Lipocalin-2/NGAL: Novus Biologicals

DY1857

Mouse Lipocalin-2/NGAL DuoSet ELISA, 15 Plate

(152 Publications)

1 Kit (for 5 Plates)

DY1857

Reactivity:

Mu

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Reactivity: Mu

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Applications:

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AF1857

Lipocalin-2/NGAL Antibody [Unconjugated]

(2 Reviews)

(122 Publications)

100 μg

AF1857

HAF017). A specific band was detected for Lipocalin-2/NGAL at approximately 24 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1." class="big_lightbox">

Western blot shows lysates of mouse uterus tissue. PVDF membrane was probed with 0.25 µg/mL of Goat Anti-Mouse Lipocalin-2/NGAL Antigen Affinity-purified Polyclonal Antibody (Catalog # AF1857) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (<a class=

HAF017). A specific band was detected for Lipocalin-2/NGAL at approximately 24 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1." alt="Western blot shows lysates of mouse uterus tissue. PVDF membrane was probed with 0.25 µg/mL of Goat Anti-Mouse Lipocalin-2/NGAL Antigen Affinity-purified Polyclonal Antibody (Catalog # AF1857) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (HAF017). A specific band was detected for Lipocalin-2/NGAL at approximately 24 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1." class="big_thumb" />

VC004). Tissue was stained using DAB (brown) and counterstained with hematoxylin (blue). Specific staining was localized to extracellular areas in ducts. View our protocol for IHC Staining with VisUCyte HRP Polymer Detection Reagents." class="big_lightbox">

Lipocalin-2/NGAL was detected in perfusion fixed frozen sections of mouse mammary gland using Goat Anti-Mouse Lipocalin-2/NGAL Antigen Affinity-purified Polyclonal Antibody (Catalog # AF1857) at 3 µg/mL for 1 hour at room temperature followed by incubation with the Anti-Goat IgG VisUCyte™ HRP Polymer Antibody (<a class=

VC004). Tissue was stained using DAB (brown) and counterstained with hematoxylin (blue). Specific staining was localized to extracellular areas in ducts. View our protocol for IHC Staining with VisUCyte HRP Polymer Detection Reagents." class="big_thumb" />

HAF109). This experiment was conducted under reducing conditions and using the 12-230 kDa separation system." class="big_lightbox">

Simple Western lane view shows lysates of mouse lung tissue, loaded at 0.2 mg/mL. A specific band was detected for Lipocalin-2/NGAL at approximately 37 kDa (as indicated) using 5 µg/mL of Goat Anti-Mouse Lipocalin-2/NGAL Antigen Affinity-purified Polyclonal Antibody (Catalog # AF1857) followed by 1:50 dilution of HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # <a class=

HAF109). This experiment was conducted under reducing conditions and using the 12-230 kDa separation system." class="big_thumb" />

Human and murine C/EBP-epsilon induces expression of HNP-1 in primary bone marrow (BM) cells from transgenic HNP-1 mice.Murine BM cells from seven transgenic HNP-1 mice were isolated and early granulocyte precursors isolated by density centrifugation on a discontinuous Percoll 1.072 gradient. Cells were retrovirally transduced with an empty expression vector (pMIG) or with a vector expressing either human or murine C/EBP-epsilon (pMIG-CEBPE or pMIG-Cebpe respectively). Cells were incubated for 48 hours. (A) Green fluorescent protein (GFP) was used as reporter gene in the vectors and transduction efficiency evaluated by flow cytometry. (B–G) Comparative quantification of mRNA for CCAAT/enhancer binding protein-epsilon (human CEBPE or murine Cebpe), human neutrophil peptide-1 (DEFA1), cathelicidin antimicrobial peptide (Camp), and lipocalin-2 (Lcn2) was done by real-time PCR using Gapdh as normalizer. Error bars depict standard deviation. (B, E–G) Levels are shown as fold induction by either murine Cebpe (mCebpe) or human CEBPE (hCEBPE) compared to levels from negative control transduction (pMIG). (C) Relative quantification of human CEBPE in murine bone marrow cells from four transgenic HNP-1 mice transduced with control vector (pMIG) or human CEBPE. (D) Expression of murine Cebpe in Cebpe transduced cells were compared to human CEBPE in CEBPE transduced cells by comparing Delta Ct between the transduced gene and Gapdh. The transduced mouse with the lowest expression of C/EBP-epsilon was used as calibrator. (H) Western blotting of C/EBP-epsilon , 24p3, and beta-actin in transduced cells from two mice. (I–J) Cells were fixed in formaldehyde. Cell and nuclear membranes were lysed before fragmentation of DNA by sonication. Chromatin was immunoprecipitated using protein A/G magnetic beads and an antibody against C/EBP-epsilon , C/EBP-alpha , or negative control rabbit IgG. After washing procedures, immune complexes were eluted and reversed and DNA recovered. DNA was used as a template for quantitative PCR. Primer

Immunolocalization of LCN2 in astrocytes and neutrophils in the ipsilateral cortex after tMCAo. Mouse brain slices isolated at 23 h after tMCAo were labeled with LCN2 antibody (green, A), Tomato Lectin (red, blood vessel, B), and GFAP antibody (blue, astrocyte, C). (D) Merged image showing the expression of LCN2 in an astrocyte whose end-feet encircle blood vessels (arrowheads). Brain slices isolated at 23 h after tMCAo were stained with antibodies recognizing LCN2 (green, E) and a specific marker for neutrophils (anti-Ly-6B.2 clone 7/4) (red, F). Nuclei were labeled with DAPI (blue, G). (H) Merged image showing the colocalization of LCN2 with 7/4 in yellow. The shaded area in the inset indicates the infarcted region. (I) The percentage of LCN2-positive cell types (n = 5). Scale bars, 10 μm (A–D), 50 μm (E–H). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32872405), licensed under a CC-BY license. Not internally tested by R&D Systems.

<b>Biological Strategies Validation. </b>Keap1 hypomorphs demonstrated unequivocal protection 10 days after ischemia-reperfusion injury (IRI).Keap1 hypomorphs (KEAP1) and wild type (WT) mice were subjected to unilateral renal IRI, with a contralateral nephrectomy performed 24 hours prior to sacrifice at 10 days. (a) Kidney sections were subjected to Masson’s Trichrome staining to evaluate for fibrosis development (collagen appears blue). WT mice also had more inflammatory cells. Low powered views are shown along with an enlarged inset of the boxed area. Bar equals 100 μm. Picrosirius red was also performed – under light microscopy collagen and other cellular components stain red. With polarized light of the same sections shown on light microscopy, birefringence is highly specific for collagen. (b) Keap1 hypomorphs had significantly decreased fibrosis, which was confirmed with fibrosis scoring (n = 5–6 for each group). (c,d) Serum creatinine and BUN were significantly reduced in the hypomorphs. Each dot represents an individual mouse with the mean ± SEM superimposed. (e,f) qRT-PCR for KIM-1 and NGAL shows significant reduction in these tubular injury markers in IRI KEAP1 kidneys compared to IRI WT kidneys. Brackets show significant differences, P < 0.05. (g) NGAL was significantly suppressed in the IRI KEAP1 kidneys compared to IRI WT kidneys, confirming the qRT-PCR result in (f). (P < 0.05, compared to similarly treated WT group). Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/srep36185), licensed under a CC-BY license. Not internally tested by R&D Systems.

