Anti gapdh gt239

Manufactured by GeneTex

Sourced in United States

Anti-GAPDH (GT239) is a primary antibody that specifically recognizes the GAPDH protein. GAPDH is a widely expressed enzyme involved in glycolysis. This antibody can be used to detect and quantify GAPDH levels in various biological samples.

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Lab products found in correlation

Poly 1 c, by InvivoGen (2 mentions) Poly da dt, by InvivoGen (2 mentions) Mouse igg, by Cell Signaling Technology (2 mentions) Saf32, by Cayman Chemical (2 mentions) Anti tfr, by Thermo Fisher Scientific (2 mentions) Anti β actin mab1501, by Merck Group (2 mentions) Na934v, by GE Healthcare (2 mentions) Anti ferritin, by Merck Group (2 mentions) Anti tf gtx2123, by GeneTex (2 mentions) Anti ceruloplasmin, by Agilent Technologies (2 mentions) Anti fpn nbp1 21502, by Novus Biologicals (2 mentions) Hoechst, by Thermo Fisher Scientific (2 mentions) Fluoromount g, by Southern Biotech (2 mentions) Pngase f, by New England Biolabs (2 mentions) Anti β actin 13e5, by Cell Signaling Technology (1 mentions) Ifnar1 mice, by Jackson ImmunoResearch (1 mentions) C57bl 6 male mice, by Jackson ImmunoResearch (1 mentions) Antibody against α tubulin, by Merck Group (1 mentions) Anti β catenin d10a8, by Cell Signaling Technology (1 mentions) Horseradish peroxidase conjugated secondary antibody, by Thermo Fisher Scientific (1 mentions)

7 protocols using anti gapdh gt239

Murine cell differentiation protocol

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C57BL/6 male mice (6-8 weeks of age) and Ifnar1 −/− mice were from the Jackson Laboratory. All mice experiments were performed in accordance with guidelines from the University of California, Los Angeles, Institutional Animal Care and Use Committee. HEK293T and RAW264.7 cells were purchased from ATCC and cultured in Dulbecco's modified Eagle's medium (DMEM) with 10% fetal bovine serum (FBS) and 1% penicillin/streptomycin. RXRα^fl/fl (WT) and LysM-Cre +/RXRα^fl/fl (Rxra−/−) mice bone marrows were overnight shipped from Dr Mercedes Ricote's Lab (Spain)^{13 (link)}. WT, Ifnar1 −/− and Rxra −/− BMMs were differentiated as described previously^{45 (link)}. WT and Rxra −/− F9 embryocarcinoma cells, as well as RXR-specific agonists AGN194204 and LG268 were obtained from Dr Peter Tontonoz's Lab (University of California, Los Angeles). HX531 was obtained from Dr Hiroyuki Kagechika's lab (Tokyo Medical and Dental University). 9cRA and 13cRA were purchased from Sigma-Aldrich. All compounds for in vitro treatment were solubilized in DMSO. PolyI:C and polydA:dT were from InvivoGen. Antibody against α-tubulin was from Sigma-Aldrich. Anti-VSV-G (P5D4) and anti-Oct1 (C-21) antibodies were from Santa Cruz Biotechnology. Anti-RXRα (D6G10), anti-β-Actin (13E5) and anti-β-Catenin (D10A8) were from Cell Signaling Technology. Anti-GAPDH (GT239) was from GeneTex.

Ma F., Liu S.Y., Razani B., Arora N., Li B., Kagechika H., Tontonoz P., Núñez V., Ricote M, & Cheng G. (2014). Retinoid X receptor α attenuates host antiviral response by suppressing type I interferon. Nature communications, 5, 5494.

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Immunoblot Analysis of Protein Samples

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Cells were lysed in M-PER Mammalian Protein Extraction Reagent (Thermo Fisher Scientific) containing protease inhibitor cocktail (Roche). Immunoblot analysis was conducted with 25–30 μg of total cell protein. The protein concentration of cell lysates was determined with the Bradford reagent (Bio-Rad). Equal amounts of total protein were subjected to SDS-PAGE on a 6% or 8% gel, and then transferred to nitrocellulose membranes (Bio-Rad). The membranes were blocked in 5% milk, and then incubated in PBST buffer with primary antibodies at 4°C overnight, followed by incubation with horseradish peroxidase-conjugated secondary antibody (1:5000, Thermo Fisher Scientific) for one hour at room temperature. Membranes were exposed to HyBlot CL film at room temperature. Primary antibodies used were anti-DHHC5 (HPA014670, Sigma-Aldrich), anti-GAPDH (GT239, GeneTex), anti-HSP90 (SC-13119, Santa Cruz Biotechnology).

Tian H., Lu J.Y., Shao C., Huffman K.E., Carstens R.M., Larsen J.E., Girard L., Liu H., Rodriguez-Canales J., Frenkel E.P., Wistuba I.I., Minna J.D, & Hofmann S.L. (2015). Systematic siRNA Screen Unmasks NSCLC Growth Dependence by Palmitoyltransferase DHHC5. Molecular cancer research : MCR, 13(4), 784-794.

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Western Blot Analysis of LuCaP Xenografts

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LuCaP xenografts were manually homogenized in RIPA buffer containing 2M Urea and protease inhibitors (Fisher Scientific). The homogenates were sonicated and centrifuged to remove insoluble material. Ten-micrograms of total protein lysate was electrophoresed on 4–12% Bis-Tris gels (Invitrogen) with MES buffer. The gels were transferred to nitrocellulose and blocked with 5% BSA in PBS/0.1% Tween-20 and subsequently probed with 1:1000 dilution of anti-SRRM4 antibody (HPA052783; Atlas Antibodies AB) or 1:2000 dilution of anti-GAPDH (GT239; Genetex). Protein was visualized using Supersignal West Femto Chemiluminescent Substrate (Thermo Scientific).

