Mouse anti gapdh sc 32233

Manufactured by Santa Cruz Biotechnology

Sourced in United States

Mouse anti-GAPDH (sc-32233) is a primary antibody that recognizes the GAPDH (glyceraldehyde-3-phosphate dehydrogenase) protein. GAPDH is a key enzyme involved in glycolysis, a fundamental metabolic pathway. This antibody can be used in various applications such as Western blotting, immunoprecipitation, and immunohistochemistry to detect and study the GAPDH protein.

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GAPDH (3335 citations) Anti-GAPDH (1455 citations) Mouse anti-GAPDH (208 citations) Sc-32233 (191 citations) GAPDH (sc-32233) (82 citations) Anti-GAPDH (sc-32233) (43 citations) Mouse monoclonal anti-GAPDH (sc-32233, (3 citations) GAPDH (mouse, (2 citations) Mouse anti-GAPDH antibody (sc-32233) (2 citations) Mouse monoclonal anti-GAPDH antibody (sc-32233), (2 citations)

9 protocols using mouse anti gapdh sc 32233

Antibody Library for Cell Signaling Research

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The following antibodies were obtained from Cell Signaling Technology (Beverly, MA): rabbit anti-CDK2 (2546), mouse anti-Cyclin B1 (4135), and rabbit anti-PCNA (13110). The following antibodies were purchased from Santa Cruz Biotechnology (Santa Cruz, CA): mouse anti-p16 (sc-74400), mouse anti-GAPDH (sc-32233), mouse anti-β-actin (sc-47778), mouse anti-E2F-1 (sc-251), rabbit anti-HBP1 (sc-25390), mouse anti-Bmi-1(sc-13519), and mouse anti-Ets-1 (sc-55581). Rabbit anti-SOD1 (ab16831), rabbit anti-SOD2 (ab13533), and rabbit anti-Ki-67 (ab15580) were purchased from Abcam (Cambridge, MA). Mouse anti-HP1γ antibody (05-690) and rabbit anti-H3K9me3 (07-442) antibody were purchased from EMD Millipore (Billerica, MA). Other chemicals and organic solvents of the highest available grade were obtained from Sigma-Aldrich. AMPKα1^−/− and AMPKα2^−/− mice were described elsewhere (Jorgensen et al., 2004 (link); Viollet et al., 2003 (link)). Mice were handled in accordance with study protocols approved by the Institutional Animal Care and Use Committee of Georgia State University (Atlanta, GA).

Ding Y., Chen J., Okon I.S., Zou M.H, & Song P. (2015). Absence of AMPK 2 Accelerates Cellular Senescence via P16 Induction in Mouse Embryonic Fibroblasts. The international journal of biochemistry & cell biology, 71, 72-80.

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Comprehensive Antibody Panel for Cytoskeletal and Cell Junction Analysis

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The following primary antibodies were used: rabbit anti-NuMA EP3976, rabbit-anti-ODF2 ab43840, and rabbit anti-NOTCH3 ab23426 (Abcam); mouse anti-β-catenin 610153, mouse anti-plakoglobin 610253, mouse anti-p150-glued 612708, and mouse anti-pericentrin 611815 (BD Bioscience); mouse anti H3P (Cell Signaling Technology); rabbit anti-filaggrin PRB-417p, rabbit anti-involucrin PRB-140c, rabbit anti-loricrin PRB-145p, and rabbit anti-K5 PRB-160p (Covance Research Products); mouse anti-γ-tubulin TU-30 (Exbio); mouse anti-claudin 1 37-4900 (Invitrogen); mouse anti-desmoglein 3 D218-3 (MBL); mouse anti-actin MAB1501 (Merck Millipore); rabbit anti-Lis1 sc-15319, rabbit anti-desmoglein 1 sc-20114, and mouse anti-GAPDH sc-32233 (Santa Cruz Biotechnology); rabbit anti α-catenin DECMA1, mouse anti-centrin 20H5, mouse anti-α-tubulin T5168, mouse anti-acetylated tubulin T7451, mouse anti-K10 SAB4501656, mouse anti-K1-10/anti-pan-cytokeratin c2562, and mouse anti-desmoplakin 11-5F (Sigma-Aldrich); rabbit anti-Ki67 RM-9106 (Thermo Fisher Scientific); rabbit anti-ninein L77 (Delgehyr et al, 2005 (link)); rabbit anti-GCP2 (Haren et al, 2006 (link)); rabbit anti-γ-tubulin R75 (Julian et al, 1993 (link)); rabbit anti-ninein (Ou & Rattner, 2000 (link)); and mouse anti-corneodesmosin F27.28 (Serre et al, 1991 (link)).

Lecland N., Hsu C.Y., Chemin C., Merdes A, & Bierkamp C. (2019). Epidermal development requires ninein for spindle orientation and cortical microtubule organization. Life Science Alliance, 2(2), e201900373.