<b>Biological Strategies Validation. </b>LCN2 monoclonal antibody (mAb) specifically immunoprecipitated recombinant and endogenous LCN2 proteins. (A) Representative Western blots showing that LCN2 mAb reduced the level of LCN2 protein by immunoprecipitation. Increasing concentrations of LCN2 mAb (0, 0.1, 0.5, and 2.5 μg) bound to the Dynabeads were incubated with a fixed amount of mouse recombinant LCN2 protein (0.1 μg). LCN2 mAb bound to the Dynabeads, immunoprecipitated LCN2 protein, and unbound LCN2 protein in the supernatant after the immunoprecipitation are shown in the top, middle, and bottom panels, respectively; (B,C) LCN2 mAb specifically immunoprecipitated the LCN2 protein that was induced after tMCAo. Ipsilateral hemisphere lysates (B) and blood sera (C) collected from naive LCN2+/+ and LCN2−/− mice (+/+ con and −/− con) and at 23 h after tMCAo (+/+ tMCAo and −/− tMCAo) were immunoprecipitated with LCN2 mAb and analyzed by Western blotting using a polyclonal antibody that recognized LCN2 protein; (D) Total RNA isolated from ipsilateral hemispheres of naive LCN2+/+ and LCN2−/− mice (+/+ con and −/− con), at 23 h after tMCAo (+/+ tMCAo and −/− tMCAo), and LCN2+/+ mice treated with LCN2 mAb at 4 h after tMCAo (+/+ tMCAo LCN2 mAb) was analyzed by real-time RT-PCR (n = 6 per group). Relative mRNA expression of LCN2 in the brain homogenates was compared between the mice groups using a one-way ANOVA and Newman–Keuls post hoc tests. LCN2 mRNA levels were significantly induced after tMCAo (*** p < 0.001) as compared with those in naive LCN2+/+ mice. LCN2 mRNA levels in mice that were treated with LCN2 mAb were significantly reduced (* p < 0.05) as compared those in LCN2+/+ mice after tMCAo; (E,F) Mice were treated with an isotype control IgG (con) or LCN2 mAb at 4 h after tMCAo. We analyzed the concentration of LCN2 in the ipsilateral hemispheres (n = 5 per group, E) and blood sera (n = 9–10 per group, F) at 23 h after reperfusion using ELISA. The concentration of LCN2 in the brains of mice treated with

Keap1 hypomorphs have improved renal function 3 days after ischemia-reperfusion injury (IRI).Wild type (WT) and hypomorph mice (KEAP1) were subjected to unilateral renal IRI, with a contralateral nephrectomy performed 24 hours prior to sacrifice at 3 days. (a,b) Histologic assessment of kidneys showed significant tubular injury with no perceptible difference between groups. Bar equals 100 μm. (c,d) Serum creatinine and BUN were significantly improved in the hypomorphs in spite of the lack of histologic differences. Each dot represents an individual animal with mean ± SEM shown. (e,f) qRT-PCR showed no significant reductions in proinflammatory mediators (n = 4–5 in each group). (g,h) qRT-PCR analysis of tubular injury markers KIM-1 and NGAL showed a significant increase (KIM-1) or trend to increase (NGAL) in injured kidneys vs CTL uninjured kidneys, but no significant difference between injured WT and KEAP1 kidneys. (j) Western blot and densitometry for NGAL confirms no decrease in NGAL in injured KEAP1 kidneys compared to injured WT kidneys. (*P < 0.05 compared to the wild type group. **P < 0.05 compared to either CTL group). Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/srep36185), licensed under a CC-BY license. Not internally tested by R&D Systems.

Histological characterization of mammary tumors.A, C, E, immunohistochemical staining for lipocalin-2 in mammary tumor in (A) PyMT, Lcn2+/+ mouse, (C) PyMT, Lcn2−/−, and (E) PyMT, Lcn2+/+ mouse as negative control, where no primary antibody was added. B, D, F, immunohistochemical staining for MMP-9 in mammary tumor in (B) PyMT, Lcn2+/+ mouse, (D) PyMT, Lcn2−/−, and (F) PyMT, Lcn2+/+ mouse as negative control, where no primary antibody was added. Original magnification x600. G, H+E staining of tumor from a PyMT, Lcn2+/+ mouse representing largest metastasis volume. F, H+E staining of tumor from PyMT, Lcn2−/− mouse representing largest metastasis volume. In both G and F strongly atypical tumor cells with numerous mitoses are seen, and surrounded by slender strands of collagen tissue. Original magnification x630. Abbreviations: PyMT: MMTV-PyMT. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0039646), licensed under a CC-BY license. Not internally tested by R&D Systems.

Immunolocalization of LCN2 in vascular endothelial cells in the ipsilateral cortex after transient middle cerebral artery occlusion (tMCAo). Brain slices isolated from naive mice (A–C) and at 23 h after tMCAo (D–L) were labeled with LCN2 antibody (green), tomato lectin (red, blood vessel), and GFAP antibody (blue, astrocyte). (D) Neutrophils detected within the blood vessel (arrowheads) and in ischemic brain parenchyma (arrows) labeled with LCN2 antibody (green). (G–L) Merged and amplified images showing the induction of LCN2 (green) on the inner surface of vascular endothelial cells (red) surrounded by astrocytic end-feet (blue). The shaded area in the inset indicates the infarcted region. Scale bars, 50 μm for the main images (A–I), and 10 μm for the amplified images (J–L). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32872405), licensed under a CC-BY license. Not internally tested by R&D Systems.

<b>Biological Strategies Validation. </b>LCN2 mAb attenuated neurological deficits and cerebral infarction after tMCAo. Neurological deficit scoring (A) and corner test (B) were performed at 20 h after one hour of tMCAo in mice treated with isotype control IgG (con) and LCN2 mAb (n = 7 per group). (C) Representative images of TTC-stained brain slices from mice treated with control IgG and LCN2 mAb after 23 h of reperfusion. Viable tissue is stained in red color, whereas the infarcted area remains unstained (white). Total infarct volume (D) and brain swelling percentage (E) in mice treated with LCN2 mAb were significantly decreased 23 h after reperfusion as compared with those in mice treated with the control IgG (n = 5 per group). ** p < 0.01, *** p < 0.001 compared with treatments with control IgG (two-tailed, unpaired t-test). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32872405), licensed under a CC-BY license. Not internally tested by R&D Systems.

Keap1 hypomorphs demonstrated unequivocal protection 10 days after ischemia-reperfusion injury (IRI).Keap1 hypomorphs (KEAP1) and wild type (WT) mice were subjected to unilateral renal IRI, with a contralateral nephrectomy performed 24 hours prior to sacrifice at 10 days. (a) Kidney sections were subjected to Masson’s Trichrome staining to evaluate for fibrosis development (collagen appears blue). WT mice also had more inflammatory cells. Low powered views are shown along with an enlarged inset of the boxed area. Bar equals 100 μm. Picrosirius red was also performed – under light microscopy collagen and other cellular components stain red. With polarized light of the same sections shown on light microscopy, birefringence is highly specific for collagen. (b) Keap1 hypomorphs had significantly decreased fibrosis, which was confirmed with fibrosis scoring (n = 5–6 for each group). (c,d) Serum creatinine and BUN were significantly reduced in the hypomorphs. Each dot represents an individual mouse with the mean ± SEM superimposed. (e,f) qRT-PCR for KIM-1 and NGAL shows significant reduction in these tubular injury markers in IRI KEAP1 kidneys compared to IRI WT kidneys. Brackets show significant differences, P < 0.05. (g) NGAL was significantly suppressed in the IRI KEAP1 kidneys compared to IRI WT kidneys, confirming the qRT-PCR result in (f). (P < 0.05, compared to similarly treated WT group). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27804998), licensed under a CC-BY license. Not internally tested by R&D Systems.

Effects of LCN2 deletion on microglial activation and hippocampal TREM2 expression in HFD/STZ-induced diabetic mice: (A,B) Western blot analysis and quantification of LCN2, TREM2, and NF-kappa Bp65 in the hippocampus; beta -actin and p84 were used as loading controls for total protein and nuclear protein, respectively; (C) representative immunofluorescence images of TREM2 (red) and Iba-1 (green) in hippocampal sections; DAPI (blue) was used to stain nuclei; scale bar = 10 µm; (D) quantification of co-localized TREM2 and Iba-1-immunostained cells in the images. CTL: control; DM: diabetic mice. Data are presented as the mean ± SEM. The indicated p-values represent a two-way ANOVA, followed by Tukey’s post hoc test. * p < 0.05 vs. WT CTL. † p < 0.05 vs. WT DM. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35884685), licensed under a CC-BY license. Not internally tested by R&D Systems.

Elucidation of kidney injury markers and MAPK signaling following rhabdomyolysis. Mice were administered 7.5 ml/kg body weight of 50% glycerol in water and harvested after 1 or 3 days. Kidneys were analyzed for the expression of (A) kidney injury molecule-1 (KIM-1), (B) neutrophil gelatinase associated lipocalin (NGAL), and (C) ferritin heavy chain (FtH) by real-time PCR analysis. Each experiment was performed at least three independent times. Results were normalized to GAPDH and presented as mean ± SEM. *p < 0.05 vs. baseline control; #p < 0.05 vs. FtHfl/fl. (D) Kidneys were analyzed for the expression of 4-hydroxynonenal, NGAL, KIM-1, FtH, p-ERK, total ERK, p-JNK, and total JNK by Western blot analysis. Membranes were stripped and re-probed for GAPDH to demonstrate equal loading. (E) Expression of the indicated proteins in the kidneys was analyzed by densitometry, normalized to GAPDH (or total JNK or total ERK) and expressed as mean ± SEM. *p < 0.05 vs. baseline control; #p < 0.05 vs. FtHfl/fl. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/36160140), licensed under a CC-BY license. Not internally tested by R&D Systems.

