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4g10 mouse anti phosphotyrosine antibody

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The 4G10 mouse anti-phosphotyrosine antibody is a laboratory reagent used to detect and quantify the presence of phosphorylated tyrosine residues in proteins. It is a specific and sensitive tool for researchers studying protein phosphorylation, a key regulatory mechanism in cellular signaling pathways.

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Lab products found in correlation

Ec10 mouse antibody, by Merck Group (3 mentions) V src antibody, by Merck Group (2 mentions)

Spelling variants of this product

Anti-phosphotyrosine 4G10 (36 citations) Anti-phosphotyrosine antibody (4G10, (34 citations) Anti-phosphotyrosine (27 citations) Phosphotyrosine (4G10; (16 citations) Anti-phosphotyrosine antibody (8 citations) Mouse anti-phosphotyrosine monoclonal antibody 4G10 (4 citations) 4G10 mouse anti-phosphotyrosine (3 citations) Mouse monoclonal anti-phosphotyrosine antibody (clone 4G10) (2 citations) Mouse anti-phosphotyrosine antibody (clone 4G10®) (2 citations)

5 protocols using 4g10 mouse anti phosphotyrosine antibody

1

Src Induction and Activation Analysis

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v-Src induction and activation were analyzed as described previously (Mollapour et al., 2011 (link)). Expressed v-Src protein was detected with EC10 mouse antibody (Millipore) and v-Src activity with 4G10 mouse anti-phosphotyrosine antibody (Millipore). GR assay was performed as described previously (Garabedian and Yamamoto, 1992 (link)), as was measurement of HSE-LacZ expression (Hjorth-Sørensen et al., 2001 (link)). STE11ΔN induction was analyzed as described previously (Flom et al., 2008 (link); Louvion et al., 1998 (link)). Additional details are found in Supplemental Information.
Dunn D.M., Woodford M.R., Truman A.W., Jensen S.M., Schulman J., Caza T., Remillard T.C., Loiselle D., Wolfgeher D., Blagg B.S., Franco L., Haystead T.A., Daturpalli S., Mayer M.P., Trepel J.B., Morgan R.M., Prodromou C., Kron S.J., Panaretou B., Stetler-Stevenson W.G., Landas S.K., Neckers L., Bratslavsky G., Bourboulia D, & Mollapour M. (2015). c-Abl Mediated Tyrosine Phosphorylation of Aha1 Activates Its Co-chaperone Function in Cancer Cells. Cell reports, 12(6), 1006-1018.
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2

Src Induction and Activation Analysis

Cited 1 time
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v-Src induction and activation were analyzed as described previously (Mollapour et al., 2011 (link)). Expressed v-Src protein was detected with EC10 mouse antibody (Millipore) and v-Src activity with 4G10 mouse anti-phosphotyrosine antibody (Millipore). GR assay was performed as described previously (Garabedian and Yamamoto, 1992 (link)), as was measurement of HSE-LacZ expression (Hjorth-Sørensen et al., 2001 (link)). STE11ΔN induction was analyzed as described previously (Flom et al., 2008 (link); Louvion et al., 1998 (link)). Additional details are found in Supplemental Information.
Dunn D.M., Woodford M.R., Truman A.W., Jensen S.M., Schulman J., Caza T., Remillard T.C., Loiselle D., Wolfgeher D., Blagg B.S., Franco L., Haystead T.A., Daturpalli S., Mayer M.P., Trepel J.B., Morgan R.M., Prodromou C., Kron S.J., Panaretou B., Stetler-Stevenson W.G., Landas S.K., Neckers L., Bratslavsky G., Bourboulia D, & Mollapour M. (2015). c-Abl Mediated Tyrosine Phosphorylation of Aha1 Activates Its Co-chaperone Function in Cancer Cells. Cell reports, 12(6), 1006-1018.
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3

Measuring v-Src Activity and Transcriptional Reporters

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Expressed v-Src protein were detected with v-Src antibody (Millipore). v-Src activity was determined by detecting tyrosine phosphorylation with 4G10 mouse anti-phosphotyrosine antibody (Millipore). β-galactosidase assay for measuring GRE-LacZ expression (Garabedian and Yamamoto, 1992 (link)), ERE-LacZ (Picard et al., 1990 (link)), HSE-LacZ expression (Hjorth-Sorensen et al., 2001 (link)), and RLM1-LacZ (Truman et al., 2006 (link)) were described previously (Mollapour et al., 2014 (link)). Note that GRE-LacZ reporter was also used to measure AR activity (Picard et al., 1990 (link)).
Backe S.J., Sager R.A., Regan B.R., Sit J., Major L.A., Bratslavsky G., Woodford M.R., Bourboulia D, & Mollapour M. (2022). A specialized Hsp90 co-chaperone network regulates steroid hormone receptor response to ligand. Cell reports, 40(2), 111039.
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4

Analyzing v-Src Induction and Activation

Cited 1 time
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v-Src induction and activation were analyzed as described previously (Mollapour et al., 2011b (link)). Expressed v-Src protein was detected with EC10 mouse antibody (Millipore) and v-Src activity with 4G10 mouse anti-phosphotyrosine antibody (Millipore). GR assay was performed as described previously (Garabedian and Yamamoto, 1992 (link)), as was measurement of HSE-LacZ expression (Hjorth-Sorensen et al., 2001 (link)). Ste11ΔN induction was analyzed as described previously (Flom et al., 2008 (link); Louvion et al., 1998 (link)). Ste11ΔN plasmid is a gift of Jill Johnson. Additional details are found in Supplemental Data.
Mollapour M., Bourboulia D., Beebe K., Woodford M.R., Polier S., Hoang A., Chelluri R., Li Y., Guo A., Lee M.J., Fotooh-Abadi E., Khan S., Prince T., Miyajima N., Yoshida S., Tsutsumi S., Xu W., Panaretou B., Stetler-Stevenson W.G., Bratslavsky G., Trepel J.B., Prodromou C, & Neckers L. (2014). Asymmetric Hsp90 N-domain SUMOylation recruits Aha1 and ATP-competitive inhibitors. Molecular cell, 53(2), 317-329.
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5

Measuring v-Src Activity and Transcriptional Reporters

Cited 1 time
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Expressed v-Src protein were detected with v-Src antibody (Millipore). v-Src activity was determined by detecting tyrosine phosphorylation with 4G10 mouse anti-phosphotyrosine antibody (Millipore). β-galactosidase assay for measuring GRE-LacZ expression (Garabedian and Yamamoto, 1992 (link)), ERE-LacZ (Picard et al., 1990 (link)), HSE-LacZ expression (Hjorth-Sorensen et al., 2001 (link)), and RLM1-LacZ (Truman et al., 2006 (link)) were described previously (Mollapour et al., 2014 (link)). Note that GRE-LacZ reporter was also used to measure AR activity (Picard et al., 1990 (link)).
Backe S.J., Sager R.A., Regan B.R., Sit J., Major L.A., Bratslavsky G., Woodford M.R., Bourboulia D, & Mollapour M. (2022). A specialized Hsp90 co-chaperone network regulates steroid hormone receptor response to ligand. Cell reports, 40(2), 111039.
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