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Western Blot for Na+/K+ ATPase

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Primary antibodies of mouse anti-Na⁺/K⁺-ATPase A1/C464.6: sc-21712, Santa-Cruz (1:200), mouse anti-Na⁺/K⁺-ATPase β1 (C464.8): sc-21713, Santa-Cruz (1:200), mouse anti-GAPDH/sc-32233, Santa-Cruz (1:10,000) and mouse Anti-β-Actin, Clone AC-74 (A2228), Sigma (1:20,000) were used.
Secondary antibodies of donkey anti-mouse IgG (H + L) SA1-100/Invitrogen (1:10,000) and donkey anti-rabbit IgG (H + L) 31,458/Invitrogen (1:10,000) were used.

Cinarli Yuksel F., Nicolaou P., Spontarelli K., Dohrn M.F., Rebelo A.P., Koutsou P., Georghiou A., Artigas P., Züchner S.L., Kleopa K.A, & Christodoulou K. (2023). The phenotypic spectrum of pathogenic ATP1A1 variants expands: the novel p.P600R substitution causes demyelinating Charcot–Marie–Tooth disease. Journal of Neurology, 270(5), 2576-2590.

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Paxillin Immunofluorescence Staining

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Mouse anti-paxillin (no. 610052) was purchased from BD Biosciences (Franklin Lakes, NJ, USA). Rabbit anti-phosphorylated (pY118) paxillin (cat. number 44-722G) was from Invitrogen (ThermoFisher Scientific). Mouse anti-vinculin (V-9131) and mouse anti-tubulin (T-9026) were obtained from Sigma-Aldrich (St. Louis, MO, USA). Mouse anti-GAPDH (sc-32233) was purchased from Santa Cruz (Dallas, TX, USA). Rhodamin phalloidin and goat anti-mouse Alexa-488 conjugated secondary antibodies were from Molecular Probes (Invitrogen/ThermoFisher Scientific). Goat anti-rabbit CY-3 and goat anti-mouse Alexa647 conjugated secondary antibodies were from Jackson ImmunoResearch (West Grove, PA, USA). Nocodazole was purchased from Fluka (Zwijndrecht, The Netherlands).

Fokkelman M., Balcıoğlu H.E., Klip J.E., Yan K., Verbeek F.J., Danen E.H, & van de Water B. (2016). Cellular adhesome screen identifies critical modulators of focal adhesion dynamics, cellular traction forces and cell migration behaviour. Scientific Reports, 6, 31707.

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Western Blotting of Glutamate Transporters

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Mouse hippocampal homogenates were lysed in sodium phosphate buffer (pH 7.4) containing 1% SDS and 1mM PMSF, as suggested (Danbolt et al., 2016b (link)). The homogenates were passed five times through 25 gauge needle in 1 ml syringe, vortexed for 40 seconds, boiled 5 min at 95°C and centrifuged at 12,000xg for 10 min. Supernatants were collected, subjected to SDS-PAGE, transferred into PVDF membrane and revealed with the appropriate antibodies: guinea pig anti-GLT-1, rabbit against EAAT1 (GLAST) and rabbit against EAAT3 (EAAC1) (see above). Mouse anti-Gapdh (sc-32233, Santa Cruz Biotechnologies) was used as loading control. Primary antibodies were incubated overnight at 4°C. Images were obtained with a FujiLAS4000 using Lumilight Western Blotting Substrate (Roche). The results were analysed using the software Image Studio version 5.2 (LI-COR Biosciences, Germany). Experiments were performed in four individuals from each genotype.

Muñoz-Ballester C., Santana N., Perez-Jimenez E., Viana R., Artigas F, & Sanz P. (2019). In vivo glutamate clearance defects in a mouse model of Lafora disease. Experimental neurology, 320, 112959.

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Western Blot Analysis of GLT-1, EAAT2, and Nedd4.2

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Cell homogenates (30 μg protein) were subjected to SDS/PAGE and transferred into a PVDF membrane. Membranes were blocked with 5% non-fat milk in Tris-buffered saline containing 0.1% Tween-20 (TBS-T) and incubated overnight at 4°C with the corresponding antibodies: guinea pig anti-GLT-1 (AB1783, Millipore); mouse anti-EAAT2 (sc-365634, Santa Cruz Biotechnologies); rabbit anti-Nedd4.2 (#4013, Cell Signaling); mouse anti-HA (H9658, Sigma); mouse anti-Flag (F3165, Sigma) and rabbit anti-GFP (210-PS-1GFP, Inmunokontackt). Mouse anti-Gapdh (sc-32233, Santa Cruz Biotechnologies) and mouse anti-tubulin (T6199, Sigma) were used as loading controls. After washing, membranes were incubated with the corresponding HRP-conjugated secondary antibodies. When indicated, anti-HA-HRP was used (H6533, Sigma). Images were obtained with a FujiLAS400 (GE Healthcare, Barcelona, Spain) using Lumilight Western Blotting Substrate (Roche Applied Science, Barcelona, Spain). Quantification of the protein bands was carried out using the software Image Studio version 5.2 (LI-COR Biosciences, Germany). Values of the ubiquinated forms were normalized to the levels of the corresponding proteins in the crude extract and referred to those found in control levels, which were set to 100.