Effects of LCN2 deletion on hepatic TREM2 expression in HFD/STZ-induced diabetic mice: (A,B) Western blot analysis and quantitation of LCN2, TNF- alpha , and TREM2 proteins in liver lysates. beta -actin was used as loading control; (C) representative immunofluorescence images of TREM2 (red) and F4/80 (green) in liver sections; CV: central vein; (D) quantification of co-localized TREM2 and F4/80-immunostained cells in the images; (E) representative immunofluorescence images of TREM2 (red) and Ly6G (green) in liver section; quantification of co-localized TREM2 and Ly6G-immunostained cells in the images; scale bar = 10 µm. DAPI (blue) was used to stain nuclei. CTL: control; DM: diabetic mice. Data are presented as the mean ± SEM. The indicated p-values represent a two-way ANOVA, followed by Tukey’s post hoc test. * p < 0.05 vs. WT CTL. † p < 0.05 vs. WT DM. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35884685), licensed under a CC-BY license. Not internally tested by R&D Systems.

$Identification of LCN2 MAM localization and PA binding capability.LCN2 is recruited to the MAM in inguinal adipocytes (a) in response to 6 h LPS (1 μg/mL) treatment and in BAT (b) in response to 6 h LPS stimulation along with known MAM proteins including FACL4, MFN2 and DRP1. The experiments in a and b were repeated 3 times independently. LCN2 protein levels in cytosolic, crude mitochondria, pure mitochondria, and MAM fractions in BAT of mice with saline, 6 h LPS (0.3 mg/kg body weight), or 6 h CL316, 243 (0.5 mg/kg body weight) treatment (c). The experiment in c was repeated twice independently. Co-localization of LCN2 with ER marker Calnexin (d) and mitochondrial maker TOM 20 (e) in 3T3-L1 preadipocytes and adipocytes. The correlation analysis was performed using Pearson’s coefficient. For the co-localization of LCN2 with ER, n = 16 for preadipocytes and n = 13 for adipocytes (d). For the co-localization of LCN2 with mitochondria, n = 13 for preadipoctes and n = 11 for adipocytes (d). Results are presented as mean ± SEM. Binding assay of membrane lipids with mouse LCN2 recombinant protein (f). Concentration-dependent binding of LCN2 to phospholipids (g). Various concentrations of PA and PC were spotted on the membrane and subjected to LCN2 binding assay. Cell lysates from 3T3-L1 adipocytes with or without IL-1 beta (1 ng/mL) treatment were spotted as a positive control. Concentration-dependent LCN2-PA binding with PA-coated beads (h). Beads without PA-coated served as a control. The experiment in h was repeated twice independently. Source data are provided as a Source data file. Mito: mitochondria; CL: CL316, 243. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/37872178), licensed under a CC-BY license. Not internally tested by R&D Systems.$

Reactivity:

Mu

Species Glossary

Reactivity: Mu

Applications:

, , ,

Applications: , , ,

Host:

Goat Polyclonal

Host: Goat Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	AF1857U-100UG
Alexa Fluor 405	AF1857V-100UG
Alexa Fluor 488	AF1857G-100UG
Alexa Fluor 532	AF1857X-100UG
Alexa Fluor 594	AF1857T-100UG
Alexa Fluor 647	AF1857R-100UG
Alexa Fluor 700	AF1857N-100UG
Alexa Fluor 750	AF1857S-100UG
Alexa Fluor Plus 405	AF1857AFP405-100UG
Alexa Fluor Plus 488	AF1857AFP488-100UG
Alexa Fluor Plus 555	AF1857AFP555-100UG
Alexa Fluor Plus 594	AF1857AFP594-100UG
Alexa Fluor Plus 647	AF1857AFP647-100UG
Alexa Fluor Plus 680	AF1857AFP680-100UG
Allophycocyanin	AF1857A
Biotin	BAF1857
CoraFluor 1	AF1857CL1
DyLight 350	AF1857D
DyLight 405	AF1857E
DyLight 488	AF1857K
DyLight 550	AF1857L
DyLight 594	AF1857M
DyLight 650	AF1857W
DyLight 680	AF1857Y
DyLight 755	AF1857Z
FITC	AF1857F
HRP	AF1857H
Janelia Fluor 525	AF1857JF525
Janelia Fluor 549	AF1857I
Janelia Fluor 646	AF1857J
Janelia Fluor 669	AF1857JF669
PE	AF1857P
PerCP	AF1857C
mFluor Violet 450 SE	AF1857MFV450
mFluor Violet 500 SE	AF1857MFV500
mFluor Violet 610 SE	AF1857MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
Carrier Free	AF1857-SP

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DLCN20

Human Lipocalin-2/NGAL Quantikine ELISA Kit

(84 Publications)

1 Kit

DLCN20

Reactivity:

Hu

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Reactivity: Hu

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Conjugate	Catalog #	Availability	Size	Price
HRP	PDLCN20
HRP	SLCN20

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MLCN20

Mouse Lipocalin-2/NGAL Quantikine ELISA Kit

(66 Publications)

1 Kit

MLCN20

Reactivity:

Mu

Species Glossary

Reactivity: Mu

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AF1757

Lipocalin-2/NGAL Antibody [Unconjugated]

(41 Publications)

100 μg

AF1757

HAF109). A specific band was detected for Lipocalin-2/NGAL at approximately 22 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1." class="big_lightbox">

Western blot shows lysates of Capan-1 human pancreatic adenocarcinoma cell line and human pancreas tissue. PVDF membrane was probed with 0.2 µg/mL of Goat Anti-Human/Mouse/Rat Lipocalin-2/NGAL Antigen Affinity-purified Polyclonal Antibody (Catalog # AF1757) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # <a class=

HAF109). A specific band was detected for Lipocalin-2/NGAL at approximately 22 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1." alt="Western blot shows lysates of Capan-1 human pancreatic adenocarcinoma cell line and human pancreas tissue. PVDF membrane was probed with 0.2 µg/mL of Goat Anti-Human/Mouse/Rat Lipocalin-2/NGAL Antigen Affinity-purified Polyclonal Antibody (Catalog # AF1757) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF109). A specific band was detected for Lipocalin-2/NGAL at approximately 22 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1." class="big_thumb" />

HAF017). A specific band was detected for Lipocalin-2/NGAL at approximately 22 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1." class="big_lightbox">

Western blot shows lysates of mouse and rat bone marrow. PVDF membrane was probed with 0.2 µg/mL of Goat Anti-Human/Mouse/Rat Lipocalin-2/NGAL Antigen Affinity-purified Polyclonal Antibody (Catalog # AF1757) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # <a class=

HAF017). A specific band was detected for Lipocalin-2/NGAL at approximately 22 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1." class="big_thumb" />

HAF109). This experiment was conducted under reducing conditions and using the 12-230 kDa separation system." class="big_lightbox">

Simple Western lane view shows lysates of Capan-1 human pancreatic adenocarcinoma cell line, loaded at 0.2 mg/mL. A specific band was detected for Lipocalin-2/NGAL at approximately 34 kDa (as indicated) using 2 µg/mL of Goat Anti-Human/Mouse/Rat Lipocalin-2/NGAL Antigen Affinity-purified Polyclonal Antibody (Catalog # AF1757) followed by 1:50 dilution of HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # <a class=

HAF109). This experiment was conducted under reducing conditions and using the 12-230 kDa separation system." class="big_thumb" />

Enhanced expression of antimicrobial effectors by HO53 and HO56 stimulation in BCi cells. Samples were collected after 24 h (black bars) and 48 h (grey bars) post stimulation with Entinostat (10 μM), HO53 (75 μM) and HO56 (75 μM). Followed by expression analysis at mRNA and protein level by qRT-PCR and ELISA/Western blot, respectively. (a) Expression of LCN2 (lipocalin 2) at mRNA and (b) protein (lipocalin 2, NGAL) level in cell lysates. The representative Western blot is selected from one of the 3 independent experiments. GAPDH was used as a loading control. Full-length blots are presented in Supplementary Figure S10b. (c) Fold change of HBD1 (human beta -defensin 1) mRNA in comparison to control (Ctrl) and (d) secretion of hBD-1 peptide measured by ELISA in cell culture supernatants. (e) S100A8 expression was analyzed by qRT-PCR. TUBB (tubulin-beta ) was the reference gene in qRT-PCR. Each bar represents mean value of 3 independent experiments ± SEM; statistical significance was calculated in comparison to the control group using two-way ANOVA with Dunnett’s multiple comparisons test; *p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001. Significant changes are highlighted. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31068616), licensed under a CC-BY license. Not internally tested by R&D Systems.

