Anti gapdh clone d16h11

Manufactured by Cell Signaling Technology

Sourced in United States

Anti-GAPDH (clone D16H11) is a primary antibody that specifically recognizes the GAPDH (Glyceraldehyde-3-Phosphate Dehydrogenase) protein. GAPDH is a ubiquitous enzyme involved in the glycolytic pathway. This antibody can be used to detect and quantify GAPDH expression in various cell and tissue samples.

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Lab products found in correlation

Anti flag clone m2, by Merck Group (2 mentions) Anti syk clone d1i5q, by Cell Signaling Technology (2 mentions) Anti bclaf1 antibody a300 608a, by Fortis Life Sciences (2 mentions) Anti pu 1 pa5 17505, by Thermo Fisher Scientific (2 mentions) Hrp conjugated anti mouse igg, by Cell Signaling Technology (2 mentions) Ecl prime, by GE Healthcare (2 mentions) Anti akt clone c67e7, by Cell Signaling Technology (1 mentions) Anti ar clone d6f11, by Cell Signaling Technology (1 mentions) Enzalutamide, by Selleck Chemicals (1 mentions) Cell counter, by Bio-Rad (1 mentions) Anti cyclin e2, by Cell Signaling Technology (1 mentions) Propidium iodide, by Merck Group (1 mentions) Facsverse, by BD (1 mentions) G csf, by Thermo Fisher Scientific (1 mentions) Gm csf, by Thermo Fisher Scientific (1 mentions) Hrp conjugated goat anti rabbit igg, by Thermo Fisher Scientific (1 mentions) Ccl3 mip 1α, by Merck Group (1 mentions) Anti gcsf, by R&D Systems (1 mentions) Interleukin 2 (il 2), by Merck Group (1 mentions) Tnf α, by Thermo Fisher Scientific (1 mentions)

Spelling variants of this product

GAPDH (5572 citations) Anti-GAPDH (1707 citations) GAPDH (D16H11) (66 citations) Anti-GAPDH (D16H11, (22 citations) GAPDH (clone D16H11, (6 citations) Clone D16H11 (4 citations)

6 protocols using anti gapdh clone d16h11

Western Blot Analysis of Cellular Proteins

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Western blots were done on whole cell lysates (Bednarski et al., 2016 (link)). Anti-SYK (clone D1I5Q)
and anti-GAPDH (clone D16H11) antibodies were from Cell Signaling
Technology. Anti-BCLAF1 antibody (A300–608A) was from Bethyl
Laboratories. Anti-PU.1 (PA5–17505) was from Thermo Fisher
Scientific. Anti-FLAG (clone M2) was from Sigma. Secondary reagents were
horseradish peroxidase (HRP)-conjugated anti-mouse IgG (Cell Signaling;
catalog # 7076) or anti-rabbit IgG (Cell Signaling; catalog # 7074).
Westerns were developed with ECL (Pierce) and ECL Prime (GE Healthcare).

Soodgupta D., White L.S., Yang W., Johnston R., Andrews J.M., Kohyama M., Murphy K.M., Mosammaparast N., Payton J.E, & Bednarski J.J. (2019). RAG-Mediated DNA Breaks Attenuate PU.1 Activity in Early B Cells through Activation of a SPIC-BCLAF1 Complex. Cell reports, 29(4), 829-843.e5.

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Western Blot Analysis of Prostate Cancer Markers

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Anti-AKT (clone C67E7, #4691P, 1:1,000), anti-phospo-S473-AKT (clone D9E, #4060P, 1:1,000), anti-AR (clone D6F11, #5153, 1:2,000), anti-HDAC1 (clone 10E2, #5356, 1:2,000), anti-γH2AX (clone 20E3, #9718, 1:2,000), anti-actin (clone 8H10D10, #3700, 1:4,000), anti-γErbB2 (clone Tyr1248, #2247, 1:1,000), and anti-GAPDH (clone D16H11, #5174, 1:4,000–7,500) were from Cell Signalling Technology (Beverly, MA). Anti-HER2 (clone e2–4001, #MS730P0, 1:2,000) and anti-ER (clone AB-17, #RB1521PO, 1:1,500) were from Thermo Fisher (Waltham, MA). Anti-γDNP-PKcs (clone S2056, #18192, 1:1,000 was from Abcam (Cambridge, MA). Enzalutamide was from Selleck (Houston, TX). DHT was from Steraloids (Newport, RI).

Yard B.D., Adams D.J., Chie E.K., Tamayo P., Battaglia J.S., Gopal P., Rogacki K., Pearson B.E., Phillips J., Raymond D.P., Pennell N.A., Almeida F., Cheah J.H., Clemons P.A., Shamji A., Peacock C.D., Schreiber S.L., Hammerman P.S, & Abazeed M.E. (2016). A genetic basis for the variation in the vulnerability of cancer to DNA damage. Nature Communications, 7, 11428.

