Gapdh mab374

Manufactured by Merck Group

Sourced in United States, Germany

GAPDH (MAB374) is a monoclonal antibody product from Merck Group that is used for the detection of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH) protein. GAPDH is a key enzyme involved in the glycolytic pathway, catalyzing the conversion of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate. This antibody can be used in various applications such as Western blotting, immunohistochemistry, and ELISA to identify and quantify GAPDH levels in biological samples.

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Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) (MAB374) (2 citations) Anti-GAPDH antibody (MAB374, (8 citations) GAPDH (clone MAB374, (2 citations) Anti-GAPDH (MAB374, (31 citations) Mouse anti-GAPDH antibody 6C5 (MAB374), (2 citations) Antibody to GAPDH (MAB374) (2 citations) Monoclonal GAPDH antibody (MAB374, (2 citations) Mouse monoclonal anti-GAPDH (MAB374, (3 citations) GAPDH (MAB374) antibody (8 citations) Mouse anti-GAPDH (MAB374, (12 citations)

45 protocols using gapdh mab374

Multiparametric Analysis of Autophagy

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Reagents were obtained from the following sources: antibodies against MITF (sc-71587) from Santa Cruz Biotechnology; GAPDH (MAB374) from Millipore; TFE3 from Cell Marque (MRQ-37; 354R-14)); LAMP2 (ab-25631) from Abcam; TFEB (4240), LC3B (3868), phospho-T389 S6K1 (9234), S6K1 (2708), phospho-AMPK (Thr 172) (2535), AMPK (2603), phospho-ACC (Ser 79) (3661), ACC (3676), Lamin (2032), mTOR (2893) and the FLAG epitope (2368) from Cell Signaling Technology; IPO8 (NBP2-24751) and LC3II (NB600-1384) from Novus Biologicals; CTSS (HPA002988), ATP6V1H (HPA023421) and ULK2 (HPA009027) from Sigma Aldrich; FLAG M2 affinity gel, amino acids from Sigma Aldrich; RPMI, DMEM, fetal bovine serum (FBS) and dialyzed FBS (dFBS), Alexa 488 and 568-conjugated secondary antibodies; 70KDa Dextran-Oregon Green 514, DQ-Green-BSA from Invitrogen; amino acid free RMPI from US Biologicals; Bafilomycin A1 from Tocris.

Perera R.M., Stoykova S., Nicolay B.N., Ross K.N., Fitamant J., Boukhali M., Lengrand J., Deshpande V., Selig M.K., Ferrone C.R., Settleman J., Stephanopoulos G., Dyson N.J., Zoncu R., Ramaswamy S., Haas W, & Bardeesy N. (2015). Transcriptional control of the autophagy-lysosome system in pancreatic cancer. Nature, 524(7565), 361-365.

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Comprehensive Antibody Panel for Ciliary and Cytoskeletal Analysis

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The following antibodies were used in the study: acetylated α-tubulin (6–11-B-1, used at 1:10,000 to detect cilia and 1:1,000 to detect cytoplasmic microtubules) and α-tubulin (T5168, used at 1:1,000 for immunofluorescence (IF) and 1:50,000 for western blot) from Sigma; EB1 (610534, used at 1:200), β-catenin (610153, used at 1:200) and anti-PKAc (610980, used at 1:200) from BD biosciences; acetylated α-tubulin (ab24610, used at 1:500) and α-tubulin (ab18251, used at 1:500) from Abcam; IFT54 (HPA037858, Atlas Antibodies, used at 1:50 for IF and 1:1,000 for WB); ZO1 (61–7300, used at 1:100) from Life Technologies; ARL13B (17711-1-AP, Proteintech, used at 1:400); Gp135 (AF1556, R&D, used at 1:200 for IF and 1:1000 for WB); γ-tubulin (DQ-19, Sigma, used at 1:500); γ-tubulin (C-20, used at 1:200), MAP4 (H-300 and G-10, used at 1:400 for IF and 1:1,000 for WB) and ACIII (C-20, used at 1:200) from Santa Cruz; GAPDH (MAB374, used at 1:4000 for WB) from Millipore. Highly cross adsorbed secondary antibodies (Alexa Fluor 488, Alexa Fluor 546, AlexaFluor 555, AlexaFluor 532 and Alexa Fluor 647) were obtained from Molecular Probes (Life Technologies) and were used at 1:200 dilution.