VC004). Before incubation with the primary antibody, tissue was subjected to heat-induced epitope retrieval using VisUCyte Antigen Retrieval Reagent-Basic (Catalog # VCTS021). Tissue was stained using DAB (brown) and counterstained with hematoxylin (blue). Specific staining was localized to the cytoplasm. View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections." class="big_lightbox">

Lipocalin‑2/NGAL was detected in immersion fixed paraffin-embedded sections of human pancreas using Goat Anti-Human/Mouse/Rat Lipocalin‑2/NGAL Antigen Affinity-purified Polyclonal Antibody (Catalog # af1757) at 5 µg/ml for 1 hour at room temperature followed by incubation with the Anti-Goat IgG VisUCyte™ HRP Polymer Antibody (Catalog # <a class=

VC004). Before incubation with the primary antibody, tissue was subjected to heat-induced epitope retrieval using VisUCyte Antigen Retrieval Reagent-Basic (Catalog # VCTS021). Tissue was stained using DAB (brown) and counterstained with hematoxylin (blue). Specific staining was localized to the cytoplasm. View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections." class="big_thumb" />

LCN2 expression in pancreatic neoplastic lesions and PDAC cell lines.(A) The LCN2 immunostaining pattern for normal (n = 31), PanIN1 (n = 22), PanIN-2 (n = 13), PanIN -3 and PDAC (n = 82). Mean scores and the SEM for LCN2 immunostaining are noted below the sections. (B) LCN2 gene expression was examined in 21 different PDAC cell lines. Relative expression was normalized using loading controls and then normalized to the H6c7 ratio. (C) Representative immunoblots of LCN2 and GAPDH protein expression in PDAC cell lines. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/23056397), licensed under a CC-BY license. Not internally tested by R&D Systems.

The knockdown and overexpression of LCN2 expression in PDAC cell lines.(A) LCN2 mRNA expression was suppressed using three different retroviral shRNA constructs (KD) in H6c7KrT cells. (B) Representative immunoblots of LCN2 protein expression in H6c7KrT cells, where GAPDH was used as a loading control. (C) LCN2 expression was downregulated in BxPC3 and HPAF-II cells. In PANC1 cells LCN2 was overexpressed by a lentiviral expression construct. (D) Representative immunoblots of LCN2 protein expression in BxPC3, HPAF-II, and PANC1 cells. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/23056397), licensed under a CC-BY license. Not internally tested by R&D Systems.

LCN2 promotes adhesion, invasion, and gemcitabine resistance in PDAC cells.Adhesion assays on the (A) H6c7 KrT, (B) BxPC3, HPAF-II, and PANC1 cell lines. Fold changes were calculated by comparing the KD to NS or LCN2 to EV (n = 3). The fold changes in invasive ability were calculated by comparing the effects of the shRNA constructs against the NS control, or LCN2 overexpression compared to the EV control. Invasive ability was assessed in (C) H6c7KrT cells (n = 3), (D) BxPC3, HPAF-II, and PANC1 cells (n = 6) were seeded onto Matrigel or collagen IV coated membranes. To assess MMP-9 activity gelatin zymography was performed on the conditioned media from (E) H6c7 KrT cells, (F) BxPC3, HPAF-II, and PANC1 cell lines (n = 3). (G) PI exclusion assays for cell death (n = 6) and (H) immunoblot analysis after 72 hours treatment by gemcitabine on the BxPC3, HPAF-II, and PANC1 cell lines (n = 3). (Gem., gemcitabine; C3, caspase 3; CC3, cleaved caspase 3; * denotes significant differences between the test and control samples student t-tests or one-way ANOVA and Bonferroni’s post hoc tests where appropriate.). Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/23056397), licensed under a CC-BY license. Not internally tested by R&D Systems.

LCN2 promotes resistance to gemcitabine and angiogenesis.Effect of gemcitabine on the growth of tumors formed by (A) BxPC3-NS and –LCN2KD2 cell lines and (B) with PANC1-EV and –LCN2 cell lines [*denotes significance between vehicle treated cell lines (n = 10 per group, p<0.0001, mixed model multiple regression) †denotes significance between vehicle and gemcitabine treated mice injected with BxPC3 LCN2KD2 (n = 10 per group, p = 0.0003, mixed model multiple regression)]. (C) Protein lysates isolated from BxPC3 and PANC1 xenografts were assayed for caspase-3 cleavage after gemcitabine treatment (n = 10). (D) Representative histological images of xenografts formed by BxPC3 NS and –LCN2KD2, and PANC1-EV and –LCN2 cells after H&E, and immunostaining for LCN2, Ki67, and murine CD31. (E) Vascular density in five hot spots at high magnification in the BxPC3 NS and –LCN2KD2, and PANC1-EV and –LCN2 xenografts. The mRNA expression of (F) HIF1A and (G) VEGF in the BxPC3 and PANC1 xenografts. Gene expression was compared between KD and NS, or LCN2 and EV. [*denotes significance between KD and NS, or LCN2 and EV (n = 20; p<0.05, student t-test)]. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/23056397), licensed under a CC-BY license. Not internally tested by R&D Systems.

IL-6-specific up-regulation of LCN2 is dependent on NF-kappa B activation in human CRC cells(A) After stimulation with 50 ng/ml IL-6 for the indicated time, cytosolic and nuclear extracts of DLD-1 cells were prepared and used to determine the translocation of p65 from the cytosol to the nucleus. Actin and lamin B were used as loading controls. (B) After transfection with LCN2 siRNA, DLD-1 cells were stimulated with 50 ng/ml IL-6. Then the level of LCN2 in the cytosol and p65 in the nucleus were analyzed by Western blotting. Actin and lamin B were used as loading controls. (C) The cells were stimulated after transfection with p65 siRNA, then the levels of LCN2 and p65 were analyzed by Western blotting (upper panel). Cells were stimulated with IL-6 after pretreatment with PT and BAY11-7082 (NF-kappa B-specific inhibitor). Then, the levels of LCN2 and p65 were detected using Western blot analysis (lower panel). Actin was used as a loading control. All images are representatives from at least three independent experiments. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35470375), licensed under a CC-BY license. Not internally tested by R&D Systems.

IL-6 specifically up-regulated LCN2 protein and mRNA levels in human CRC cells(A,B) After stimulation with IL-6, protein and mRNA of DLD-1 cells were isolated. Then, Western blotting and reverse-transcriptase PCR were performed. The top images are Western blots and lower images are reverse-transcriptase PCR. (C) Human CRC cell lines, SW480 and HT-29, were stimulated with 50 ng/ml IL-6 for 24 h, then the levels of LCN2 protein and mRNA were detected. All images are representatives from at least three independent experiments. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35470375), licensed under a CC-BY license. Not internally tested by R&D Systems.

ADAM8 and LCN2 levels correlate in Panc89- and MB-231-derived extracellular vesicles (EV). Representative Western blots (A) of EVs derived from either Panc89 hA8 WT or KO cells, and cell lysate (CL) of Panc89 hA8 WT cells, and (B) of EVs derived from either MB-231 hA8 WT or MB-231 KO cells show the detection of ADAM8, MMP-9, LCN2, and Flotillin-1 in the upper part. Diagrams below illustrate the quantification and downregulation of LCN2 secretion (relative to Flotillin-1 secretion) in EVs isolated from Panc89 (hA8 WT or hA8 KO 1) or MB-231 (hA8 WT or hA8 KO) cells (n = 3). Data are presented as mean values ± S.D. ** p < 0.01. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35216088), licensed under a CC-BY license. Not internally tested by R&D Systems.

