Product Search for gapdh g3pdh: Novus Biologicals

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2275-PC-100

GAPDH Antibody [Unconjugated]

(111 Publications)

100 uL

2275-PC-100

Western blot shows lysates of U2OS human osteosarcoma cell line, A20 mouse B cell lymphoma cell line, and L6 rat myoblast cell line. PVDF membrane was probed with 0.1 µg/mL Rabbit Anti-Human/Mouse/Rat GAPDH Polyclonal Antibody (Catalog # 2275-PC) followed by HRP-conjugated Anti-Rabbit IgG Secondary Antibody (Catalog # HAF008). A specific band was detected for GAPDH at approximately 36 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.

Simple Western shows lysates of Exosome Standards (LNCaP) (NBP3-11687), Exosome Standards (HT‑29) (NBP3-11685) and Jurkat human acute T cell leukemia cell line, loaded at 0.5 mg/ml. A specific band was detected for GAPDH at approximately 41 kDa (as indicated) using 5 µg/mL of Rabbit Anti-Human/Mouse/Rat GAPDH Antigen Affinity-purified Polyclonal Antibody (Catalog # 2275-PC-100). This experiment was conducted under reducing conditions and using the 12-230kDa separation system.

Simple Western lane view shows lysates of Jurkat human acute T cell leukemia cell line, C2C12 mouse myoblast cell line, and C6 rat glioma cell line, loaded at 0.2 mg/mL. A specific band was detected for GAPDH at approximately 43 kDa (as indicated) using 1 µg/mL of Rabbit Anti-Human/Mouse/Rat GAPDH Antigen Affinity-purified Polyclonal Antibody (Catalog # 2275-PC-100) . This experiment was conducted under reducing conditions and using the 12-230 kDa separation system.

Higher levels of CD4 are found in macrophages expressing LCK.A) Schematic diagram of self-inactivating lentiviral construct used to express wild-type Lck and puroR (LCKWT P). A similar construct was used to express a kinase inactive form of Lck and puroR (LCKINACTIVE P) or to express puroR only (‘control P’). B) Detection of protein expression of LCK and CD4. Control and transgenic PSC-macrophages lysates were analysed by western blotting using anti-LCK and anti-CD4 antibodies. The loading control GAPDH was detected using anti-GAPDH antibody. C) Protein levels were measured with Odyssey software (Li-COR) and CD4 expression was normalised to GAPDH expression. Symbols represent normalised CD4 expression, relative to the PSC-macrophages control group, of two independent experiments. D) Detection of surface CD4 and total LCK expression. Representative two-colour immunofluorescence (dot plot) analysis is shown. Gates were determined by using the two relevant isotype control antibodies. Quantification of total LCK expression (E) and surface CD4 expression (F), expressed as the ratio of the geometric mean fluorescence intensity (MFI) over the isotype control ±SEM of independent experiments (n = 7). G) Detergent resistance of CD4, expressed as mean Flow Cytometric Detergent Resistance (FCDR) index of CD4 (n = 4) in PSC-macrophages, calculated as described in materials and methods. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/24465876), licensed under a CC-BY license. Not internally tested by R&D Systems.

CD4 knock-down in genetically modified stem cell-derived macrophages. C) Detection of protein expression of CD4. Control and transgenic PSC-macrophages lysates were analysed by western blotting using anti-CD4 antibodies. GAPDH, a loading control, was detected using anti-GAPDH antibody. Representative blot is shown. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/24465876), licensed under a CC-BY license. Not internally tested by R&D Systems.

Higher levels of CD4 are found in macrophages expressing LCK.A) Schematic diagram of self-inactivating lentiviral construct used to express wild-type Lck and puroR (LCKWT P). A similar construct was used to express a kinase inactive form of Lck and puroR (LCKINACTIVE P) or to express puroR only (‘control P’). B) Detection of protein expression of LCK and CD4. Control and transgenic PSC-macrophages lysates were analysed by western blotting using anti-LCK and anti-CD4 antibodies. The loading control GAPDH was detected using anti-GAPDH antibody. C) Protein levels were measured with Odyssey software (Li-COR) and CD4 expression was normalised to GAPDH expression. Symbols represent normalised CD4 expression, relative to the PSC-macrophages control group, of two independent experiments. D) Detection of surface CD4 and total LCK expression. Representative two-colour immunofluorescence (dot plot) analysis is shown. Gates were determined by using the two relevant isotype control antibodies. Quantification of total LCK expression (E) and surface CD4 expression (F), expressed as the ratio of the geometric mean fluorescence intensity (MFI) over the isotype control ±SEM of independent experiments (n = 7). G) Detergent resistance of CD4, expressed as mean Flow Cytometric Detergent Resistance (FCDR) index of CD4 (n = 4) in PSC-macrophages, calculated as described in materials and methods. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/24465876), licensed under a CC-BY license. Not internally tested by R&D Systems.

CD4 knock-down in genetically modified stem cell-derived macrophages.C) Detection of protein expression of CD4. Control and transgenic PSC-macrophages lysates were analysed by western blotting using anti-CD4 antibodies. GAPDH, a loading control, was detected using anti-GAPDH antibody. Representative blot is shown. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/24465876), licensed under a CC-BY license. Not internally tested by R&D Systems.

