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Polyclonal rabbit anti gapdh

Manufactured by Merck Group
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Polyclonal rabbit anti-GAPDH is a lab equipment product that detects the presence of the GAPDH protein in biological samples. It is a polyclonal antibody raised in rabbits against the GAPDH protein.

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Lab products found in correlation

Irdye 680 lt conjugated polyclonal donkey anti mouse igg, by LI COR (2 mentions) Irdye 800 cw conjugated polyclonal goat anti rabbit igg, by LI COR (2 mentions) Odyssey infrared imaging system, by LI COR (2 mentions) Rabbit monoclonal anti activated caspase 3, by Cell Signaling Technology (2 mentions) Rabbit anti actin, by Merck Group (2 mentions) Fetal calf serum (fcs), by Thermo Fisher Scientific (1 mentions) Pefablock, by Merck Group (1 mentions) Amikacin sulphate, by Merck Group (1 mentions) Rpmi 1640, by Thermo Fisher Scientific (1 mentions) L glutamine, by Thermo Fisher Scientific (1 mentions) Gentamicin, by Merck Group (1 mentions) Aprotinin, by Merck Group (1 mentions) Leupeptin, by Merck Group (1 mentions) Sodium orthovanadate, by Merck Group (1 mentions) Phosphatase inhibitor cocktail 3, by Merck Group (1 mentions) Nuclear extract kit, by Active Motif (1 mentions) Human asm cells, by Lonza (1 mentions) Polyclonal rabbit anti mlc, by Cell Signaling Technology (1 mentions) Anti mouse ig hrp, by Agilent Technologies (1 mentions) Anti rabbit ig hrp, by Agilent Technologies (1 mentions)

Close spelling variants of this product

Rabbit polyclonal anti-GAPDH antibody Rabbit anti-GAPDH Anti-GAPDH GAPDH Rabbit anti-

8 protocols using polyclonal rabbit anti gapdh

1

Antibody-based Protein Detection Protocol

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The following antibodies were obtained from commercial sources: monoclonal mouse anti-CD59 (MEM-43, Abcam, Cat. No. ab9182), monoclonal rabbit anti-flotillin-1 (D2V7J) XP (Cell Signaling, Cat. No. 18634), monoclonal mouse anti-flotillin-2 (BD Biosciences, Cat. No. 610383), polyclonal rabbit anti-GAPDH (Sigma, Cat. No. G9545), monoclonal rabbit anti-phospho-Src Family (Tyr416, Cell Signaling, Cat. No. 6943), monoclonal rabbit anti-Src Family (Cell Signaling, Cat. No. 2109), monoclonal rabbit anti-caveolin-1 (D46G3) XP (Cell Signaling, Cat. No. 3267). LecA was detected by a custom-made polyclonal rabbit anti-LecA antibody (Eurogentec, France).
The protease inhibitors Aprotinin, Leupeptin, Pefablock, Sodium orthovanadate and Phosphatase Inhibitor Cocktail 3 were all obtained from Sigma-Aldrich. RPMI 1640, DPBS-/-, FCS and l-Glutamine were all purchased from Gibco (Thermo Fisher Scientific). The following chemicals were obtained from Roth: BSA, DABCO, DAPI, EDTA, glycerol, LB, Mowiol, NaCl, sodium deoxycholate, NH4Cl, paraformaldehyde, SDS, Tris (hydroxymethyl)-aminoethane, Triton X-100 and Tween 20. Amikacin sulphate and Gentamicin were obtained from Sigma-Aldrich. StxB was purchased from Sigma-Aldrich (Cat. No. SML0562).
Brandel A., Aigal S., Lagies S., Schlimpert M., Meléndez A.V., Xu M., Lehmann A., Hummel D., Fisch D., Madl J., Eierhoff T., Kammerer B, & Römer W. (2021). The Gb3-enriched CD59/flotillin plasma membrane domain regulates host cell invasion by Pseudomonas aeruginosa. Cellular and Molecular Life Sciences, 78(7), 3637-3656.
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2