Zhang X., Coleman I.M., Brown L.G., True L.D., Kollath L., Lucas J.M., Lam H.M., Dumpit R., Corey E., Chéry L., Lakely B., Higano C.S., Montgomery B., Roudier M., Lange P.H., Nelson P.S., Vessella R.L, & Morrissey C. (2015). SRRM4 Expression and the Loss of REST Activity May Promote the Emergence of the Neuroendocrine Phenotype in Castration-Resistant Prostate Cancer. Clinical cancer research : an official journal of the American Association for Cancer Research, 21(20), 4698-4708.

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Mouse Knockout Models for Innate Immunity

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Wild type C57BL/6 (6~8 weeks of age) and age-matched Ifnar1−/−, Stat1−/−, Myd88−/−, Trif−/−, Cardif−/−, Sting-gt/gt, and Irf3−/− male mice were either bred at the UCLA animal facility or purchased from the Jackson Laboratory. All mice experiments were performed in accordance with guidelines from the University of California, Los Angeles Institutional Animal Care and Use Committee. cGAMP, polyI:C, and polydA:dT were purchased from InvivoGen (San Diego, CA). LipidA was from Enzo life sciences (Farmingdale, NY). LPS (Escherichia coli 0111:B4), anti-α-tubulin antibody, human cGAS antibody (anti-C6ORF150), and anti-p204 antibody were from Sigma-Aldrich (St. Louis, MO). Anti-Ddx41 (H00051428) antibody was from Novus Biologicals (Littleton, CO). Anti-GAPDH (GT239) was from GeneTex (Irvine, CA). Recombinant human and mouse IFNα was from PBL interferon source (Piscataway, NJ) and recombinant mouse IFNγ was from R&D systems (Minneapolis, MN).

Ma F., Li B., Liu S.Y., Iyer S.S., Yu Y., Wu A, & Cheng G. (2015). Positive feedback regulation of type I IFN production by the IFN-inducible DNA sensor cGAS. Journal of immunology (Baltimore, Md. : 1950), 194(4), 1545-1554.

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Antibodies for Protein Analysis

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The following antibodies were used in this study: Anti-PrP antibodies 3F4 and 8H4 (Signet Laboratories, Dedham, MA), and SAF32 (189720, Cayman chemicals, USA), anti-ferritin (F5012, Sigma Aldrich, USA), anti-TfR (136800, Invitrogen, USA), anti-Tf (GTX2123, GeneTEX, USA), anti-ceruloplasmin (Dako, USA), Mouse IgG (5415, Cell signaling Technology, USA), anti-Fpn (NBP1-21502, Novus biological, USA), anti β-actin (MAB1501, Milipore, USA) and anti GAPDH (GT239, GeneTEX). HRP-conjugated anti-mouse, NA931V and anti-rabbit, NA934V (GE Healthcare, UK). Alexa Fluor-conjugated secondary antibodies (molecular probes), PNGase F (P0704S, NEB, USA). NAP (Non-animal protein) blocking solution (786-190T, G-Biosciences, USA), Hoechst (#33342, Invitrogen, USA), Fluoromount-G (Southern Biotech, USA).

Ashok A., Karmakar S., Chandel R., Ravikumar R., Dalai S., Kong Q, & Singh N. (2018). Prion protein modulates iron transport in the anterior segment: Implications for ocular iron homeostasis and prion transmission. Experimental eye research, 175, 1-13.

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Antibodies for Protein Analysis

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Western Blot Analysis of Autophagy Markers

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To verify the induction of autophagy, a Western blot analysis was conducted using 40 µg of the total protein extracted from the breast cancer (BC) cells. The cells were lysed using Cell Lysis Buffer II (Thermo-Fisher Scientific, Waltham, MA, USA), following treatment with DDC for 24 and 48 h as well as with the positive control resveratrol (Rv). The proteins were separated on 7.5 or 12% SDS-PAGE gels and subsequently transferred onto polyvinylidene fluoride (PVDF) membranes (both from Thermo-Fisher Scientific, Waltham, MA, USA). The membranes were blocked for 1 h using 5.0% (w/v) BSA in TTBS and then incubated overnight at 4 °C with primary antibodies: anti-mTOR-Ser2448 (Proteintech, Rosemont, Illinois, USA), anti-Beclin-1 (D40C5) (Cell Signaling Technology, Denver, MA, USA), anti-p62, and anti-LC3-II (GeneTex, Irvine, CA, USA). Anti-GAPDH (GT239) (GeneTex, Irvine, CA, USA) was employed as the loading control.
Following primary antibody incubation, the membranes were incubated for 2 h at room temperature with either anti-mouse IgG or anti-rabbit IgG secondary antibodies (1:5000) (Merck Group, Darmstadt, Germany) [28 (link)]. Bands were visualized using the 1-Step™ TMB-Blotting Substrate Solution (Thermo-Fisher Scientific, Waltham, MA, USA), which generates a blue precipitate. Band density was normalized and semi-quantified using the ImageJ V 1.8.0 software.

Mendez-Callejas G., Piñeros-Avila M., Celis C.A., Torrenegra R., Espinosa-Benitez A., Pestana-Nobles R, & Yosa-Reyes J. (2024). Natural 2′,4-Dihydroxy-4′,6′-dimethoxy Chalcone Isolated from Chromolaena tacotana Inhibits Breast Cancer Cell Growth through Autophagy and Mitochondrial Apoptosis. Plants, 13(5), 570.

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