Co-culture of THP1-derived macrophages with Panc89 hA8 WT and KO cells. (A) The schematic model depicts the interactions of THP1-derived macrophages (green, M0) and Panc89 cells with or without ADAM8 (red). Created with BioRender.com. (B) ADAM8 mRNA expression in both Panc89 hA8 WT and KO is not affected by M0, whereas LCN2 mRNA expression. Data are presented as mean values ± S.D. *** p < 0.001. (C) is upregulated after co-culture in an ADAM8-dependent manner. Data are presented as mean values ± S.D. *** p < 0.001. (D) The graph illustrates the upregulation of MMP-9 mRNA expression in both Panc89 hA8 WT and KO after co-culture (n = 2). Data are presented as mean values ± S.D. *** p < 0.001. (E) Representative immunoblot shows the detection of ADAM8, MMP-9, and LCN2 with or without co-culture. In addition to the qPCR results, MMP-9 and LCN2 are upregulated after co-culture at the protein level (n = 2). (F) Representative zymography of Panc89 hA8 WT and KO cells with or without co-culture demonstrates less active MMP-9 in Panc89 hA8 KO cells than in Panc89 hA8 WT cells after co-culture. (G) Quantification of active MMP-9 refers to total MMP-9 in zymography of Panc89 hA8 WT and KO cells after co-culture (n = 2). Data are presented as mean values ± S.D. * p < 0.05. Representative images of Panc89 cells before and after co-culture are shown in (H); scale bar, 100 μm. After co-culture, morphological changes are visible in both Panc89 hA8 WT and KO cells. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35216088), licensed under a CC-BY license. Not internally tested by R&D Systems.

IL-6-induced LCN2 regulates cell survival and anti-apoptotic molecules mediated by the NF-kB/STAT3 pathway(A) After transfection with p65, STAT3 and LCN2 siRNA, DLD-1 cells were stimulated with 50 ng/ml IL-6 for 24 h, total extracts of DLD-1 cells were prepared and used to determine the phosphorylation of PI3k/AKT/mTOR. Actin was used as a loading control. (B) Total extracts prepared by the same methods were analyzed to determine the protein levels that are target gene products of STAT3 and NF-kB. Actin was used as a loading control. All images are representatives from at least three independent experiments. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35470375), licensed under a CC-BY license. Not internally tested by R&D Systems.

Downstream signaling of EGFR is affected by ADAM8 KO in Panc89 cells. (A) Representative immunoblot of EGFR and MAPK phosphorylation, and LCN2 expression after treatment with recombinant LCN2 (rLCN2) and recombinant transforming growth factor-alpha (rTGF-alpha ) for 1 h. (B) Quantification of LCN2 shows the downregulation of LCN2 expression in Panc89 hA8 KO cells. The addition of rLCN2 does not increase LCN2 expression in Panc89 hA8 KO cells, whereas rTGF-alpha alone or combined with rLCN2 adjusts LCN2 expression to Panc89 hA8 WT levels. (C) Quantification of p-EGFR illustrates no significant changes in EGFR phosphorylation of Panc89 hA8 KO compared to Panc89 hA8 WT cells. (D) The diagram displays the quantification of p-MAPK. The phosphorylation of MAPK is significantly downregulated in Panc89 hA8 KO cells. rTGF-alpha stimulation decreases MAPK phosphorylation in both Panc89 hA WT and KO cells. Data are presented as mean values ± S.D. * p < 0.05, ** p < 0.01 (n = 2). Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35216088), licensed under a CC-BY license. Not internally tested by R&D Systems.

Co-culture of THP1-derived and polarized macrophages with Panc89 hA8 WT and KO cells. (A) Western blot illustrates the detection of ADAM8, MMP-9, and LCN2 in Panc89 hA8 WT and KO control cells (Ø) and after co-culture with M0, M1, and M2 macrophages (two time points: 0 h and 1 h). ADAM8 is upregulated in Panc89 hA8 WT cells after co-culture with M2-polarized macrophages. Panc89 cells show the highest MMP-9 expression after co-culture with M0, but M1 macrophages also upregulate MMP-9. LCN2 is dependent on ADAM8 when upregulated in Panc89 cells after co-culture with M0 and M2 macrophages but independent of ADAM8 in Panc89 cells co-cultured with M1 macrophages. (B) ADAM8, (C) MMP-9, and (D) LCN2 ELISA of Panc89 hA8 WT and KO cell-derived supernatants of control cells and after co-culture with M0, M1, and M2 (two time points: 0 h and 1 h). In accordance with the immunoblot results of (A), ADAM8 is upregulated in supernatants derived from Panc89 hA8 WT cells after co-culture with M2 macrophages (B). At the same time, macrophages increase MMP-9 secretion from an undetectable level to almost 80,000 pg/mL in Panc89 hA8 WT and 60,000 pg/mL in Panc89 hA8 KO cells. M1 and M2 macrophages increase MMP-9 secretion of Panc89 independent of ADAM8, but not as high as in Panc89 cells co-cultured with M0. In contrast, LCN2 is upregulated in Panc89 hA8 WT cells by M0 and M1, but not by M2 macrophages. In the absence of ADAM8, Panc89 hA8 KO cells show low LCN2 secretion in control cells and after co-culture with M0 and M2 macrophages. Only after co-culture with M1 macrophages is the LCN2 secretion level increased (n = 1). Data are presented as mean values ± S.D. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35216088), licensed under a CC-BY license. Not internally tested by R&D Systems.

ADAM8 regulates LCN2 levels in tumor cell lines MB-231 and Panc89. The Human Protease/Protease Inhibitory Array demonstrates downregulation of ADAM8 (A), MMP-9 (B), and LCN2 (C) in supernatants derived from MB-231 hA8 KO cells. (D) mRNA expression and (E) representative Western blot of LCN2 in MB-231 hA8 WT and hA8 KO cells confirm results from (C) (n = 2). (F) mRNA expression and (G) representative Western blot of LCN2 in Panc89 hA8 WT, KO 1, and KO 2 cells demonstrate decreased LCN2 expression in hA8 KO cells (n = 2). Data are presented as mean values ± S.D., ** p < 0.01, *** p < 0.001. (H) Recombinant LCN2 (1 ng, 10 ng, 100 ng) does not affect protease activity of recombinant ADAM8 using a CD23 substrate (PepDAB# 13). Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35216088), licensed under a CC-BY license. Not internally tested by R&D Systems.

IL-6-specific up-regulation of LCN2 is dependent on STAT3 activation in human CRC cells(A) After stimulation with 50 ng/ml IL-6 for the indicated time, cytosolic and nuclear extracts of DLD-1 cells were prepared and used to determine the translocation of p-STAT3. Actin and lamin B were used as loading controls. (B) After transfection with LCN2 siRNA, DLD-1 cells were stimulated with 50 ng/ml IL-6. Then the level of LCN2 in cytosol and p-STAT3 in the nucleus were analyzed by Western blotting. Actin and lamin B were used as loading controls. (C) The cells were stimulated after transfection with STAT3 siRNA, then the level of LCN2 and p-STAT3 were analyzed by Western blotting (upper panel). After pretreatment with 5 μM stattic (STAT3-specific inhibitor), the cells were stimulated with IL-6. Then, the level of LCN2 and p-STAT3 were detected using Western blotting analysis (lower panel). Actin was used as a loading control. All images are representatives from at least three independent experiments. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35470375), licensed under a CC-BY license. Not internally tested by R&D Systems.

The expression of LCN2 was specifically induced in colon tissue of AOM/DSS-induced CAC mouse models The mice were given 7.4 mg/kg body weight of AOM and 3% DSS and subsequently killed (normal = 10, AOM/DSS = 12 mice). (A) Macroscopic appearance was captured for detecting tumor formation in the colon. (B) H&E staining (magnification ×10) of colonic mucosal tissue sections from mice were photographed using microscopy (upper panel). Colon length and body weight were statistically analyzed (lower panel). Data shown are presented as the mean ± SE. **P<0.01 versus control and CAC group. (C) After homogenizing colonic tissues, levels of LCN2 in tissue were detected by ELISA as described in the ‘Materials and methods’ section. Data shown are presented as the mean ± SE. **P<0.01 versus the control and CAC groups. (D) Total tissue extracts were prepared after killing and analyzed using LCN2 and actin antibody by Western blotting. Actin was used as a loading control. (E) IHC images of LCN2 expression in the colonic tissues from control and CAC mice are shown and the positively binding cells are shown in brown. The numbers of positive cells in the tumor samples were counted. Values represent means ± SEs. ***P<0.001 vs. the normal group. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35470375), licensed under a CC-BY license. Not internally tested by R&D Systems.