Western Blot Analysis of Nicotine-Induced NF-κB Activation

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Western blot analysis was performed as previously described [17] (link). After overnight serum starvation, primary lung fibroblasts ± nicotine (50 µg/ml) were cultured in complete serum-free media for 24–72 hours as noted in the figure legends. Cytoplasmic and nuclear protein fractions were isolated using the Nuclear Extract Kit (Active Motif, Carlsbad, CA) according to the manufacturer’s protocol. Primary antibodies employed included polyclonal rabbit anti-p65 (1∶1000, Cell-Signaling), polyclonal rabbit anti-phospho-p65 Ser536 (1∶500, Cell Signaling), monoclonal mouse anti β-tubulin (1∶500, Millipore), polyclonal rabbit anti-histone (1∶2000, Cell Signaling), and polyclonal rabbit anti-GAPDH (1∶10,000, Sigma). Secondary antibodies used were IRDye 680 LT conjugated polyclonal donkey anti-mouse IgG (1∶20,000, LI-COR Biosciences) and IRDye 800 CW conjugated polyclonal goat anti-rabbit IgG (1∶20,000, LI-COR Biosciences). Quantification of protein expression was performed by measuring integrated intensity using the Odyssey Infrared Imaging System (LI-COR Biosciences) and measuring densitometry using ImageJ software (National Institutes of Health) and then normalized to the appropriate loading control. Results are reported as fold change compared to untreated conditions.
Wongtrakool C., Grooms K., Bijli K.M., Crothers K., Fitzpatrick A.M, & Hart C.M. (2014). Nicotine Stimulates Nerve Growth Factor in Lung Fibroblasts through an NFκB-Dependent Mechanism. PLoS ONE, 9(10), e109602.
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3

Nicotine-Induced Smooth Muscle Cell Regulation

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After overnight serum starvation, human ASM cells (Lonza, Switzerland) ± nicotine (50 μg/ml, 72 h) and human ASM cells isolated from healthy and asthmatic donors were cultured in serum-free media. Primary antibodies employed included polyclonal rabbit anti-MLC (1:1000, Cell Signaling Technologies), polyclonal rabbit anti-phospho-MLC (1:500, Cell Signaling Technologies), and polyclonal rabbit anti-GAPDH (1:10,000, Sigma). Secondary antibodies used were IRDye 680LT conjugated polyclonal donkey anti-mouse IgG (1:20,000, LI-COR Biosciences) and IRDye 800CW conjugated polyclonal goat anti-rabbit IgG (1: 20,000, LI-COR Biosciences). Quantification of protein expression was performed by measuring integrated intensity using the Odyssey Infrared Imaging System (LI-COR Biosciences). Densitometry was used to quantify relative protein expression levels using Image J (National Institutes of Health). The band of the protein of interest was normalized to the appropriate loading control.
Galior K., Ma V.P., Liu Y., Su H., Baker N., Panettieri R J.r., Wongtrakool C, & Salaita K. (2018). Molecular Tension Probes to Investigate the Mechanopharmacology of Single Cells: A Step Towards Personalized Mechano-medicine. Advanced healthcare materials, 7(14), e1800069.
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4

Western Blot Detection of PAXX Protein

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To detect the PAXX protein by western blot, we used rabbit polyclonal anti‐PAXX/C9orf142 IgG (NovusBio, Littleton, CO, USA, NBP1‐94172, dilution 1 : 500), which recognizes the C‐terminal half of the PAXX protein (amino acids 109‐204); anti‐PAXX/C9orf142 IgG (Abcam, Cambridge, UK, ab126353, 1 : 200) and swine polyclonal anti‐rabbit Ig‐HRP (Dako antibodies, #P0399, 1 : 3000). Anti‐GAPDH rabbit polyclonal (Sigma, St. Louis, MO, USA, #G9545, developed to recognize 314–333 amino acids of mouse GAPDH, 1 : 2000) and mouse monoclonal anti‐β‐actin (Abcam, ab8226, 1 : 3000) with rabbit polyclonal anti‐mouse Ig‐HRP (Dako antibodies, #P0260, 1 : 3000) were used to control protein loading.
Gago‐Fuentes R., Xing M., Sæterstad S., Sarno A., Dewan A., Beck C., Bradamante S., Bjørås M, & Oksenych V. (2018). Normal development of mice lacking PAXX, the paralogue of XRCC4 and XLF. FEBS Open Bio, 8(3), 426-434.
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5

SUN1 and SUN2 Protein Detection

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Rabbit Monoclonal clone EPR6557 antibody against SUN2 was obtained from Millipore. Rabbit polyclonal antibody against SUN1 was obtained from Genetex. Anti-FLAG rabbit polyclonal, Anti-GAPDH rabbit polyclonal, anti-mouse Alexa 594, and anti-rabbit Alexa 488 were obtained from Sigma.
Persaud M., Selyutina A., Buffone C., Opp S., Donahue D.A., Schwartz O, & Diaz-Griffero F. (2021). Nuclear restriction of HIV-1 infection by SUN1. Scientific Reports, 11, 19128.
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6

