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Ab51013

Manufactured by Abcam
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AB51013 is a monoclonal antibody that targets the protein GAPDH (Glyceraldehyde 3-phosphate dehydrogenase). GAPDH is a key enzyme involved in glycolysis, a fundamental metabolic pathway. This antibody can be used for the detection and quantification of GAPDH in various sample types.

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Lab products found in correlation

Ab184565, by Abcam (3 mentions) Ab129002, by Abcam (2 mentions) Star117p, by Bio-Rad (2 mentions) Dylight680, by Cell Signaling Technology (2 mentions) Fusion fx imaging system, by Vilber (2 mentions) Laemmli 2xbuffer, by Merck Group (2 mentions) Ls b10851, by LifeSpan BioSciences (2 mentions) F1804 or f3165, by Merck Group (2 mentions) Dylight800, by Cell Signaling Technology (2 mentions) Star54, by Bio-Rad (2 mentions) Passive lysis buffer (plb), by Promega (2 mentions) Mini protean tgx precast gel, by Bio-Rad (2 mentions) A2103, by Merck Group (1 mentions) Flag m2 antibody f1804, by Merck Group (1 mentions) Gtx118991, by GeneTex (1 mentions) Ab200836, by Abcam (1 mentions) Immobilon western chemiluminescent hrp substrate kit, by Merck Group (1 mentions) Na934v, by GE Healthcare (1 mentions) Na931v, by GE Healthcare (1 mentions) Phenylmethylsulfonyl fluoride, by Merck Group (1 mentions)

4 protocols using ab51013

1

Western Blot Procedure for ANP32 Proteins

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Cells were lysed in Passive Lysis buffer (Promega) or NP40 lysis buffer (for cellular fractionation) and prepared in Laemmli 2xbuffer (Sigma-Aldrich). Cell proteins were resolved by SDS-PAGE using Mini-PROTEAN® TGX™ Precast Gels (Bio-Rad). Immunoblotting was carried out using the following primary antibodies: α-chANP32A rabbit polyclonal (LS-B10851, LifeSpan BioSciences, Inc.), α-huANP32A rabbit polyclonal (AB51013, Abcam), α-huANP32B rabbit monoclonal (AB184565, Abcam), α-vinculin rabbit monoclonal (AB129002, Abcam), α-FLAG® M2 mouse monoclonal (F1804 or F3165, Sigma-Aldrich), α-PB2 rabbit polyclonal (2N580, a kind gift from Paul Digard, Roslin Institute), and followed with secondary horseradish peroxidase-conjugated (HRP) antibodies: α-mouse IgG (H/L):HRP goat polyclonal (STAR117P, AbD Serotec) and α-rabbit IgG:HRP sheep polyclonal (STAR54, AbD Serotec). For quantification of cellular fractions, the following secondary antibodies were used: α-rabbit IgG (H/L):DyLight™ 800 (5151P, Cell signalling) and α-mouse IgG (H/L):DyLight™ 680 (5470P, Cell signalling). Protein bands were visualised by chemiluminescence (ECL+ western blotting substrate, Pierce) using a FUSION-FX imaging system (Vilber Lourmat).
Long J.S., Giotis E.S., Moncorgé O., Frise R., Mistry B., James J., Morisson M., Iqbal M., Vignal A., Skinner M.A, & Barclay W.S. (2016). Species difference in ANP32A underlies influenza A virus polymerase host restriction. Nature, 529(7584), 101-104.
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2

Western Blot Procedure for ANP32 Proteins

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Cells were lysed in Passive Lysis buffer (Promega) or NP40 lysis buffer (for cellular fractionation) and prepared in Laemmli 2xbuffer (Sigma-Aldrich). Cell proteins were resolved by SDS-PAGE using Mini-PROTEAN® TGX™ Precast Gels (Bio-Rad). Immunoblotting was carried out using the following primary antibodies: α-chANP32A rabbit polyclonal (LS-B10851, LifeSpan BioSciences, Inc.), α-huANP32A rabbit polyclonal (AB51013, Abcam), α-huANP32B rabbit monoclonal (AB184565, Abcam), α-vinculin rabbit monoclonal (AB129002, Abcam), α-FLAG® M2 mouse monoclonal (F1804 or F3165, Sigma-Aldrich), α-PB2 rabbit polyclonal (2N580, a kind gift from Paul Digard, Roslin Institute), and followed with secondary horseradish peroxidase-conjugated (HRP) antibodies: α-mouse IgG (H/L):HRP goat polyclonal (STAR117P, AbD Serotec) and α-rabbit IgG:HRP sheep polyclonal (STAR54, AbD Serotec). For quantification of cellular fractions, the following secondary antibodies were used: α-rabbit IgG (H/L):DyLight™ 800 (5151P, Cell signalling) and α-mouse IgG (H/L):DyLight™ 680 (5470P, Cell signalling). Protein bands were visualised by chemiluminescence (ECL+ western blotting substrate, Pierce) using a FUSION-FX imaging system (Vilber Lourmat).
Long J.S., Giotis E.S., Moncorgé O., Frise R., Mistry B., James J., Morisson M., Iqbal M., Vignal A., Skinner M.A, & Barclay W.S. (2016). Species difference in ANP32A underlies influenza A virus polymerase host restriction. Nature, 529(7584), 101-104.
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3

Influenza Virus Protein Interactions

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Polymerase reconstitution assays, vPol interaction assays (co-immunoprecipitations), and western blot analyses were all performed using standard described methods15 (link). FLAG-tagged constructs were detected using FLAG M2 antibody F1804 (Sigma; 1:2000 dilution), PB2 was detected using a custom rabbit polyclonal anti-serum (1:2000 dilution), PA was detected using antibody GTX118991 (Genetex; 1:2000 dilution), actin was detected using antibody A2103 (Sigma; 1:3000 dilution), and ANP32A and ANP32B were detected using antibodies ab51013 and ab184565 (Abcam; 1:1000 dilution), respectively.
Domingues P., Eletto D., Magnus C., Turkington H.L., Schmutz S., Zagordi O., Lenk M., Beer M., Stertz S, & Hale B.G. (2019). Profiling host ANP32A splicing landscapes to predict influenza A virus polymerase adaptation. Nature Communications, 10, 3396.
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4

Western Blot Analysis of Actin, FLAG, PHAP1, and PHAPI2

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For Western blot analysis, cells were lysed in NP-40 lysis buffer containing 1× cOmplete Protease Inhibitor Cocktail (Roche) and 1× Phenylmethylsulfonyl fluoride (Sigma-Aldrich) and cleared from the insoluble fraction by centrifugation at 17,000 × g for 5 min at 4°C. Samples were analyzed by SDS-PAGE and transferred onto nitrocellulose membranes. Membranes were probed with mouse monoclonal anti-Actin (Thermo Scientific, MS-1295), mouse monoclonal anti-FLAG M2 (Sigma-Aldrich, F1804), rabbit polyclonal anti-PHAP1 (Abcam, ab51013), and rabbit monoclonal anti-PHAPI2 (Abcam, ab200836) antibodies. Primary antibodies were detected using HRP-conjugated secondary anti-mouse (GE Healthcare, NA931V) and anti-rabbit (GE Healthcare, NA934V) antibodies and visualized using Immobilon Western Chemiluminescent HRP substrate kit (Millipore) according to the manufacturer’s instructions.
Nilsson-Payant B.E., tenOever B.R, & te Velthuis A.J. (2022). The Host Factor ANP32A Is Required for Influenza A Virus vRNA and cRNA Synthesis. Journal of Virology, 96(4), e02092-21.
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