Rabbit monoclonal anti gapdh 14c10

Manufactured by Cell Signaling Technology

The Rabbit monoclonal anti-GAPDH (14C10) is a primary antibody that specifically recognizes the GAPDH (Glyceraldehyde 3-phosphate dehydrogenase) protein. GAPDH is a widely expressed enzyme involved in glycolysis.

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Lab products found in correlation

Anti rab13 rabbit polyclonal, by Novus Biologicals (3 mentions) Mouse monoclonal anti histone h3 96c10, by Cell Signaling Technology (2 mentions) Anti phospho fak y397, by Cell Signaling Technology (2 mentions) Alexa 647, by Thermo Fisher Scientific (2 mentions) Anti rep 1, by Abcam (2 mentions) Anti rabgdi, by Santa Cruz Biotechnology (2 mentions) Anti rabif mouse monoclonal antibody d 12, by Santa Cruz Biotechnology (2 mentions) Rabbit polyclonal anti gfp, by Thermo Fisher Scientific (2 mentions) Gentamycin solution, by Merck Group (1 mentions) Anti hbd 3 antibody, by Novus Biologicals (1 mentions) Mouse monoclonal anti α tubulin t5168, by Merck Group (1 mentions) Shc002, by Merck Group (1 mentions) Mouse monoclonal anti α tubulin, by Merck Group (1 mentions) Anti transferrin receptor clone h68, by Thermo Fisher Scientific (1 mentions)

Close spelling variants of this product

Anti-GAPDH rabbit monoclonal antibody (14C10, Rabbit anti-GAPDH (14C10) Anti-GAPDH (14C10) Rabbit monoclonal anti-GAPDH GAPDH (14C10) Rabbit monoclonal GAPDH Monoclonal anti-GAPDH Rabbit anti-GAPDH Monoclonal rabbit Anti-GAPDH

6 protocols using rabbit monoclonal anti gapdh 14c10

Antibody Detection: PARP1, Histone H3, GAPDH

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The following antibodies were used: rabbit polyclonal anti-PARP1 (#9542), mouse monoclonal anti-Histone H3 (96C10; #3638) and rabbit monoclonal anti-GAPDH (14C10; #2118) from Cell Signaling Technology; mouse monoclonal anti-PAR (10H; ab14459) from Abcam. Densitometric analyses of immunoblots were carried out using Image J software (NIH).

Parsels L.A., Engelke C.G., Parsels J., Flanagan S.A., Zhang Q., Tanska D., Wahl D.R., Canman C.E., Lawrence T.S, & Morgan M.A. (2020). Combinatorial efficacy of olaparib with radiation and ATR inhibitor requires PARP1 protein in homologous recombination proficient pancreatic cancer. Molecular cancer therapeutics, 20(2), 263-273.

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Comprehensive Antibody Panel for Cell Signaling

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The following antibodies were used: Rabbit monoclonal anti-pY15-Cdc2 (10A11; #4539), rabbit polyclonal anti-PARP1 (#9542), mouse monoclonal anti-Histone H3 (96C10; #3638) and rabbit monoclonal anti-GAPDH (14C10; #2118) from Cell Signaling Technology; rabbit polyclonal anti-pS10-Histone H3 (06–570), mouse monoclonal anti-γH2AX (JBW301; 05–636) and rabbit polyclonal anti-CDC2/CDK1 (06–966) from Millipore; mouse monoclonal anti-PAR (10H, Ab1) from either Calbiochem or Abcam; mouse monoclonal anti-RPA32 (9H8; ab2175) from Abcam; and rabbit polyclonal anti-phospho-RPA32 (S4/S8; A300-245A) and anti-phospho-RPA32 (S33; A300-246A-M) from Bethyl Labs.

Parsels L.A., Karnak D., Parsels J.D., Zhang Q., Vélez-Padilla J., Reichert Z.R., Wahl D.R., Maybaum J., O’Connor M.J., Lawrence T.S, & Morgan M.A. (2017). PARP1 Trapping and DNA Replication Stress Enhance Radiosensitization with Combined WEE1 and PARP Inhibitors. Molecular cancer research : MCR, 16(2), 222-232.

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Reagents and Plasmids for Cell Signaling

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N-phosphonacetyl-l-aspartate (PALA, NSC224131) was obtained from the National Cancer Institute (NCI)/Division of Cancer Treatment and Diagnosis (DCTD)/Developmental Therapeutics Program (DTP) Open Chemical Repository (http:dtp.cancer.gov). Aquaphor® and Neosporin® were purchased from Target (Cleveland Heights, OH). Gentamycin solution was purchased from Sigma (St. Louis, MO). Rabbit monoclonal anti-CAD antibody (EP711Y) was purchased from Novus Biologicals (Littleton, CO). Rabbit polyclonal anti-RICK (H-300) was purchased from Santa Cruz Biotechnology (Santa Cruz, CA). Rabbit monoclonal anti-GAPDH (14C10) was purchased from Cell Signaling Technologies (Danvers, MA). Mouse monoclonal anti-α-tubulin (T5168) was purchased from Sigma. Antibodies against LL-37 (sc-166770) and HBD2 (sc-20798) were purchased from Santa Cruz Biotechnology. Anti-HBD3 antibody was purchased from Novus Biologicals (NB200-117). The plasmids, pcDNA3-HA-NOD1, pcDNA3-HA-NOD2, pBVIII-Luc, and pCMV-βgal were gifts of Gabriel Nuñez (University of Michigan) and have been previously described^{56 (link)}. MISSION short hairpin RNA (shRNA) constructs targeting CAD (NM_004341.3-6910s21c1), NOD2 (NM_022162.1-2959s1c1), RIP2 (NM_003821.5-2364s21c1), and non-targeting shRNA control (SHC002) were purchased from Sigma.