Higher levels of CD4 are found in macrophages expressing LCK.A) Schematic diagram of self-inactivating lentiviral construct used to express wild-type Lck and puroR (LCKWT P). A similar construct was used to express a kinase inactive form of Lck and puroR (LCKINACTIVE P) or to express puroR only (‘control P’). B) Detection of protein expression of LCK and CD4. Control and transgenic PSC-macrophages lysates were analysed by western blotting using anti-LCK and anti-CD4 antibodies. The loading control GAPDH was detected using anti-GAPDH antibody. C) Protein levels were measured with Odyssey software (Li-COR) and CD4 expression was normalised to GAPDH expression. Symbols represent normalised CD4 expression, relative to the PSC-macrophages control group, of two independent experiments. D) Detection of surface CD4 and total LCK expression. Representative two-colour immunofluorescence (dot plot) analysis is shown. Gates were determined by using the two relevant isotype control antibodies. Quantification of total LCK expression (E) and surface CD4 expression (F), expressed as the ratio of the geometric mean fluorescence intensity (MFI) over the isotype control ±SEM of independent experiments (n = 7). G) Detergent resistance of CD4, expressed as mean Flow Cytometric Detergent Resistance (FCDR) index of CD4 (n = 4) in PSC-macrophages, calculated as described in materials and methods. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/24465876), licensed under a CC-BY license. Not internally tested by R&D Systems.

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Hu, Mu, Rt

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Reactivity: Hu, Mu, Rt

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Rabbit Polyclonal

Host: Rabbit Polyclonal

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AF5718

GAPDH Antibody [Unconjugated]

(4 Reviews)

(64 Publications)

100 μg

AF5718

Western blot shows lysates of mouse, human, and rat brain tissue. PVDF membrane was probed with 1 µg/mL of Goat Anti-Human/Mouse/Rat GAPDH/G3PDH Antigen Affinity-purified Polyclonal Antibody (Catalog # AF5718) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF017). A specific band was detected for GAPDH/G3PDH at approximately 38 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 2.

GAPDH was detected in immersion fixed HeLa human cervical epithelial carcinoma cell line using Goat Anti-Human/Mouse/Rat GAPDH Antigen Affinity-purified Polyclonal Antibody (Catalog # AF5718) at 5 µg/mL for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Anti-Goat IgG Secondary Antibody (red; Catalog # NL001) and counterstained with DAPI (blue). View our protocol for Fluorescent ICC Staining of Cells on Coverslips.

GAPDH/G3PDH was detected in immersion fixed paraffin-embedded sections of normal human kidney using Goat Anti-Human/Mouse/Rat GAPDH/G3PDH Antigen Affinity-purified Polyclonal Antibody (Catalog # AF5718) at 8 µg/mL overnight at 4 °C. Tissue was stained using the Anti-Goat HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS008) and counterstained with hematoxylin (blue). Specific staining was localized to cytoplasm and nuclei of convoluted tubules. View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections.This application has not been tested in mouse or rat samples.

GAPDH was detected in immersion fixed paraffin-embedded sections of human prostate cancer tissue using Goat Anti-Human/Mouse/Rat GAPDH Antigen Affinity-purified Polyclonal Antibody (Catalog # AF5718) at 3 µg/mL for 1 hour at room temperature followed by incubation with the Anti-Goat IgG VisUCyte™ HRP Polymer Antibody (Catalog # VC004). Tissue was stained using DAB (brown) and counterstained with hematoxylin (blue). Specific staining was localized to cytoplasm and nuclei. View our protocol for IHC Staining with VisUCyte HRP Polymer Detection Reagents.

Simple Western lane view shows lysates of human brain (motor cortex) tissue and HepG2 human hepatocellular carcinoma cell line, loaded at 0.2 mg/mL. A specific band was detected for GAPDH at approximately 43 kDa (as indicated) using 10 µg/mL of Goat Anti-Human/Mouse/Rat GAPDH Antigen Affinity-purified Polyclonal Antibody (Catalog # AF5718) followed by 1:50 dilution of HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF109). This experiment was conducted under reducing conditions and using the 12-230 kDa separation system.

Role of Akt pathway in aliskiren's effects on attenuating collagen expression.A and B demonstrate the results of Western blotting for phospho- and total Akt in hearts of mice treated with various diets. C shows changes in the protein levels of collagen type I, phospho- and total Akt in response to 24 hours of exposure to D,L. Homocysteine (200 µmol/L) with or without pre-treatment with aliskiren 10 µmol/L (AL), wortmannin 1 µmol/L or Akt Inhibitor VIII 1 µmol/L. Hhe – Hhe-inducing diet; D,L, homocysteine (lower panel); AL 0.05– aliskiren 0.5 mg/kg/day; AL 5– aliskiren 5 mg/kg/day; AL 50– aliskiren 50 mg/kg/day; Wort – wortmannin; Akt in – Akt inhibitor VIII. *p<0.05; **p<0.01; and ***p<0.001. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/24349097), licensed under a CC-BY license. Not internally tested by R&D Systems.

Effect of prodigiosins on the mRNA and protein expression of HO-1 in gastric tissue.Data (means ± SEM of three assays) were normalized to the levels of GAPDH and expressed as fold induction (log2 scale), relative to the level of HO-1 in the control. aP < 0.05, significant difference vs. the health rats; bP < 0.05, significant difference vs. HCl/ethanol-induced rats, Duncan's post-hoc test. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31194753), licensed under a CC-BY license. Not internally tested by R&D Systems.

The DU145FP cells express higher levels of cancer stemness related genes. (A) Transcriptome analyses of prostate cancer stemness-related markers. The Log2 transformed ratio of FPKM values (e.g., FP/WT) are indicated by color-coded index bars. (B) Cells were stained with fluorophore conjugated monoclonal antibodies against CD44 and EPCAM, the antibody against integrin alpha 2 beta 3 without fluorophore conjugation was detected by using secondary antibody conjugated with fluorophore, and stained cells were analyzed by flow cytometry. The scatter plots and histograms show representative results. CTRL denote cell stained with isotype control antibody or only secondary antibody; ST denote cell stained with antibody against EPCAM and integrin alpha 2 beta 3; US denote unstained cells. (C) Immunoblotting confirmation of the protein expression of A-tubulin, GAPDH, SOX9, SLUG, HIF1A, HIF2A, CD44 and integrin alpha 2 beta 3. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28698547), licensed under a CC-BY license. Not internally tested by R&D Systems.