Bizet A.A., Becker-Heck A., Ryan R., Weber K., Filhol E., Krug P., Halbritter J., Delous M., Lasbennes M.C., Linghu B., Oakeley E.J., Zarhrate M., Nitschké P., Garfa-Traore M., Serluca F., Yang F., Bouwmeester T., Pinson L., Cassuto E., Dubot P., Elshakhs N.A., Sahel J.A., Salomon R., Drummond I.A., Gubler M.C., Antignac C., Chibout S., Szustakowski J.D., Hildebrandt F., Lorentzen E., Sailer A.W., Benmerah A., Saint-Mezard P, & Saunier S. (2015). Mutations in TRAF3IP1/IFT54 reveal a new role for IFT proteins in microtubule stabilization. Nature Communications, 6, 8666.

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Subcellular Protein Extraction and Analysis

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Total protein extraction was performed as previously described in ref. ^{27 (link)}.
Nuclear and cytoplasmic proteins fractionation, was performed using buffers A and B (A: Hepes 10 mM, KCl 10 mM, EDTA 0,2 mM, DTT 1 mM, PMSF 1 mM, okadaic acids 1 μM, cocktail of phosphatase and protease inhibitors; B: Hepes 20 mM, NaCl 0,4 M, EDTA 0,2 M, DTT 1 mM, PMSF 1 mM, okadaic acids 1 μM, cocktail of phosphatase and protease inhibitors and glicerol 10% (v/v)).
Western blot (WB) was performed as previously described in ref. ^{27 (link)}. The following primary antibodies were used: PARP (#9542), LC3B (2775 S), phospho FOXO3a Ser318-321 (9465 S), phospho p65 Ser536 (#3031), CK1α (2655 S) (Cell Signaling Technology, MA, USA); β-actina (A5441) (Sigma-Aldrich, Italy); GAPDH (MAB374) (Millipore, USA); p62 (#P0067), FOXO3a (ab12162), p65 (ab7970-1) (ABCAM, UK). Anti-rabbit-HRP (Cell Signaling, USA) and anti-mouse-HRP (KPL, USA) were used as secondary antibodies. Acquisition of the bands was performed in chemiluminescence using the Image Quant LAS 500 machine (GE Healthcare, USA) and the densitometric analysis of the bands was performed with the Image Quant TL software (GE Healthcare, USA).

Carrino M., Quotti Tubi L., Fregnani A., Canovas Nunes S., Barilà G., Trentin L., Zambello R., Semenzato G., Manni S, & Piazza F. (2019). Prosurvival autophagy is regulated by protein kinase CK1 alpha in multiple myeloma. Cell Death Discovery, 5, 98.

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Protein Extraction and Western Blotting

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Cells were lysed using a modified RIPA buffer (50 mM Tris (pH 8.0), 150 mM NaCl, 1.0% NP-40, 0.5% Sodium deoxycholate, 0.1% SDS, 10mM Na₄P₂O₇, 10 mM β-glycerolphosphate, 10mM NaF, 10mM EDTA, 1mM EGTA) with 1X HALT phosphatase/protease inhibitor cocktail (Thermo) added prior to lysis as described [35 (link)]. The following antibodies were used: Sigma, anti-Cx43 (C6219); Cell Signaling Technology, total ERK (9102L), phospho-ERK (9101L), total PKCδ (2058S), phospho-PKCδ Thr505 (9374S), PCNA (2586S), anti-Rabbit HRP (7074S), anti mouse HRP (7076S); Millipore, GAPDH (MAB374) and anti-osterix (AB3743). Representative blots are shown and were repeated a minimum of two times.