Western Blot Analysis of Apoptosis Markers

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Western blot analysis was performed as previously reported36 (link). In brief, total cellular protein concentration was determined using BCA method then separated by SDS-PAGE and transferred to nitrocellulose (Schleicher and Schuell, Keene, NH). The primary antibodies used were , rabbit monoclonal anti-Smac/Diablo, rabbit monoclonal anti-cytochrome c, rabbit monoclonal anti-activated caspase-3, rabbit monoclonal anti-PARP, (Cell signaling Technology, MA, USA), rabbit monoclonal anti-Id1 (Calbioreagents, San Mateo, CA), rabbit anti-actin, an affinity isolated antigen specific antibody (Sigma, Saint Louis, MO), and rabbit polyclonal anti-GAPDH (Sigma) and mouse monoclonal anti-Spectrin (EMD Millipore, CA, USA). Rabbit monoclonal anti-pAMPKα(T172), rabbit monoclonal anti-AMPK, rabbit monoclonal-pACC(Ser79), rabbit monoclonal-anti-BMPR2 and rabbit monoclonal COX1/MT C01 were purchased from Cell signaling Technology, USA.
Mondal A., Jia D., Bhatt V., Akel M., Roberge J., Guo J.Y, & Langenfeld J. (2022). Ym155 localizes to the mitochondria leading to mitochondria dysfunction and activation of AMPK that inhibits BMP signaling in lung cancer cells. Scientific Reports, 12, 13135.
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7

Protein Extraction and Western Blot Analysis

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Total cellular protein was prepared using RIPA buffer containing a protease inhibitor cocktail and protein concentration was measured using the BCA assay as described [4 (link)]. In brief, protein was analyzed by SDS-PAGE, transferred to nitrocellulose (Schleicher and Schuell, Keene, NH). After blocking, the blots were incubated overnight at 4 °C with the appropriate primary antibody in Tris-buffered saline with 1 % Tween (TBST) and 5 % BSA. Secondary antibodies were applied for 1 h at room temperature. Specific proteins were detected using the enhanced chemiluminescence system (Amersham, Arlington Heights, IL). The primary antibodies that were used were rabbit monoclonal anti-pSmad 1/5, rabbit monoclonal anti-pSmad2, rabbit monoclonal anti-Smad2, rabbit monoclonal anti-pTAK1, rabbit monoclonal XIAP, rabbit anti-monoclonal p-p65, rabbit monoclonal anti-activated caspase-3, rabbit polyclonal anti-BMPRII, and rabbit monoclonal anti-EGR-1 (Cell signaling Technology, Danvers MA), Rabbit monoclonal anti-TAK1 (Invitrogen, Grand Island NY), rabbit anti-actin, an affinity isolated antigen specific antibody (Sigma, Saint Louis, MO), rabbit monoclonal anti-Id1 and rabbit monoclonal anti-Id3 (Calbioreagents, San Mateo, CA), rabbit polyclonal anti-GAPDH (Sigma, St. Louis, MO) and rabbit polyclonal pMEK-1/2 (Cell Signaling, Danvers MA).
Augeri D.J., Langenfeld E., Castle M., Gilleran J.A, & Langenfeld J. (2016). Inhibition of BMP and of TGFβ receptors downregulates expression of XIAP and TAK1 leading to lung cancer cell death. Molecular Cancer, 15, 27.
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8

Protein Extraction and Western Blot Analysis

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For the preparation of total cell extracts, tissue samples were homogenized in RIPA buffer (50 mMTris-HCl, pH 7.4, 150 mM NaCl, 1% Triton-X100, 0.5% sodium deoxycholate, 0.1% SDS) supplemented with 1 mM PMSF and 1% protease and phosphatase inhibitor cocktail (Sigma-Aldrich). Protein concentration was determined using the Bradford method [38] . Equivalent amounts (50 µg) of protein were subjected to electrophoresis on a 4-12% Mini-PROTEAN® TGX™ Gel (Bio-Rad) and transferred to a Hybond ECL nitrocellulose membrane (GE Healthcare Bio-Science). The following primary antibodies were used: rabbit polyclonal anti-GAPDH (1:5000, Sigma-Aldrich), rabbit polyclonal anti-STAT3 (1:1000, Sigma-Aldrich), rabbit polyclonal anti-phospho-STAT3 (1:1000, Cell Signaling Technology), and rabbit polyclonal anti-BDNF (1:500, Santa Cruz Biotechnology). An HRP-conjugated goat anti-rabbit IgG (1:5000, Jackson ImmunoResearch Laboratories) secondary antibody was used. Densitometric analysis of digitized images was performed using Chemidoc XRS Imaging Systems and Image LabTM Software (Bio-Rad).
Galvani G., Mottolese N., Gennaccaro L., Loi M., Medici G., Tassinari M., Fuchs C., Ciani E., & Trazzi S. (2021). Inhibition of Microglia Over-activation Restores Neuronal Survival in a Mouse Model of CDKL5 Deficiency Disorder.
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