Effects of aliskiren on homocysteine-induced matrix expression in cultured cardiac fibroblasts.Fibroblasts were cultured in the presence or absence of D,L, homocysteine 200 µmol/L for 24 hours after pretreatment with varying concentrations of aliskiren (0.1–10 µmol/L). Real time PCR was done to measure relative expression of COLIA2 (alpha 2 chain of type I collagen; A) and COL3A1 (alpha 1 chain of type III collagen; B) genes. Figure 5C demonstrates the results of real time PCR to compare the effects of losartan and captopril with aliskiren on homocysteine induced expression of COL1A2 gene. Western blotting was conducted to measure the expression of collagen type I protein (D and E) Glyceraldehyde 3 phosphate dehydrogenase (GAPDH) was used as internal control. Hcy-D,L, homocysteine; AL-aliskiren; Los – losartan; and Cap – captopril. *p<0.05. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/24349097), licensed under a CC-BY license. Not internally tested by R&D Systems.

Role of Akt pathway in aliskiren's effects on attenuating collagen expression.A and B demonstrate the results of Western blotting for phospho- and total Akt in hearts of mice treated with various diets. C shows changes in the protein levels of collagen type I, phospho- and total Akt in response to 24 hours of exposure to D,L. Homocysteine (200 µmol/L) with or without pre-treatment with aliskiren 10 µmol/L (AL), wortmannin 1 µmol/L or Akt Inhibitor VIII 1 µmol/L. Hhe – Hhe-inducing diet; D,L, homocysteine (lower panel); AL 0.05– aliskiren 0.5 mg/kg/day; AL 5– aliskiren 5 mg/kg/day; AL 50– aliskiren 50 mg/kg/day; Wort – wortmannin; Akt in – Akt inhibitor VIII. *p<0.05; **p<0.01; and ***p<0.001. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/24349097), licensed under a CC-BY license. Not internally tested by R&D Systems.

Effects of aliskiren on myocardial matrix gene expression.Real time PCR was performed with ventricular tissue obtained from mice after 12-inducing diet and different doses of aliskiren. Figure 3A demonstrates changes in expression of COL1A1(alpha 1 chain of type I collagen) and 3B shows changes in COL1A2(alpha2 chain of type I collagen) genes. Lower right panels (3C and 3D) demonstrate the results of western blotting for collagen type I in various groups. Hhe – Hhe-inducing diet; AL 0.5– aliskiren 0.5 mg/kg/day; AL 5– aliskiren 5 mg/kg/day; and AL 50– aliskiren 50 mg/kg/day. * p<0.05; and *** p<0.001. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/24349097), licensed under a CC-BY license. Not internally tested by R&D Systems.

S. Typhimurium evades autophagy by disrupting Sirt1-dependent AMPK activation.(A) Immunofluorescence image of S. Typhimurium co-localization with LC3 in GFP-LC3 expressing BMDMs at indicated time points. Data shown are representative of 3 independent experiments (n = 3). (B) Immunoblot analysis of p62 and LC3 expression upon S. Typhimurium infection in BMDMs. (C) LC3 and p62 expression levels are quantified by densitometry analysis. Data shown are from 3 independent experiments. (D) Confocal image of macrophages stained for Sirt1 and LC3. (E) BMDMs stained for LC3 and AMPK upon S. Typhimurium infection. (F) Confocal image of macrophages stained for LKB1 and LC3. (G) Immunoblot analysis of Sirt1, AMPK and LKB1 in wild type (WT) and Atg7-deficient macrophages. (H) Densitometric analysis of Sirt1, AMPK and LKB1 immunoblots (n = 3). Bar graphs are expressed as mean ± SEM, ***p≤0.001, **p≤0.01 and *p≤0.05. Scale bar = 10μm for microscopical images. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28192515), licensed under a CC-BY license. Not internally tested by R&D Systems.

$S. Typhimurium mediated targeting of Sirt1 for lysosomal degradation is virulence dependent.Immunoblot analysis of ACC and LKB1 activation upon infection with delta ssrB(A) and delta ssaV(B) compared to S. Typhimurium. Sirt1 and acetylated-NF kappa B from macrophages infected with delta ssrB(C)and delta ssaV(D) compared to S. Typhimurium. (E) Expression of Sirt1 from cytoplasmic (C) and nuclear (N) fraction from BMDMs infected with delta ssrB. (F) Confocal image of Sirt1 and LysoTracker Red in delta ssrB-infected BMDMs. Sirt1-LysoTracker Red co-localization in untreated BMDMs infected with S. Typhimurium for 4h is shown for comparison (n = 3). (G) Immunoblot analysis of LC3 and p62. (H) Densitometric analysis of LC3 lipidation and p62 (n = 4). (I) Immunofluorescence image of delta ssrB-infected BMDMs stained for LC3 and LPS of S. Typhimurium (n = 3). (J) Quantitation of LC3 co-localization with SCVs. 100 SCVs were counted and expressed as percentage co-localization. (K) AKT, mTOR, p70S6K, NDRG1 expression upon S. Typhimurium (ST) and delta ssrB infection in BMDMs. (L) Densitometric analysis of AKT, mTOR, p70S6K and NDRG1 are shown from 3 independent experiments. Bar graphs are expressed as mean ± SEM, ***p≤0.001. Scale bar = 10μm for microscopical images. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28192515), licensed under a CC-BY license. Not internally tested by R&D Systems.$

S. Typhimurium evades autophagy by disrupting Sirt1-dependent AMPK activation.(A) Immunofluorescence image of S. Typhimurium co-localization with LC3 in GFP-LC3 expressing BMDMs at indicated time points. Data shown are representative of 3 independent experiments (n = 3). (B) Immunoblot analysis of p62 and LC3 expression upon S. Typhimurium infection in BMDMs. (C) LC3 and p62 expression levels are quantified by densitometry analysis. Data shown are from 3 independent experiments. (D) Confocal image of macrophages stained for Sirt1 and LC3. (E) BMDMs stained for LC3 and AMPK upon S. Typhimurium infection. (F) Confocal image of macrophages stained for LKB1 and LC3. (G) Immunoblot analysis of Sirt1, AMPK and LKB1 in wild type (WT) and Atg7-deficient macrophages. (H) Densitometric analysis of Sirt1, AMPK and LKB1 immunoblots (n = 3). Bar graphs are expressed as mean ± SEM, ***p≤0.001, **p≤0.01 and *p≤0.05. Scale bar = 10μm for microscopical images. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28192515), licensed under a CC-BY license. Not internally tested by R&D Systems.