1757-LC) was serially diluted and captured by Rat Anti-Human Lipocalin‑2/NGAL Monoclonal Antibody (Catalog # MAB17571) coated on a Clear Polystyrene Microplate (Catalog # DY990). Goat Anti-Human/Mouse/Rat Lipocalin‑2/NGAL Antigen Affinity-purified Polyclonal Antibody (Catalog # AF1757) was biotinylated and incubated with the protein captured on the plate. Detection of the standard curve was achieved by incubating Streptavidin-HRP (Catalog # DY998)" class="big_lightbox">

Recombinant Human Lipocalin‑2/NGAL (Catalog # <a class=

1757-LC) was serially diluted and captured by Rat Anti-Human Lipocalin‑2/NGAL Monoclonal Antibody (Catalog # MAB17571) coated on a Clear Polystyrene Microplate (Catalog # DY990). Goat Anti-Human/Mouse/Rat Lipocalin‑2/NGAL Antigen Affinity-purified Polyclonal Antibody (Catalog # AF1757) was biotinylated and incubated with the protein captured on the plate. Detection of the standard curve was achieved by incubating Streptavidin-HRP (Catalog # DY998)" class="big_thumb" />

Reactivity:

Hu, Mu, Rt

Species Glossary

Reactivity: Hu, Mu, Rt

Applications:

, ,

Applications: , ,

Host:

Goat Polyclonal

Host: Goat Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	AF1757U-100UG
Alexa Fluor 405	AF1757V-100UG
Alexa Fluor 488	AF1757G-100UG
Alexa Fluor 532	AF1757X-100UG
Alexa Fluor 594	AF1757T-100UG
Alexa Fluor 647	AF1757R-100UG
Alexa Fluor 700	AF1757N-100UG
Alexa Fluor 750	AF1757S-100UG
Alexa Fluor Plus 405	AF1757AFP405-100UG
Alexa Fluor Plus 488	AF1757AFP488-100UG
Alexa Fluor Plus 555	AF1757AFP555-100UG
Alexa Fluor Plus 594	AF1757AFP594-100UG
Alexa Fluor Plus 647	AF1757AFP647-100UG
Alexa Fluor Plus 680	AF1757AFP680-100UG
Allophycocyanin	AF1757A
Biotin	BAF1757
CoraFluor 1	AF1757CL1
DyLight 350	AF1757D
DyLight 405	AF1757E
DyLight 488	AF1757K
DyLight 550	AF1757L
DyLight 594	AF1757M
DyLight 650	AF1757W
DyLight 680	AF1757Y
DyLight 755	AF1757Z
FITC	AF1757F
HRP	AF1757H
Janelia Fluor 525	AF1757JF525
Janelia Fluor 549	AF1757I
Janelia Fluor 646	AF1757J
Janelia Fluor 669	AF1757JF669
PE	AF1757P
PerCP	AF1757C
mFluor Violet 450 SE	AF1757MFV450
mFluor Violet 500 SE	AF1757MFV500
mFluor Violet 610 SE	AF1757MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
Carrier Free	AF1757-SP

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DY1757

Human Lipocalin-2/NGAL DuoSet ELISA, 15 Plate

(41 Publications)

1 Kit (for 5 Plates)

DY1757

Reactivity:

Hu

Species Glossary

Reactivity: Hu

Applications:

Applications:

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AF3508

Lipocalin-2/NGAL Antibody [Unconjugated]

(1 Review)

(14 Publications)

100 μg

AF3508

HAF019). A specific band was detected for Lipocalin-2/NGAL at approximately 25 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 8." class="big_lightbox">

Western blot shows lysates of rat ovary tissue and mouse lung tissue. PVDF membrane was probed with 1 µg/mL of Mouse/Rat Lipocalin-2/NGAL Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3508) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # <a class=

HAF019). A specific band was detected for Lipocalin-2/NGAL at approximately 25 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 8." alt="Western blot shows lysates of rat ovary tissue and mouse lung tissue. PVDF membrane was probed with 1 µg/mL of Mouse/Rat Lipocalin-2/NGAL Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3508) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF019). A specific band was detected for Lipocalin-2/NGAL at approximately 25 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 8." class="big_thumb" />

Visualization of expression of selected proteins by Western blot analysis. Protein extracts were prepared from livers of WT and Lcn2-/- mice that were subjected to indicated diets for 4 or 6 weeks (n=3 animals/group). Antibodies used are mentioned in the Section 2. GAPDH was used as the loading control. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28725667), licensed under a CC-BY license. Not internally tested by R&D Systems.

Increased LCN2 expression in Esr1-deficient ovaries. Ovaries from wild-type (WT, n = 8) and Esr1 null mice (n = 6) were dissected and either embedded in paraffin or prepared for RNA analysis. (A) Hematoxylin and eosin (H & E) staining showed characteristic histological changes in Esr1-deficient compared to WT ovaries. (B) Immunohistochemical staining for LCN2 and ER alpha was performed. Sections were counterstained with hematoxylin (LCN2) or methyl green (ER alpha ). Magnifications: 100×, 400×; scale bars: 100 µm, 50 µm. (C) Tissue samples were subjected to immunofluorescence double staining for LCN2 and STAR. Magnifications: 100×; scale bars: 100 µm. (D) Lcn2 and Star expression was analyzed in ovarian tissues using RT-qPCR. Data are displayed as means ± SD. In case of normal distribution, Student’s t-tests were chosen for statistical analysis, otherwise a Mann–Whitney test was performed. Significant differences between groups are marked with asterisks: *** p < 0.001. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/37298232), licensed under a CC-BY license. Not internally tested by R&D Systems.

LCN2 and ER alpha expression in the lung and kidney. Tissues from wild-type (WT, female: n = 9, male: n = 8) and Esr1 knockout (female: n = 6, male: n = 8) mice were either embedded in paraffin for immunostaining or processed for protein analysis. Immunohistochemistry staining was performed to localize LCN2 expression in (A) lung and (C) kidney tissue. Isotope-specific negative control IgG staining was performed to document antibody specificity. Magnifications: 100×; scale bar: 100 µm. LCN2 and ER alpha protein expression was analyzed in (B) lung and (D) kidney tissues by Western blot analysis in WT and Esr1 null mice. The expression of GAPDH (lungs) and vinculin (kidneys) was used to demonstrate equal protein loading. Unspecific bands are marked with asterisks (*) and are separated from specific bands by dashed lines. Protein expression of LCN2 was quantified densitometrically and plotted relative to the expression of the loading control. Mann–Whitney test (lungs) or Student’s t-tests (kidney) was used for statistical analysis. Significant differences between groups are indicated with asterisks: * p < 0.05. Data are displayed as means ± SD and non-significant results are marked with ns. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/37298232), licensed under a CC-BY license. Not internally tested by R&D Systems.