Buo A.M., Tomlinson R.E., Eidelman E.R., Chason M, & Stains J.P. (2017). Connexin43 and Runx2 Interact to Affect Cortical Bone Geometry, Skeletal Development, and Osteoblast and Osteoclast Function. Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research, 32(8), 1727-1738.

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Antibody Validation for Ubiquitin

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Anti-K48 (clone Apu2.07) and -K63 (clone Apu3) ubiquitin and GAPDH (MAB374) antibodies were purchased from Millipore. The anti-K11 ubiquitin antibody (clone 2A3/2E6) was a kind gift from V. Dixit (Genentech) and has been previously described [25 (link)]. α-Tubulin, Calnexin (SPA-860), p97 (sc-57492) and Grp78 (sc13968), and hexahistidine-tag (A00186) antibodies were purchased from Zymed, Enzo Life Sciences, Santa Cruz Biotechnology, and Genscript, respectively.

Locke M., Toth J.I, & Petroski M.D. (2014). K11- and K48-Linked Ubiquitin Chains Interact with p97 during Endoplasmic Reticulum-Associated Degradation. The Biochemical journal, 459(1), 205-216.

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Comprehensive Flow Cytometry Panel for Mouse T Cells

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Flow cytometry monoclonal antibodies against mouse antigens (CD4, clone RM4-5; CD8a, clone 53–6.7; CD62L, clone MEL-14; IFN-γ, clone XMG1.2; IL-2, clone JES6-16E3; Ifnar1, clone MAR1-5A3; PD-1, clone RMP1-30; T-bet, clone 4B10) were obtained from Biolegend. Tim-3 monoclonal antibody (clone 5D12) was a gift from V. Kuchroo. Carboxyfluorescein succinimidyl ester (CFSE) was obtained from Biolegend. The following recombinant cytokines and antibodies were used for in vitro T cell cultures: mIFN-β (PBL InterferonSource, indicated concentrations), mIL-12 (R&D Biosystems, 10 ng mL^-1), mIL-2 (Miltenyi, 5 ng mL^-1), hTGF-β (Miltenyi, 3 ng mL^-1), mIL-6 (Miltenyi, 20 ng mL^-1), mIL-23 (R&D Biosystems, 20 ng mL^-1), anti-mIL-4 (BioXCell; clone 11B11, 10 μg mL^-1), anti-CD3 (eBioscience; Functional Grade Purified, clone 145-2C11, 2 μg mL^-1), anti-CD28 (Biolegend; LEAF-purified, clone 37.51, 2 μg mL^-1). Western blotting primary antibodies were obtained from BD Transduction Laboratories (Stat1, clone 42/Stat1, dilution 1:1000; Stat1 pY701, clone 14/P-STAT1, dilution 1:1000; Stat4 pY693, clone 42/Stat1, dilution 1:500), Cell Signaling (Stat4, clone C46B10, dilution 1:500) or Millipore (GAPDH, mAb374, dilution 1:1000). Anti-mouse or-rabbit secondary antibodies were obtained from Jackson Immunoresearch and were used at 1:10000.

Boivin N., Baillargeon J., Doss P.M., Roy A.P, & Rangachari M. (2015). Interferon-β Suppresses Murine Th1 Cell Function in the Absence of Antigen-Presenting Cells. PLoS ONE, 10(4), e0124802.

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Mitochondrial Dynamics Protein Analysis

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Antibodies: DRP1(H00010059-M01) and MFN2 (H00009927-M01) from Abnova; OPA1 (612607) and TIM23 (611222) from BD Biosciences; HSP60 (SC-13966) from Santa Cruz; ATG5 (12994), ATG7 (8558), DRP1-phosphoS616 (3455), and TOM20 (42406) from Cell signaling; NDUFA9 (ab14713), SDHA (ab14715), UQCRC2 (ab14745), COX IV (ab14744), ATP5A (ab1801) and CS (ab129095) from Abcam; GAPDH (MAB374) from Millipore; LC3 (L7543), ACTIN (SAB00001) and TUBULIN (T6557) from Sigma-Aldrich; Mitotracker CMX Ros (M7512) from ThermoFisher Scientific. Horseradish peroxidase-conjugated secondary antibodies from Jackson Immuno Research (Mouse 115-035-146, Rabbit 111-035-144). ECL western blotting kit from Biorad or Thermo Scientific Pierce. Fluorescent secondary antibodies anti-rabbit (926-32210) or anti-mouse (926-68071) from Licor.