$S. Typhimurium mediated targeting of Sirt1 for lysosomal degradation is virulence dependent.Immunoblot analysis of ACC and LKB1 activation upon infection with delta ssrB(A) and delta ssaV(B) compared to S. Typhimurium. Sirt1 and acetylated-NF kappa B from macrophages infected with delta ssrB(C)and delta ssaV(D) compared to S. Typhimurium. (E) Expression of Sirt1 from cytoplasmic (C) and nuclear (N) fraction from BMDMs infected with delta ssrB. (F) Confocal image of Sirt1 and LysoTracker Red in delta ssrB-infected BMDMs. Sirt1-LysoTracker Red co-localization in untreated BMDMs infected with S. Typhimurium for 4h is shown for comparison (n = 3). (G) Immunoblot analysis of LC3 and p62. (H) Densitometric analysis of LC3 lipidation and p62 (n = 4). (I) Immunofluorescence image of delta ssrB-infected BMDMs stained for LC3 and LPS of S. Typhimurium (n = 3). (J) Quantitation of LC3 co-localization with SCVs. 100 SCVs were counted and expressed as percentage co-localization. (K) AKT, mTOR, p70S6K, NDRG1 expression upon S. Typhimurium (ST) and delta ssrB infection in BMDMs. (L) Densitometric analysis of AKT, mTOR, p70S6K and NDRG1 are shown from 3 independent experiments. Bar graphs are expressed as mean ± SEM, ***p≤0.001. Scale bar = 10μm for microscopical images. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28192515), licensed under a CC-BY license. Not internally tested by R&D Systems.$

$S. Typhimurium mediated targeting of Sirt1 for lysosomal degradation is virulence dependent.Immunoblot analysis of ACC and LKB1 activation upon infection with delta ssrB(A) and delta ssaV(B) compared to S. Typhimurium. Sirt1 and acetylated-NF kappa B from macrophages infected with delta ssrB(C)and delta ssaV(D) compared to S. Typhimurium. (E) Expression of Sirt1 from cytoplasmic (C) and nuclear (N) fraction from BMDMs infected with delta ssrB. (F) Confocal image of Sirt1 and LysoTracker Red in delta ssrB-infected BMDMs. Sirt1-LysoTracker Red co-localization in untreated BMDMs infected with S. Typhimurium for 4h is shown for comparison (n = 3). (G) Immunoblot analysis of LC3 and p62. (H) Densitometric analysis of LC3 lipidation and p62 (n = 4). (I) Immunofluorescence image of delta ssrB-infected BMDMs stained for LC3 and LPS of S. Typhimurium (n = 3). (J) Quantitation of LC3 co-localization with SCVs. 100 SCVs were counted and expressed as percentage co-localization. (K) AKT, mTOR, p70S6K, NDRG1 expression upon S. Typhimurium (ST) and delta ssrB infection in BMDMs. (L) Densitometric analysis of AKT, mTOR, p70S6K and NDRG1 are shown from 3 independent experiments. Bar graphs are expressed as mean ± SEM, ***p≤0.001. Scale bar = 10μm for microscopical images. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28192515), licensed under a CC-BY license. Not internally tested by R&D Systems.$

$S. Typhimurium mediated targeting of Sirt1 for lysosomal degradation is virulence dependent.Immunoblot analysis of ACC and LKB1 activation upon infection with delta ssrB(A) and delta ssaV(B) compared to S. Typhimurium. Sirt1 and acetylated-NF kappa B from macrophages infected with delta ssrB(C)and delta ssaV(D) compared to S. Typhimurium. (E) Expression of Sirt1 from cytoplasmic (C) and nuclear (N) fraction from BMDMs infected with delta ssrB. (F) Confocal image of Sirt1 and LysoTracker Red in delta ssrB-infected BMDMs. Sirt1-LysoTracker Red co-localization in untreated BMDMs infected with S. Typhimurium for 4h is shown for comparison (n = 3). (G) Immunoblot analysis of LC3 and p62. (H) Densitometric analysis of LC3 lipidation and p62 (n = 4). (I) Immunofluorescence image of delta ssrB-infected BMDMs stained for LC3 and LPS of S. Typhimurium (n = 3). (J) Quantitation of LC3 co-localization with SCVs. 100 SCVs were counted and expressed as percentage co-localization. (K) AKT, mTOR, p70S6K, NDRG1 expression upon S. Typhimurium (ST) and delta ssrB infection in BMDMs. (L) Densitometric analysis of AKT, mTOR, p70S6K and NDRG1 are shown from 3 independent experiments. Bar graphs are expressed as mean ± SEM, ***p≤0.001. Scale bar = 10μm for microscopical images. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28192515), licensed under a CC-BY license. Not internally tested by R&D Systems.$

S. Typhimurium evades autophagy by disrupting Sirt1-dependent AMPK activation.(A) Immunofluorescence image of S. Typhimurium co-localization with LC3 in GFP-LC3 expressing BMDMs at indicated time points. Data shown are representative of 3 independent experiments (n = 3). (B) Immunoblot analysis of p62 and LC3 expression upon S. Typhimurium infection in BMDMs. (C) LC3 and p62 expression levels are quantified by densitometry analysis. Data shown are from 3 independent experiments. (D) Confocal image of macrophages stained for Sirt1 and LC3. (E) BMDMs stained for LC3 and AMPK upon S. Typhimurium infection. (F) Confocal image of macrophages stained for LKB1 and LC3. (G) Immunoblot analysis of Sirt1, AMPK and LKB1 in wild type (WT) and Atg7-deficient macrophages. (H) Densitometric analysis of Sirt1, AMPK and LKB1 immunoblots (n = 3). Bar graphs are expressed as mean ± SEM, ***p≤0.001, **p≤0.01 and *p≤0.05. Scale bar = 10μm for microscopical images. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28192515), licensed under a CC-BY license. Not internally tested by R&D Systems.