3508-LC) was serially diluted and captured by Goat Anti-Rat Lipocalin‑2/NGAL Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3508) coated on a Clear Polystyrene Microplate (Catalog # DY990). Goat Anti-Rat Lipocalin‑2/NGAL Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3508) was biotinylated and incubated with the protein captured on the plate. Detection of the standard curve was achieved by incubating Streptavidin-HRP (Catalog # DY998)" class="big_lightbox">

Recombinant Rat Lipocalin‑2/NGAL (Catalog # <a class=

3508-LC) was serially diluted and captured by Goat Anti-Rat Lipocalin‑2/NGAL Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3508) coated on a Clear Polystyrene Microplate (Catalog # DY990). Goat Anti-Rat Lipocalin‑2/NGAL Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3508) was biotinylated and incubated with the protein captured on the plate. Detection of the standard curve was achieved by incubating Streptavidin-HRP (Catalog # DY998)" class="big_thumb" />

3508-LC) was serially diluted and captured by Goat Anti-Rat Lipocalin‑2/NGAL Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3508) coated on a Clear Polystyrene Microplate (Catalog # DY990). Goat Anti-Rat Lipocalin‑2/NGAL Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3508) was biotinylated and incubated with the protein captured on the plate. Detection of the standard curve was achieved by incubating Streptavidin-HRP (Catalog # DY998)" class="big_lightbox">

3508-LC) was serially diluted and captured by Goat Anti-Rat Lipocalin‑2/NGAL Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3508) coated on a Clear Polystyrene Microplate (Catalog # DY990). Goat Anti-Rat Lipocalin‑2/NGAL Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3508) was biotinylated and incubated with the protein captured on the plate. Detection of the standard curve was achieved by incubating Streptavidin-HRP (Catalog # DY998)" class="big_thumb" />

Reactivity:

Rt

Species Glossary

Reactivity: Rt

Applications:

, ,

Applications: , ,

Host:

Goat Polyclonal

Host: Goat Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	AF3508U-100UG
Alexa Fluor 405	AF3508V-100UG
Alexa Fluor 488	AF3508G-100UG
Alexa Fluor 532	AF3508X-100UG
Alexa Fluor 594	AF3508T-100UG
Alexa Fluor 647	AF3508R-100UG
Alexa Fluor 700	AF3508N-100UG
Alexa Fluor 750	AF3508S-100UG
Alexa Fluor Plus 405	AF3508AFP405-100UG
Alexa Fluor Plus 488	AF3508AFP488-100UG
Alexa Fluor Plus 555	AF3508AFP555-100UG
Alexa Fluor Plus 594	AF3508AFP594-100UG
Alexa Fluor Plus 647	AF3508AFP647-100UG
Alexa Fluor Plus 680	AF3508AFP680-100UG
Allophycocyanin	AF3508A
Biotin	BAF3508
CoraFluor 1	AF3508CL1
DyLight 350	AF3508D
DyLight 405	AF3508E
DyLight 488	AF3508K
DyLight 550	AF3508L
DyLight 594	AF3508M
DyLight 650	AF3508W
DyLight 680	AF3508Y
DyLight 755	AF3508Z
FITC	AF3508F
HRP	AF3508H
Janelia Fluor 525	AF3508JF525
Janelia Fluor 549	AF3508I
Janelia Fluor 646	AF3508J
Janelia Fluor 669	AF3508JF669
PE	AF3508P
PerCP	AF3508C
mFluor Violet 450 SE	AF3508MFV450
mFluor Violet 500 SE	AF3508MFV500
mFluor Violet 610 SE	AF3508MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
Carrier Free	AF3508-SP

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1757-LC

Recombinant Human Lipocalin-2/NGAL Protein, CF

(29 Publications)

50 μg

Reactivity:

Hu

Species Glossary

Reactivity: Hu

Applications:

Applications:

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1857-LC

Recombinant Mouse Lipocalin-2/NGAL Protein, CF

(29 Publications)

50 μg

Reactivity:

Mu

Species Glossary

Reactivity: Mu

Applications:

Applications:

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MAB1757

Lipocalin-2/NGAL Antibody (220310) [Unconjugated]

(22 Publications)

100 μg

MAB1757

HAF005). A specific band was detected for Lipocalin-2/NGAL at approximately 22 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1." class="big_lightbox">

Western blot shows lysates of K562 human chronic myelogenous leukemia cell line. PVDF membrane was probed with 1 µg/mL of Rat Anti-Human Lipocalin-2/NGAL Monoclonal Antibody (Catalog # MAB1757) followed by HRP-conjugated Anti-Rat IgG Secondary Antibody (Catalog # <a class=

HAF005). A specific band was detected for Lipocalin-2/NGAL at approximately 22 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1." alt="Western blot shows lysates of K562 human chronic myelogenous leukemia cell line. PVDF membrane was probed with 1 µg/mL of Rat Anti-Human Lipocalin-2/NGAL Monoclonal Antibody (Catalog # MAB1757) followed by HRP-conjugated Anti-Rat IgG Secondary Antibody (Catalog # HAF005). A specific band was detected for Lipocalin-2/NGAL at approximately 22 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1." class="big_thumb" />

CTS005) and counterstained with hematoxylin (blue). Specific staining was localized to plasma membrane of ductal cells. View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections." class="big_lightbox">

Lipocalin-2/NGAL was detected in immersion fixed paraffin-embedded sections of human pancreas using Rat Anti-Human Lipocalin-2/NGAL Monoclonal Antibody (Catalog # MAB1757) at 15 µg/mL overnight at 4 °C. Tissue was stained using the Anti-Rabbit HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # <a class=

CTS005) and counterstained with hematoxylin (blue). Specific staining was localized to plasma membrane of ductal cells. View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections." class="big_thumb" />

HAF005). A specific band was detected for Lipocalin-2/NGAL at approximately 22 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1." class="big_lightbox">

Western blot shows lysates of Capan-1 human pancreatic adenocarcinoma cell line, HT-29 human colon adenocarcinoma cell line, and human bone marrow tissue. PVDF membrane was probed with 0.2 µg/mL of Rat Anti-Human Lipocalin-2/NGAL Monoclonal Antibody (Catalog # MAB1757) followed by HRP-conjugated Anti-Rat IgG Secondary Antibody (Catalog # <a class=

HAF005). A specific band was detected for Lipocalin-2/NGAL at approximately 22 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1." class="big_thumb" />

Silencing of LCN2 impairs cell cycle‐associated proteins. (A) The top proteins downregulated in LCN2‐silenced cells compared with control cells after RPPA proteomic analysis. (B) Gene set enrichment analysis of RPPA data identified pathways that are enriched or downregulated in control vs LCN2‐silenced SUM149 cells. (C) STRING interaction network of predicted active kinases based on enrichment of kinase substrates and protein interactions identified using KEA. The confidence of the interaction is reflected by the edge thickness. Based on node distribution analysis, four central proteins were identified (MAPK1, MAPK8, RPS6KB1, and MTOR). (D) Silencing of LCN2 in SUM149 cells reduced pMEK and pERK expression. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/34342930), licensed under a CC-BY license. Not internally tested by R&D Systems.

LCN2 was highly expressed in tumors from patients with IBC. (A) High LCN2 expression was associated with shorter overall survival in a meta‐dataset of patients with non‐IBC. (B, C) LCN2 mRNA expression was higher in tumors from IBC patients vs non‐IBC patients in two independent breast cancer datasets [IBC World Consortium Dataset; GSE45582]. (D) LCN2 mRNA expression was higher in ER‐negative compared to ER+ samples IBC samples. (E) LCN2 mRNA expression was higher in more aggressive molecular subtypes, ERBB2+ and TNBC, compared to HR‐positive/HERBB2‐negative subtype. (F) LCN2‐high expression correlates with shorter overall survival in patients with IBC. (G) LCN2 mRNA expression was higher in IBC cell lines compared to non‐IBC cell lines. (H, I) LCN2 protein expression was higher in IBC cell lines compared to non‐IBC cell lines shown by (H) immunoblotting or (I) ELISA for secreted LCN2 in supernatants. Bar graphs indicate mean ± SEM from three independent experiments. graphpad prism software was used to obtain the P values, with Mann–Whitney tests used to compare two categories or one‐way analysis of variance to compare three or more categories. Black lines in each group (B–E, and G) indicate mean ± SD. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/34342930), licensed under a CC-BY license. Not internally tested by R&D Systems.