Aleo S.J., Del Dotto V., Fogazza M., Maresca A., Lodi T., Goffrini P., Ghelli A., Rugolo M., Carelli V., Baruffini E, & Zanna C. (2020). Drug repositioning as a therapeutic strategy for neurodegenerations associated with OPA1 mutations. Human Molecular Genetics, 29(22), 3631-3645.

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Multiparametric Analysis of Autophagy

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Western Blotting Analysis of Src and Rb

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Cells were lysed using the RIPA lysis buffer (Santa Cruz Biotechnology, Inc.). Proteins were separated by 7.5% SDS-PAGE (Bio-Rad Laboratories) and transferred to nitrocellulose membranes (Bio-Rad Laboratories). The membranes were blocked in 3% BSA in 0.1% Tween 20 TBS for 1 h at room temperature and then incubated with the following primary antibodies overnight at 4°C: Src (47405; 1:1,000; rabbit; Abcam), Src (16885; 1:1,000; mouse; Abcam), ppRb (G3-245; 1:1,000; mouse; BD), underphosphorylated Rb (G99-549; 1:1,000; mouse; BD), or GAPDH (MAB374; 1:1,000; mouse; Millipore) as the loading control. After washing, the membranes were incubated with secondary antibodies for 1 h at room temperature: anti–mouse HRP (1:3,000; Cell Signaling Technology) or anti–rabbit HRP (1:5,000; Cell Signaling Technology), and then incubated in chemiluminescent HRP substrate (Millipore) for signal detection and development.

Chetty S., Engquist E.N., Mehanna E., Lui K.O., Tsankov A.M, & Melton D.A. (2015). A Src inhibitor regulates the cell cycle of human pluripotent stem cells and improves directed differentiation. The Journal of Cell Biology, 210(7), 1257-1268.

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Western Blot Analysis of Receptor Proteins

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Immunoblot analysis was performed as previously described (1 ). Precast 4–20% gradient gels (Bio-Rad) were used for EGFR and GRB2 immunoprecipitations. The following antibodies were used from Cell Signaling Technology: pTRK Y490 (9141 or 4619) and Y464/65 (C50F3), pEGFR Y1068 (D7A5) and Y1173 (53A5), total EGFR (2232L or XP D38B1), HA (C29F4 or 6E2), pALK Y1278/1282/1283 (3983), total ALK (D5F3, 3333, or 31F12), total ROS1 (D4D6), pRET Y905 (3221), total RET (C31B4), pERK1/2 XP T202/Y204, total ERK1/2 (3A7), pAKT S473 XP (D9E 4060 or 193H12), GRB2 (3972), and pan-keratin (C11). Total RET was also purchased from Abcam (ab134100), GAPDH (MAB374) and pTYR (4G10) from Millipore, total EGFR (610017) from BD Biosciences, total TRK (C-14) and Tubulin antibodies from Santa Cruz Biotechnology and FGFR1 antibody (#TA301021) was purchased from Origene.

Vaishnavi A., Schubert L., Rix U., Marek L.A., Le A.T., Keysar S.B., Glogowska M.J., Smith M.A., Kako S., Sumi N.J., Davies K.D., Ware K.E., Varella-Garcia M., Haura E.B., Jimeno A., Heasley L.E., Aisner D.L, & Doebele R.C. (2017). EGFR mediates responses to small molecule drugs targeting oncogenic fusion kinases. Cancer research, 77(13), 3551-3563.

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