$S. Typhimurium mediated targeting of Sirt1 for lysosomal degradation is virulence dependent.Immunoblot analysis of ACC and LKB1 activation upon infection with delta ssrB(A) and delta ssaV(B) compared to S. Typhimurium. Sirt1 and acetylated-NF kappa B from macrophages infected with delta ssrB(C)and delta ssaV(D) compared to S. Typhimurium. (E) Expression of Sirt1 from cytoplasmic (C) and nuclear (N) fraction from BMDMs infected with delta ssrB. (F) Confocal image of Sirt1 and LysoTracker Red in delta ssrB-infected BMDMs. Sirt1-LysoTracker Red co-localization in untreated BMDMs infected with S. Typhimurium for 4h is shown for comparison (n = 3). (G) Immunoblot analysis of LC3 and p62. (H) Densitometric analysis of LC3 lipidation and p62 (n = 4). (I) Immunofluorescence image of delta ssrB-infected BMDMs stained for LC3 and LPS of S. Typhimurium (n = 3). (J) Quantitation of LC3 co-localization with SCVs. 100 SCVs were counted and expressed as percentage co-localization. (K) AKT, mTOR, p70S6K, NDRG1 expression upon S. Typhimurium (ST) and delta ssrB infection in BMDMs. (L) Densitometric analysis of AKT, mTOR, p70S6K and NDRG1 are shown from 3 independent experiments. Bar graphs are expressed as mean ± SEM, ***p≤0.001. Scale bar = 10μm for microscopical images. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28192515), licensed under a CC-BY license. Not internally tested by R&D Systems.$

$S. Typhimurium mediated targeting of Sirt1 for lysosomal degradation is virulence dependent.Immunoblot analysis of ACC and LKB1 activation upon infection with delta ssrB(A) and delta ssaV(B) compared to S. Typhimurium. Sirt1 and acetylated-NF kappa B from macrophages infected with delta ssrB(C)and delta ssaV(D) compared to S. Typhimurium. (E) Expression of Sirt1 from cytoplasmic (C) and nuclear (N) fraction from BMDMs infected with delta ssrB. (F) Confocal image of Sirt1 and LysoTracker Red in delta ssrB-infected BMDMs. Sirt1-LysoTracker Red co-localization in untreated BMDMs infected with S. Typhimurium for 4h is shown for comparison (n = 3). (G) Immunoblot analysis of LC3 and p62. (H) Densitometric analysis of LC3 lipidation and p62 (n = 4). (I) Immunofluorescence image of delta ssrB-infected BMDMs stained for LC3 and LPS of S. Typhimurium (n = 3). (J) Quantitation of LC3 co-localization with SCVs. 100 SCVs were counted and expressed as percentage co-localization. (K) AKT, mTOR, p70S6K, NDRG1 expression upon S. Typhimurium (ST) and delta ssrB infection in BMDMs. (L) Densitometric analysis of AKT, mTOR, p70S6K and NDRG1 are shown from 3 independent experiments. Bar graphs are expressed as mean ± SEM, ***p≤0.001. Scale bar = 10μm for microscopical images. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28192515), licensed under a CC-BY license. Not internally tested by R&D Systems.$

$S. Typhimurium mediated targeting of Sirt1 for lysosomal degradation is virulence dependent.Immunoblot analysis of ACC and LKB1 activation upon infection with delta ssrB(A) and delta ssaV(B) compared to S. Typhimurium. Sirt1 and acetylated-NF kappa B from macrophages infected with delta ssrB(C)and delta ssaV(D) compared to S. Typhimurium. (E) Expression of Sirt1 from cytoplasmic (C) and nuclear (N) fraction from BMDMs infected with delta ssrB. (F) Confocal image of Sirt1 and LysoTracker Red in delta ssrB-infected BMDMs. Sirt1-LysoTracker Red co-localization in untreated BMDMs infected with S. Typhimurium for 4h is shown for comparison (n = 3). (G) Immunoblot analysis of LC3 and p62. (H) Densitometric analysis of LC3 lipidation and p62 (n = 4). (I) Immunofluorescence image of delta ssrB-infected BMDMs stained for LC3 and LPS of S. Typhimurium (n = 3). (J) Quantitation of LC3 co-localization with SCVs. 100 SCVs were counted and expressed as percentage co-localization. (K) AKT, mTOR, p70S6K, NDRG1 expression upon S. Typhimurium (ST) and delta ssrB infection in BMDMs. (L) Densitometric analysis of AKT, mTOR, p70S6K and NDRG1 are shown from 3 independent experiments. Bar graphs are expressed as mean ± SEM, ***p≤0.001. Scale bar = 10μm for microscopical images. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28192515), licensed under a CC-BY license. Not internally tested by R&D Systems.$

CD44bright cells are mainly positive for ABCG2, Oct3/4 and Nanog.(A) Double staining of CD44 and ABCG2 surface markers with flow cytometry assay shows higher levels expressions of these factors in both cell lines under hypoxia for 48 hours. (B) The CD44bright cells under normoxia express higher levels of ABCG2, Oct3/4 and Nanog, but the CD44dim cells under the same normoxia condition express very low levels of these factors. The CD44bright cells pretreated under 1% O2 for 48 hours show even higher levels of these factors compared to the CD44bright cells cultivated under normoxia. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/22216200), licensed under a CC-BY license. Not internally tested by R&D Systems.

