils seed the aggregation of monomers, leading to an increase in Thioflavin T fluorescence](http://images.novusbio.com/fullsize/Recombinant-Human-SOD1-Cu-Zn-SOD-Pre-formed-Fibrils-Protein-In-vitro-assay-NBP3-14783-img0001.jpg "In vitro assay: Recombinant Human SOD1/Cu-Zn SOD Pre-formed Fibrils Protein [NBP3-14783] - Thioflavin T assay of SOD1 pre-formed fibrils (PFFs) (NBP3-14783) combined with SOD1 monomers . Pre-formed fibrils seed the aggregation of monomers, leading to an increase in Thioflavin T fluorescence")
![Electron Microscopy: Recombinant Human SOD1/Cu-Zn SOD Pre-formed Fibrils Protein [NBP3-14783] - TEM of human SOD1 pre-formed fibrils (PFFs)](http://images.novusbio.com/fullsize/Recombinant Human SOD1-Cu-Zn SOD Pre-formed Fibrils Protein-Electron Microscopy-NBP3-14783-img0003.jpg)
![Electron Microscopy: Recombinant Human SOD1/Cu-Zn SOD Pre-formed Fibrils Protein [NBP3-14783] - TEM of human SOD1 pre-formed fibrils (PFFs)](http://images.novusbio.com/fullsize/Recombinant-Human-SOD1-Cu-Zn-SOD-Pre-formed-Fibrils-Protein-Electron-Microscopy-NBP3-14783-img0002.jpg)