Jatana S., Homer C.R., Madajka M., Ponti A.K., Kabi A., Papay F, & McDonald C. (2018). Pyrimidine synthesis inhibition enhances cutaneous defenses against antibiotic resistant bacteria through activation of NOD2 signaling. Scientific Reports, 8, 8708.

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Western Blot Antibody Detection

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For Western blot detection the following antibodies were used: anti-Rab13 rabbit polyclonal (Novus Biologicals, cat# NBP1-85799) and anti-GAPDH rabbit monoclonal 14C10 (Cell Signaling Technology, cat# 2118).

Moissoglu K., Yasuda K., Wang T., Chrisafis G, & Mili S. (2019). Translational regulation of protrusion-localized RNAs involves silencing and clustering after transport. eLife, 8, e44752.

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Immunofluorescence and Western Blot Protocols for Rab13 and Related Proteins

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For IF, cells were plated onto collagen IV‐coated glass coverslips (10 μg/ml) and then fixed with 4% paraformaldehyde (PFA) in PBS (phosphate‐buffered saline) for 15 min, permeabilized with 0.2% Triton X‐100 in PBS for 5 min, blocked with 5% goat serum in PBS for 1 h, and incubated with Rab13 rabbit polyclonal antibody (Novus Biologicals, cat# NBP1‐85799, 1/200 dilution) for 1 h. Secondary antibodies were conjugated with Alexa 647 (Thermo Fisher Scientific).
For Western blot detection, the following antibodies were used: anti‐Rab13 rabbit polyclonal (Novus Biologicals, cat# NBP1‐85799, 1/1,000 dilution), anti‐GFP rabbit polyclonal (Invitrogen, cat# A11122, 1/2,000 dilution), anti‐RhoGDI, anti‐transferrin receptor (clone H68.4, Thermo Fisher Scientific, cat# 13‐6800), anti‐α‐tubulin mouse monoclonal (Sigma‐Aldrich, cat# T6199, 1/10,000 dilution), anti‐GAPDH rabbit monoclonal 14C10 (Cell Signaling Technology, cat# 2118, 1/2,000 dilution), anti‐phospho‐FAK(Y397) (Cell Signaling Technology, cat# 3283), anti‐REP‐1 (Abcam, cat# 134964), anti‐RabGDI (Santa Cruz Biotechnology, cat# sc‐374649), and anti‐RABIF mouse monoclonal antibody D‐12 (Santa Cruz biotechnology, cat# sc‐390759, 1/1,000 dilution).

Moissoglu K., Stueland M., Gasparski A.N., Wang T., Jenkins L.M., Hastings M.L, & Mili S. (2020). RNA localization and co‐translational interactions control RAB13 GTPase function and cell migration. The EMBO Journal, 39(21), e104958.

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Immunofluorescence and Western Blot Analysis of Rab13

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For IF, cells were plated onto collagen IV-coated glass coverslips (10µg/ml) and then fixed with 4% paraformaldehyde (PFA) in PBS (phosphate-buffered saline) for 15min, permeabilized with 0.2% Triton X-100 in PBS for 5 min, blocked with 5% goat serum in PBS for 1h, and incubated with Rab13 rabbit polyclonal antibody (Novus Biologicals, cat# NBP1-85799, 1/200 dilution) for 1h. Secondary antibodies were conjugated with Alexa 647 (Thermo Fisher Scientific).
For Western blot detection the following antibodies were used: anti-Rab13 rabbit polyclonal (Novus Biologicals, cat# NBP1-85799, 1/1,000 dilution), anti-GFP rabbit polyclonal (Invitrogen, cat# A11122, 1/2,000 dilution), anti-RhoGDI, anti-Transferrin receptor (clone H68.4, ThermoFisher Scientific, cat# 13-6800), anti-a-tubulin mouse monoclonal (Sigma-Aldrich, cat# T6199, 1/10,000 dilution), and anti-GAPDH rabbit monoclonal 14C10 (Cell Signaling Technology, cat# 2118, 1/2,000 dilution), anti-phospho-FAK(Y397) (Cell Signaling Technology, cat# 3283), anti-REP-1 (Abcam, cat# 134964), anti-RabGDI (Santa Cruz Biotechnology, cat# sc-374649), anti-RABIF mouse monoclonal antibody D-12 (Santa Cruz biotechnology, cat# sc-390759, 1/1,000 dilution).

Moissoglu K., Stueland M., Gasparski A.N., Wang T., Jenkins L.M., Hastings M.L., & Mili S. (2020). Local RNA translation controls cell migration and Rab GTPase function.

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