Evaluation of ZL-2201 antiproliferative activity in vitro. A, Chemical structure of ZL-2201, a potent and selective DNA-PK inhibitor. B, Concentration-dependent response to ZL-2201 in M059J and M059K glioblastoma cancer cells measured by CTG after 6-day of treatment. The graph represents the average inhibitory (IC50) values (n = 3). C, Concentration-dependent response to ZL-2201 in CRISPR KO of ATM in A549 and FaDu cancer cells measured by CTG after 6 days of treatment. The graph represents the average inhibitory (IC50) values (n = 2–5). D, IC50 responses to ZL-2201 in ATM mutant cell lines (black bars) versus ATM WT A549 cell line (gray bar). Cell growth was measured by CTG after 6 days of treatment. The graph represents the average inhibitory (IC50) values (n = 2–6). NCI-H1703 (E) and A549 (F) cancer cells were treated with bleomycin (10 μmol/L) for 2 hours followed by the addition of increasing concentration of ZL-2201 for 2 hours. Whole-cell lysates were harvested, and concentration-dependent inhibition of DNA-PK protein were analyzed by Simple Western. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/37663435), licensed under a CC-BY license. Not internally tested by R&D Systems.

Phenotypic evaluation of ZL-2201 synergy with various DNA-damaging agents. C, NCI-H1703 cells treated with ZL-2201 (0.1, 0.3, 0.5, 1,&3.6 μmol/L)&a low dose of doxorubicin (0.006 μmol/L) for 2 hours. Whole-cell lysates harvested,&Simple Western was used to show the inhibition of pDNA-PK upon combination treatment of ZL-2201 with doxorubicin. Image collected & cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/37663435), licensed under a CC-BY license. Not internally tested by R&D Systems.

Evaluation of ZL-2201 antiproliferative activity in vitro. A, Chemical structure of ZL-2201, a potent and selective DNA-PK inhibitor. B, Concentration-dependent response to ZL-2201 in M059J and M059K glioblastoma cancer cells measured by CTG after 6-day of treatment. The graph represents the average inhibitory (IC50) values (n = 3). C, Concentration-dependent response to ZL-2201 in CRISPR KO of ATM in A549 and FaDu cancer cells measured by CTG after 6 days of treatment. The graph represents the average inhibitory (IC50) values (n = 2–5). D, IC50 responses to ZL-2201 in ATM mutant cell lines (black bars) versus ATM WT A549 cell line (gray bar). Cell growth was measured by CTG after 6 days of treatment. The graph represents the average inhibitory (IC50) values (n = 2–6). NCI-H1703 (E) and A549 (F) cancer cells were treated with bleomycin (10 μmol/L) for 2 hours followed by the addition of increasing concentration of ZL-2201 for 2 hours. Whole-cell lysates were harvested, and concentration-dependent inhibition of DNA-PK protein were analyzed by Simple Western. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/37663435), licensed under a CC-BY license. Not internally tested by R&D Systems.

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	AF5718U-100UG
Alexa Fluor 405	AF5718V-100UG
Alexa Fluor 488	AF5718G-100UG
Alexa Fluor 532	AF5718X-100UG
Alexa Fluor 594	AF5718T-100UG
Alexa Fluor 647	AF5718R-100UG
Alexa Fluor 700	AF5718N-100UG
Alexa Fluor 750	AF5718S-100UG
Allophycocyanin	AF5718A
Biotin	AF5718B
CoraFluor 1	AF5718CL1
DyLight 350	AF5718D
DyLight 405	AF5718E
DyLight 488	AF5718K
DyLight 550	AF5718L
DyLight 594	AF5718M
DyLight 650	AF5718W
DyLight 680	AF5718Y
DyLight 755	AF5718Z
FITC	AF5718F
HRP	AF5718H
Janelia Fluor 525	AF5718JF525
Janelia Fluor 549	AF5718I
Janelia Fluor 646	AF5718J
Janelia Fluor 669	AF5718JF669
PE	AF5718P
PerCP	AF5718C
mFluor Violet 450 SE	AF5718MFV450
mFluor Violet 500 SE	AF5718MFV500
mFluor Violet 610 SE	AF5718MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
Carrier Free	AF5718-SP

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MAB5718

GAPDH Antibody (686613) [Unconjugated]

(1 Review)

(43 Publications)

100 μg

MAB5718

Western blot shows lysates of human brain tissue, mouse brain tissue, and rat brain tissue. PVDF Membrane was probed with 0.05 µg/mL of Mouse Anti-Human/Mouse/Rat GAPDH/G3PDH Monoclonal Antibody (Catalog # MAB5718) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF007). A specific band was detected for GAPDH/G3PDH at approximately 39 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 2.

GAPDH was detected in immersion fixed HeLa human cervical epithelial carcinoma cell line using Mouse Anti-Human/Mouse/Rat GAPDH Monoclonal Antibody (Catalog # MAB5718) at 8 µg/mL for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Anti-Mouse IgG Secondary Antibody (red; Catalog # NL007) and counterstained with DAPI (blue). View our protocol for Fluorescent ICC Staining of Cells on Coverslips.

GAPDH/G3PDH was detected in immersion fixed paraffin-embedded sections of human kidney using Mouse Anti-Human/Mouse/Rat GAPDH/G3PDH Monoclonal Antibody (Catalog # MAB5718) at 15 µg/mL overnight at 4 °C. Before incubation with the primary antibody, tissue was subjected to heat-induced epitope retrieval using Antigen Retrieval Reagent-Basic (Catalog # CTS013). Tissue was stained using the Anti-Mouse HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS002) and counterstained with hematoxylin (blue). Specific staining was localized to cytoplasm and nuclei. View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections.