Perez-Jimenez E., Viana R., Muñoz-Ballester C., Vendrell-Tornero C., Moll-Diaz R., Garcia-Gimeno M.A, & Sanz P. (2020). Endocytosis of the glutamate transporter 1 is regulated by Laforin and Malin: implications in Lafora Disease.. Glia, 69(5), 1170-1183.

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Western Blot of CYP3A4 and GAPDH

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Total protein extracts were prepared from 500,000 cells with RIPA buffer (Tebu-Bio) in presence of antiproteases (Roche). The protein concentration was determined by the bicinchoninic acid method, according to the manufacturer's instructions (Pierce Chemical Co.). Bovine serum albumin (Pierce Chemical Co.) was used as standard. Cell lysates were resolved on SDS-PAGE and transferred to a Hybond-ECL membrane (GE Healthcare). Membranes were incubated with rabbit anti-CYP3A4 (5316, 1/10,000, Epitomics) or mouse anti-GAPDH (sc#32233, 1/5,000, Santa Cruz) monoclonal antibodies. Immunocomplexes were detected with horseradish peroxidase-conjugated rabbit (A0545, 1/10,000, Sigma) or mouse (A9044, 1/10,000, Sigma) secondary antibodies followed by enhanced chemiluminescence reaction (Millipore). Chemiluminescence was monitored using a ChemiDoc-XRS⁺ apparatus (Bio-Rad Laboratories).

Delfosse V., Dendele B., Huet T., Grimaldi M., Boulahtouf A., Gerbal-Chaloin S., Beucher B., Roecklin D., Muller C., Rahmani R., Cavaillès V., Daujat-Chavanieu M., Vivat V., Pascussi J.M., Balaguer P, & Bourguet W. (2015). Synergistic activation of human pregnane X receptor by binary cocktails of pharmaceutical and environmental compounds. Nature Communications, 6, 8089.

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Cell Lysis and Western Blot Analysis

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Cell lysis and WB were performed as described in reference 62 (link). Antibodies were as follows: rabbit anti-TPX2 (1:1,000; Novus Biologicals), mouse anti-Aurora-A (0.5 µg/ml; BD Transduction Laboratories), rabbit anti-pAurora-A (Thr288) (3079 clone C39D8, 1:100; Cell Signaling Technology, Inc.), and mouse anti-GAPDH (SC-32233, 1:1,000; Santa Cruz Biotechnology). HRP-conjugated secondary antibodies (Bio-Rad Laboratories S.r.l.) were revealed using the Clarity Western ECL Substrate (Bio-Rad Laboratories S.r.l.).

Asteriti I.A., Polverino F., Stagni V., Sterbini V., Ascanelli C., Naso F.D., Mastrangelo A., Rosa A., Paiardini A., Lindon C, & Guarguaglini G. (2023). AurkA nuclear localization is promoted by TPX2 and counteracted by protein degradation. Life Science Alliance, 6(5), e202201726.

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Western Blot Analysis of HCN Channels

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Cells were lysed with RIPA and the proteins were separated on 10% SDS-PAGE gel before transferring onto PVDF membranes. The membranes were blocked overnight with 5% BSA and then were respectively incubated with polyclonal anti-HCN1 (APC-056), anti-HCN2 (APC-030), anti-HCN3 (APC-057), anti-HCN4 (AGP-004) at 1:1000 dilution (Alomone Labs, Jerusalem, Israel), or with anti-GAP-43 (sc-135915) or anti-TH (sc-136100) at 1:1000 dilution (Santa Cruz Biotechnology, Inc. United States) overnight at 4°C. On the second day, blots were washed with phosphate buffered saline (PBS) and then incubated with a goat anti-rabbit IgG-HRP (sc-2004) or goat anti-mouse IgG-HRP (sc-2005) (1:2000 dilution) for 2 h at room temperature. Mouse anti-GAPDH (sc-32233) (1:2000 dilution) (Santa Cruz Biotechnology, Inc., United States) was used as an internal standard for protein quantification. After three washes with PBS, visualization was performed using enhanced chemiluminescence (ECL) plus the Western Blotting Detection system (Amersham Biosciences). Protein quantification was carried out with Image-Pro Plus (Media Cybernetics, Inc., United States) software.

Zhong L.Y., Fan X.R., Shi Z.J., Fan Z.C., Luo J., Lin N., Liu Y.C., Wu L., Zeng X.R., Cao J.M, & Wei Y. (2019). Hyperpolarization-Activated Cyclic Nucleotide-Gated Ion (HCN) Channels Regulate PC12 Cell Differentiation Toward Sympathetic Neuron. Frontiers in Cellular Neuroscience, 13, 415.

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