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Cell Cycle Regulation in SKBR3 Breast Cancer

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SKBR3-WT and -KO cells were plated in 96-well plates at 1000 cells/well. Cell growth rates were monitored using a Cell Counter (BioRad, CA, USA) for 7 days. For cell cycle analysis, cells were grown to 70–80% confluency, treated with RNase A, stained with propidium iodide (Sigma-Aldrich, MO, USA) and then subjected to flow cytometry with BD FACS Verse, and cell cycle distribution was calculated using the FlowJo 10. Immunoblotting was used to analyze the expression levels of cell cycle regulators in SKBR3-KO and SKBR3-WT. Rabbit anti-human primary antibodies were obtained from Cell Signaling Technology (CST, MA, USA), including anti-Cyclin D1(clone 92G2, #2978), anti-Cyclin E2(#4132), anti-CDK2(clone 78B2, #2546), anti-CDK4(clone D9G3E, #12,790), anti-p27(clone D69C12, #3686) and anti-GAPDH (clone D16H11, #5174) antibodies.

Zhou L., Wu J., Ruan M., Xiao Y., Lan H., Wu Q., Yu C.W, & Zhang Q. (2023). The loss of B7-H4 expression in breast cancer cells escaping from T cell cytotoxicity contributes to epithelial-to-mesenchymal transition. Breast Cancer Research : BCR, 25, 115.

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Cytokine Profiling for Immune Modulation

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CCL3 (MIP-1α) and IL-2 were purchased from Millipore (Billerica, MA, USA). Monoclonal antibodies anti-Stat3 (clone: 79D7), anti-phospho-Stat3 (Tyr705) (clone: D3A7), and anti-GAPDH (clone: D16H11) were purchased from Cell Signaling Technology (Beverly, MA). Ly6G mAb (clone 1A8) was from BioExpress. Mouse IL-18 binding protein (IL-18BP) was from BIOHJ Corporation (USA). Anti-NKG2D (MI-6), anti-NKp46 (29A1.4) and anti-G-CSF antibodies were from R&D Systems. G-CSF, GM-CSF, IL-6, and TNF-α were from PeproTech (Rocky Hill, NJ). STAT3 inhibitor (FLLL32) was from Selleck. Rabbit anti-DX5 (clone EPR5788), anti-PD-L1 (clone EPR20529), and anti-PD-1 (clone J43) antibodies were from Abcam. Rabbit anti-mouse CCR1 (clone PA1–41062) and HRP-conjugated Goat anti-Rabbit IgG were from ThermoFisher Scientific. PE-conjugated anti-mouse IFN-γ (clone XMG1.2), PE-conjugated anti-mouse PD-L1 (clone MIH5), PE-conjugated anti-mouse PD-1 (clone RMP1–30) and PE-conjugated anti-mouse DX5 were from eBioscience (San Diego, CA).

Sun R., Xiong Y., Liu H., Gao C., Su L., Weng J., Yuan X., Zhang D, & Feng J. (2020). Tumor-associated neutrophils suppress antitumor immunity of NK cells through the PD-L1/PD-1 axis. Translational Oncology, 13(10), 100825.

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Comprehensive Protein Analysis by Western Blot

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Total proteins were separated by electrophoresis on 4–20% gradient PAGE gels (Bio‐Rad, 4561093) and transferred onto nitrocellulose membrane. The following antibodies were used: anti‐phosphoAKT (Ser473) (Cell Signaling, 9271S), anti‐AKT (Cell Signaling, 9272S), anti‐phosphoCREB (Ser133) (Millipore, aa77‐343), anti‐phosphoERK (Cell signaling, 4370S), anti‐ERK (Cell signaling, 4695S), anti‐phospho‐CTD RNA polymerase II (Ser2) (Abcam, ab5095), anti‐CTD RNA polymerase II (Abcam, ab817), anti‐N‐terminal RNA polymerase II A‐10 (Santa Cruz, sc17798), anti‐ACTININ (Abcam, ab68194), anti‐COFILIN (Abcam, ab54532), anti‐GAPDH (clone D16H11, Cell Signaling, 5174), anti‐MECP2 (Cell Signaling, 3456), anti‐U1‐70K (clone H111, Synaptic Systems, 203011), anti‐LAMIN B1 (Abcam, ab133741), anti‐hnRNPA1 (clone D21H11, Cell Signaling, 8443), and anti‐betaIII TUBULIN (Abcam, ab18207).

Mazille M., Buczak K., Scheiffele P, & Mauger O. (2022). Stimulus‐specific remodeling of the neuronal transcriptome through nuclear intron‐retaining transcripts. The EMBO Journal, 41(21), e110192.

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Western Blot Analysis of Cellular Proteins

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