Simple Western lane view shows lysates of Jurkat human acute T cell leukemia cell line and C2C12 mouse myoblast cell line, loaded at 0.2 mg/mL. A specific band was detected for GAPDH/G3PDH at approximately 41 kDa (as indicated) using 0.25 µg/mL of Mouse Anti-Human/Mouse/Rat GAPDH/G3PDH Monoclonal Antibody (Catalog # MAB5718). This experiment was conducted under reducing conditions and using the12-230 kDa separation system.

Simple Western lane view shows lysates of Jurkat human acute T cell leukemia cell line, HeLa human cervical epithelial carcinoma cell line, C2C12 mouse myoblast cell line, and C6 rat glioma cell line, loaded at 0.2 mg/mL. A specific band was detected for GAPDH at approximately 42 kDa (as indicated) using 1 µg/mL of Mouse Anti-Human/Mouse/Rat GAPDH Monoclonal Antibody (Catalog # MAB5718) . This experiment was conducted under reducing conditions and using the 12-230 kDa separation system.

Simultaneous knockdown of multiple genes in primary human islets following electroporation. (A) Graph shows RT-qPCR results of islets electroporated with non-targeting control siRNA or siRNA targeting RB and p130 (L-003299). (B) Graph shows RT-qPCR results of islets electroporated with non-targeted control siRNA or siRNAs targeting the indicated gene products. The housekeeping gene GAPDH was used as the control. Representative experiment shown from 3 separate experiments. Error bars indicate standard deviation. (C) Western blot for RB protein in human islet lysates after electroporation of control or targeting siRNA. GAPDH was used as a loading control. RB appears as a characteristic doublet representing the hypo and hyperphosphorylated protein. Representative experiment shown from 3 different experiments. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/25305068), licensed under a CC-BY license. Not internally tested by R&D Systems.

Evaluation of CPP/mRNA-mediated protein expression. (A) Representative fluorescence images and a quantitative graph showing mCherry-positive CT26.CL25 cells 24 h after treatment with CPP/mCherry mRNA complexes (6.8 nM). Scale bar: 275 μm. Data are presented as the mean ± SD (n = 3). (B) Representative flow cytometry histograms and graphs of EGFP-positive CL26.CL25 cells transfected with CPP/EGFP mRNA complexes (6.8 nM). Data are presented as the mean ± SD (n = 3). (C) Western blot analysis of the expression levels of OVA and GAPDH in CT26.CL25 cells. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35745843), licensed under a CC-BY license. Not internally tested by R&D Systems.

Evaluation of CPP/mRNA-mediated protein expression. (A) Representative fluorescence images and a quantitative graph showing mCherry-positive CT26.CL25 cells 24 h after treatment with CPP/mCherry mRNA complexes (6.8 nM). Scale bar: 275 μm. Data are presented as the mean ± SD (n = 3). (B) Representative flow cytometry histograms and graphs of EGFP-positive CL26.CL25 cells transfected with CPP/EGFP mRNA complexes (6.8 nM). Data are presented as the mean ± SD (n = 3). (C) Western blot analysis of the expression levels of OVA and GAPDH in CT26.CL25 cells. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35745843), licensed under a CC-BY license. Not internally tested by R&D Systems.

Molecular effect of intraluminal chloride and GsMTx4 in smooth muscle cells. a-c Upper panel represents the main cumulative effect of intraluminal chloride concentration ([Cl−]) and medium supplementation with and without GsMTx4. a Examples of representative blots are shown. b, c Protein expression levels for b myosin light chain 2 (MLC2), and c alpha-smooth muscle actin ( alpha -SMA) are quantified. d–f Lower panel shows the additional effect of PIEZO1/2 inhibition after intraluminal injection of Cl− channels inhibitors: cystic fibrosis transmembrane conductance regulator inhibitor172 (CFTRinh) to CFTR and; calcium-dependent Cl− channel inhibitor A01 (CaCCinh) to CaCCs. d Examples of representative blots are shown. e–f Relative expression levels of e MLC2, and f alpha -SMA are displayed. 143 mM Cl− and standard solution (SS) represent the control condition for [Cl−] and Cl− channels inhibitors, respectively. White and dotted rectangles represent the medium supplementation with and without GsMTx4, respectively. Each lane represents a pooled-tissue sample, and the relative expression levels were determined against GAPDH. n ≥ 4 were used per antibody/condition. Results are presented as mean ± SD. Symbols indicate the main effects and non-redundant interactions of the two-way ANOVA. p < alpha 0.0001, beta 0.001, gamma 0.01, µ0.05 Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/36740669), licensed under a CC-BY license. Not internally tested by R&D Systems.

Molecular effect of intraluminal chloride and GsMTx4 in smooth muscle cells. a-c Upper panel represents the main cumulative effect of intraluminal chloride concentration ([Cl−]) and medium supplementation with and without GsMTx4. a Examples of representative blots are shown. b, c Protein expression levels for b myosin light chain 2 (MLC2), and c alpha-smooth muscle actin ( alpha -SMA) are quantified. d–f Lower panel shows the additional effect of PIEZO1/2 inhibition after intraluminal injection of Cl− channels inhibitors: cystic fibrosis transmembrane conductance regulator inhibitor172 (CFTRinh) to CFTR and; calcium-dependent Cl− channel inhibitor A01 (CaCCinh) to CaCCs. d Examples of representative blots are shown. e–f Relative expression levels of e MLC2, and f alpha -SMA are displayed. 143 mM Cl− and standard solution (SS) represent the control condition for [Cl−] and Cl− channels inhibitors, respectively. White and dotted rectangles represent the medium supplementation with and without GsMTx4, respectively. Each lane represents a pooled-tissue sample, and the relative expression levels were determined against GAPDH. n ≥ 4 were used per antibody/condition. Results are presented as mean ± SD. Symbols indicate the main effects and non-redundant interactions of the two-way ANOVA. p < alpha 0.0001, beta 0.001, gamma 0.01, µ0.05 Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/36740669), licensed under a CC-BY license. Not internally tested by R&D Systems.