Reactivity:

Hu

Species Glossary

Reactivity: Hu

Applications:

,

Applications: ,

Host:

Rat Monoclonal

Host: Rat Monoclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	FAB1757U-100UG
Alexa Fluor 405	FAB1757V-100UG
Alexa Fluor 488	FAB1757G-100UG
Alexa Fluor 532	FAB1757X-100UG
Alexa Fluor 594	FAB1757T-100UG
Alexa Fluor 647	FAB1757R-100UG
Alexa Fluor 700	FAB1757N-100UG
Alexa Fluor 750	FAB1757S-100UG
Alexa Fluor Plus 405	FAB1757AFP405-100UG
Alexa Fluor Plus 488	FAB1757AFP488-100UG
Alexa Fluor Plus 555	FAB1757AFP555-100UG
Alexa Fluor Plus 594	FAB1757AFP594-100UG
Alexa Fluor Plus 647	FAB1757AFP647-100UG
Alexa Fluor Plus 680	FAB1757AFP680-100UG
Allophycocyanin	FAB1757A
Biotin	FAB1757B
CoraFluor 1	FAB1757CL1
DyLight 350	FAB1757D
DyLight 405	FAB1757E
DyLight 488	FAB1757K
DyLight 550	FAB1757L
DyLight 594	FAB1757M
DyLight 650	FAB1757W
DyLight 680	FAB1757Y
DyLight 755	FAB1757Z
FITC	FAB1757F
HRP	FAB1757H
Janelia Fluor 525	FAB1757JF525
Janelia Fluor 549	FAB1757I
Janelia Fluor 646	FAB1757J
Janelia Fluor 669	FAB1757JF669
PE	FAB1757P
PerCP	FAB1757C
mFluor Violet 450 SE	FAB1757MFV450
mFluor Violet 500 SE	FAB1757MFV500
mFluor Violet 610 SE	FAB1757MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
Carrier Free	MAB1757-SP
Carrier Free	MAB1757-500

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MAB1857

Lipocalin-2/NGAL Antibody (228418) [Unconjugated]

(21 Publications)

100 μg

MAB1857

HAF005). A specific band was detected for Lipocalin-2/NGAL at approximately 23 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1." class="big_lightbox">

Western blot shows lysates of mouse spleen tissue, mouse uterus tissue, and mouse epididymis tissue. PVDF membrane was probed with 0.5 µg/mL of Rat Anti-Mouse Lipocalin-2/NGAL Monoclonal Antibody (Catalog # MAB1857) followed by HRP-conjugated Anti-Rat IgG Secondary Antibody (Catalog # <a class=

HAF005). A specific band was detected for Lipocalin-2/NGAL at approximately 23 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1." alt="Western blot shows lysates of mouse spleen tissue, mouse uterus tissue, and mouse epididymis tissue. PVDF membrane was probed with 0.5 µg/mL of Rat Anti-Mouse Lipocalin-2/NGAL Monoclonal Antibody (Catalog # MAB1857) followed by HRP-conjugated Anti-Rat IgG Secondary Antibody (Catalog # HAF005). A specific band was detected for Lipocalin-2/NGAL at approximately 23 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1." class="big_thumb" />

Response of Low-FBS/+FGF2 Cultured Astrocytes to LPS+IFN-gamma Stimulation at the Protein Level(A) Representative western blot illustrating temporal induction of pSTAT3 upon 1 and 48 hr of treatment with LPS+IFN-gamma . (B and C) Representative western blots of activation markers in resting versus LPS+IFN-gamma -stimulated low-FBS astrocytes: (B) Lcn2 expression in resting and 24-hr-stimulated astrocytes; and (C) GFAP and Vim levels under resting conditions and following 48 hr of activation followed by 3 or 5 days of rest. beta -Actin was used as a loading control. (D) Representative immunofluorescence micrographs of GFAP, Vim, and Lcn2 immunoreactivity in resting and activated conditions (GFAP/Vim: green; Lcn2: red; DAPI nuclear stain: blue). Scale bars, 100 μm. (E) Secreted IL-6 as measured by ELISA, resting versus activated conditions, at 48 and 120 hr post-stimulation. Data are expressed as the mean of n ≥ 3 biological replicates ± SD. *p ≤ 0.05, relative to non-activated control samples (multiple t tests with statistical significance determined using the Holm-Sidak method, alpha = 0.05). Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/29499926), licensed under a CC-BY license. Not internally tested by R&D Systems.

1857-LC) was serially diluted and captured by Rat Anti-Mouse Lipocalin‑2/NGAL Monoclonal Antibody (Catalog # MAB18571) coated on a Clear Polystyrene Microplate (Catalog # DY990). Rat Anti-Mouse Lipocalin‑2/NGAL Monoclonal Antibody (Catalog # MAB1857) was biotinylated and incubated with the protein captured on the plate. Detection of the standard curve was achieved by incubating Streptavidin-HRP (Catalog # DY998)" class="big_lightbox">

Recombinant Mouse Lipocalin‑2/NGAL (Catalog # <a class=

1857-LC) was serially diluted and captured by Rat Anti-Mouse Lipocalin‑2/NGAL Monoclonal Antibody (Catalog # MAB18571) coated on a Clear Polystyrene Microplate (Catalog # DY990). Rat Anti-Mouse Lipocalin‑2/NGAL Monoclonal Antibody (Catalog # MAB1857) was biotinylated and incubated with the protein captured on the plate. Detection of the standard curve was achieved by incubating Streptavidin-HRP (Catalog # DY998)" class="big_thumb" />

Reactivity:

Mu

Species Glossary

Reactivity: Mu

Applications:

Applications:

Host:

Rat Monoclonal

Host: Rat Monoclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	FAB1857U-100UG
Alexa Fluor 405	FAB1857V-100UG
Alexa Fluor 488	FAB1857G-100UG
Alexa Fluor 532	FAB1857X-100UG
Alexa Fluor 594	FAB1857T-100UG
Alexa Fluor 647	FAB1857R-100UG
Alexa Fluor 700	FAB1857N-100UG
Alexa Fluor 750	FAB1857S-100UG
Alexa Fluor Plus 405	FAB1857AFP405-100UG
Alexa Fluor Plus 488	FAB1857AFP488-100UG
Alexa Fluor Plus 555	FAB1857AFP555-100UG
Alexa Fluor Plus 594	FAB1857AFP594-100UG
Alexa Fluor Plus 647	FAB1857AFP647-100UG
Alexa Fluor Plus 680	FAB1857AFP680-100UG
Allophycocyanin	FAB1857A
Biotin	BAM1857
CoraFluor 1	FAB1857CL1
DyLight 350	FAB1857D
DyLight 405	FAB1857E
DyLight 488	FAB1857K
DyLight 550	FAB1857L
DyLight 594	FAB1857M
DyLight 650	FAB1857W
DyLight 680	FAB1857Y
DyLight 755	FAB1857Z
FITC	FAB1857F
HRP	FAB1857H
Janelia Fluor 525	FAB1857JF525
Janelia Fluor 549	FAB1857I
Janelia Fluor 646	FAB1857J
Janelia Fluor 669	FAB1857JF669
PE	FAB1857P
PerCP	FAB1857C
mFluor Violet 450 SE	FAB1857MFV450
mFluor Violet 500 SE	FAB1857MFV500
mFluor Violet 610 SE	FAB1857MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
Carrier Free	MAB1857-SP
Carrier Free	MAB1857-500

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DY3508

Rat Lipocalin-2/NGAL DuoSet ELISA, 15 Plate

(20 Publications)

1 Kit (for 15 Plates)

DY3508

Reactivity:

Rt

Species Glossary

Reactivity: Rt

Applications:

Applications:

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At	=	A. thaliana	SyHa	=	Golden Syrian Hamster
All	=	All Species	Ha	=	Hamster
An	=	Animal	Hu	=	Human
ArHa	=	Armenian Hamster	I	=	Insect
Av	=	Avian	Ll	=	Llama
Bb	=	Baboon	Ma	=	Mammal
Ba	=	Bacteria	Mk	=	Monkey
Bv	=	Bovine	Mu	=	Mouse
Ca	=	Canine	Multi	=	Multi-species
Ce	=	C. Elegans	NA	=	Non-species specific
Ch	=	Chicken	Or	=	Orangutan
ChHa	=	Chinese Hamster	Pl	=	Plant
Cm	=	Cynomolgus Monkey	Pm	=	Primate
Do	=	Donkey	Po	=	Porcine
Dr	=	Drosophilia	Rb	=	Rabbit
Ec	=	E. Coli	Rt	=	Rat
Eq	=	Equine	RM	=	Rhesus Macaque
Fe	=	Feline	Sh	=	Sheep
Ft	=	Ferret	Vb	=	Vertebrate
Fi	=	Fish	Vi	=	Virus
Fu	=	Fungi	Xp	=	Xenopus
Ge	=	Gerbil	Ye	=	Yeast
GP	=	Guinea Pig	Ze	=	Zebrafish
Gt	=	Goat

Category

Protein/Target

Applications

Reactivity

Citation

Antibody Validation

Reviews

Host

Available Conjugates

Format

Modification

Clonality

Clone

Gene Symbol

Images Type

Isotype

Preservative

Protein Or Peptide

Research Areas

Has Sample Size

Promotional Item

Species Glossary

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Lipocalin-2/NGAL Antibody (228418) [Unconjugated]

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