The impact of combination therapy on protein and gene expression in SJSA-1 osteosarcoma cells. (A) A Western blot analysis illustrating the effects of the combination treatment on key proteins involved in metastasis, cell survival, and apoptosis in SJSA-1 osteosarcoma cells. The expression levels of MMP9 and MMP13, which facilitate tumor cell invasion and metastasis through ECM degradation, were significantly reduced, indicating a potential inhibitory effect of the combination therapy on metastatic progression. Additionally, phosphorylated AKT (pAKT), a central regulator of the PI3K/AKT pathway associated with cell survival and chemoresistance, and runt-related transcription factor 2 (RUNX2), a critical modulator of osteosarcoma progression and tumor aggressiveness, were both downregulated, suggesting the suppression of key oncogenic pathways. Conversely, apoptotic markers, including cleaved caspase-8, cleaved caspase-3, and total caspase-3, exhibited increased activation following treatment, indicating enhanced apoptotic signaling. GAPDH was used as a loading control to ensure equal protein loading across samples. (B) A densitometric analysis of the Western blot bands representing the expression levels of target proteins after 48 h of treatment. The band intensities were quantified using Image Lab software (Version 6.1.0 build 7) and normalized to the GAPDH. Relative protein expression levels are expressed as a fold change compared to the untreated control group. The data represent the mean ± the standard deviation from two independent experiments. (C) qRT-PCR analyzed the gene expression of the apoptosis-related markers p16 and p53 following treatment. The results highlight the upregulation of p16 and stable expression of p53 in treated cells. (* p < 0.05 and ** p < 0.01). Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/40332124), licensed under a CC-BY license. Not internally tested by R&D Systems.

Reactivity:

Hu, Mu, Rt

Species Glossary

Reactivity: Hu, Mu, Rt

Applications:

, , ,

Applications: , , ,

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	FAB5718U-100UG
Alexa Fluor 405	FAB5718V-100UG
Alexa Fluor 488	FAB5718G-100UG
Alexa Fluor 532	FAB5718X-100UG
Alexa Fluor 594	FAB5718T-100UG
Alexa Fluor 647	FAB5718R-100UG
Alexa Fluor 700	FAB5718N-100UG
Alexa Fluor 750	FAB5718S-100UG
Allophycocyanin	FAB5718A
Biotin	FAB5718B
CoraFluor 1	FAB5718CL1
DyLight 350	FAB5718D
DyLight 405	FAB5718E
DyLight 488	FAB5718K
DyLight 550	FAB5718L
DyLight 594	FAB5718M
DyLight 650	FAB5718W
DyLight 680	FAB5718Y
DyLight 755	FAB5718Z
FITC	FAB5718F
HRP	FAB5718H
Janelia Fluor 525	FAB5718JF525
Janelia Fluor 549	FAB5718I
Janelia Fluor 646	FAB5718J
Janelia Fluor 669	FAB5718JF669
PE	FAB5718P
PerCP	FAB5718C
mFluor Violet 450 SE	FAB5718MFV450
mFluor Violet 500 SE	FAB5718MFV500
mFluor Violet 610 SE	FAB5718MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
Carrier Free	MAB5718-SP

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DYC5718-2

Human/Mouse/Rat Total GAPDH DuoSet IC ELISA, 2 Plate

(2 Publications)

1 Kit (for 2 Plates)

DYC5718-2

ELISA GAPDH [Biotin]

Reactivity:

Hu, Mu, Rt

Species Glossary

Reactivity: Hu, Mu, Rt

Applications:

Applications:

Conjugate	Catalog #	Availability	Size	Price
Biotin	DYC5718-5

Available Formulations

Formulation	Catalog #	Availability	Price
Carrier Free	DYC5718-5

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AF6276

GAPDH-2 Antibody

100 μg

AF6276

Western blot shows lysates of human testis tissue. PVDF Membrane was probed with 1 µg/mL of Goat Anti-Human GAPDH-2 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF6276) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF109). A specific band was detected for GAPDH-2 at approximately 56 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.

GAPDH-2 was detected in immersion fixed paraffin-embedded sections of human testes using Goat Anti-Human GAPDH-2 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF6276) at 3 µg/mL overnight at 4 °C. Before incubation with the primary antibody, tissue was subjected to heat-induced epitope retrieval using Antigen Retrieval Reagent-Basic (Catalog # CTS013). Tissue was stained using the Anti-Goat HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS008) and counterstained with hematoxylin (blue). Specific staining was localized to cytoplasm of sperm cells. View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections.

Reactivity:

Hu

Species Glossary

Reactivity: Hu

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	AF6276U-100UG
Alexa Fluor 405	AF6276V-100UG
Alexa Fluor 488	AF6276G-100UG
Alexa Fluor 532	AF6276X-100UG
Alexa Fluor 594	AF6276T-100UG
Alexa Fluor 647	AF6276R-100UG
Alexa Fluor 700	AF6276N-100UG
Alexa Fluor 750	AF6276S-100UG
Allophycocyanin	AF6276A
Biotin	AF6276B
CoraFluor 1	AF6276CL1
DyLight 350	AF6276D
DyLight 405	AF6276E
DyLight 488	AF6276K
DyLight 550	AF6276L
DyLight 594	AF6276M
DyLight 650	AF6276W
DyLight 680	AF6276Y
DyLight 755	AF6276Z
FITC	AF6276F
HRP	AF6276H
Janelia Fluor 525	AF6276JF525
Janelia Fluor 549	AF6276I
Janelia Fluor 646	AF6276J
Janelia Fluor 669	AF6276JF669
PE	AF6276P
PerCP	AF6276C
mFluor Violet 450 SE	AF6276MFV450
mFluor Violet 500 SE	AF6276MFV500
mFluor Violet 610 SE	AF6276MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
Carrier Free	AF6276-SP

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