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Product Includes Quantity Applications Reactivity MW(kDa) Isotype
Phospho-Src Family (Tyr416) (D49G4) Rabbit mAb 6943 x 40 µl
H M R 60 Rabbit IgG
Non-phospho-Src (Tyr527) Antibody 2107 x 40 µl
H M R 60 Rabbit 
Non-phospho-Src (Tyr416) (7G9) Mouse mAb 2102 x 40 µl
H M R 60 Mouse IgG2b
Phospho-Src (Tyr527) Antibody 2105 x 40 µl
H M R 60 Rabbit 
Src (32G6) Rabbit mAb 2123 x 40 µl
H M R 60 Rabbit IgG
Anti-rabbit IgG, HRP-linked Antibody 7074 x 100 µl
All Goat 
Anti-mouse IgG, HRP-linked Antibody 7076 x 100 µl
All Horse 

Product Description

The Src Antibody Sampler kit provides an economical means of evaluating total Src protein levels and its phosphorylation status. The kit contains enough primary and secondary antibodies to perform four Western blot experiments per primary antibody.


Specificity / Sensitivity

Each antibody in the kit detects endogenous levels of Src only when in the indicated phosphorylation state at the indicated residue. The antibodies may cross-react with other Src family members when in equivalent phosphorylation states.


Source / Purification

Polyclonal antibodies are produced by immunizing animals with synthetic phospho- or non-phosphopeptides corresponding to residues surrounding Tyr527 of human Src protein. The mouse monoclonal antibody is produced by immunizing animals with a synthetic non-phosphopeptide corresponding to residues surrounding Tyr416 of human Src protein. The rabbit monoclonal antibody for P-Src Y416 is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr416 of human Src protein. The Src (32G6) rabbit monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the amino-terminus of human Src. Polyclonal antibodies are purified by protein A and peptide affinity chromatography.

The Src family of protein tyrosine kinases, which includes Src, Lyn, Fyn, Yes, Lck, Blk, and Hck, are important in the regulation of growth and differentiation of eukaryotic cells (1). Src activity is regulated by tyrosine phosphorylation at two sites, but with opposing effects. While phosphorylation at Tyr416 in the activation loop of the kinase domain upregulates enzyme activity, phosphorylation at Tyr527 in the carboxy-terminal tail by Csk renders the enzyme less active (2).


Lyn is a member of the Src family that is predominantly expressed in hematopoietic cells (3). Lyn participates in signaling from multiple cell surface receptors such as the B cell Ag receptor (BCR) and CD40 (4).

Lck is essential for T-lymphocyte activation and differentiation (5,6). The activity of Lck is regulated by protein kinases and phosphatases. Phosphorylation of the C-terminal tyrosine 505 serves to downregulate Lck catalytic activity, while phosphorylation at tyrosine 394 leads to an increase in Lck activity (7).


1.  Thomas, S.M. and Brugge, J.S. (1997) Annu Rev Cell Dev Biol 13, 513-609.

2.  Hunter, T. (1987) Cell 49, 1-4.

3.  Yamanashi, Y. et al. (1989) Proc. Natl. Acad. Sci. USA 86, 6538-6542.

4.  Yamanashi, Y. et al. (1991) Science 251, 192-194.

5.  Molina, T. J. et al. (1992) Nature 357, 161-164.

6.  Straus, D. B. et al. (1992) Cell 70, 585-593.

7.  Chow, L. M. et al. (1993) Nature 365, 156-160.


Entrez-Gene Id 2534, 3055, 3932, 4067, 6714, 7525
Swiss-Prot Acc. P06241, P08631, P06239, P07948, P12931, P07947

Protein Specific References

Nguyen TH et al. (2002) J Biol Chem 277, 24274–9

Nguyen TH et al. (2002) J Biol Chem 277, 24274–9

Alonso A et al. (2004) J Biol Chem 279, 4922–8

Chichili GR and Rodgers W (2007) J Biol Chem 282, 36682–91

Wagner MJ and Smiley JR (2009) J Virol 83, 12452–61

Alonso A et al. (2004) J Biol Chem 279, 4922–8

Chichili GR and Rodgers W (2007) J Biol Chem 282, 36682–91

Wagner MJ and Smiley JR (2009) J Virol 83, 12452–61

Motiwala T et al. (2010) J Cell Biochem 110, 846–56

Jin LL et al. (2010) J Proteome Res 9, 2752–61

Motiwala T et al. (2010) J Cell Biochem 110, 846–56

Jin LL et al. (2010) J Proteome Res 9, 2752–61

Wang YH et al. (2001) Am J Physiol Cell Physiol 281, C1667–75

Schmitt JM and Stork PJ (2002) Mol Cell 9, 85–94

Abrahamsen H et al. (2003) J Biol Chem 278, 17170–7

Kim M et al. (2004) Oncogene 23, 1645–55

Zhou S et al. (2004) J Biol Chem 279, 54463–9

Ren Y et al. (2004) J Biol Chem 279, 8497–505

Kim HP et al. (2004) Biochem J 379, 141–50

Feistritzer C et al. (2005) Exp Cell Res 305, 214–20

Daoud G et al. (2006) J Physiol 571, 537–53

Eichhorn PJ et al. (2007) PLoS Genet 3, e218

Zhu S et al. (2007) Cancer Res 67, 10129–37

Zhou, J. et al. (2003) J Biol Chem 278, 6936-41.

Wang YH et al. (2001) Am J Physiol Cell Physiol 281, C1667–75

Schmitt JM and Stork PJ (2002) Mol Cell 9, 85–94

Abrahamsen H et al. (2003) J Biol Chem 278, 17170–7

Kim M et al. (2004) Oncogene 23, 1645–55

Zhou S et al. (2004) J Biol Chem 279, 54463–9

Ren Y et al. (2004) J Biol Chem 279, 8497–505

Kim HP et al. (2004) Biochem J 379, 141–50

Feistritzer C et al. (2005) Exp Cell Res 305, 214–20

Daoud G et al. (2006) J Physiol 571, 537–53

Eichhorn PJ et al. (2007) PLoS Genet 3, e218

Zhu S et al. (2007) Cancer Res 67, 10129–37

Zhou, J. et al. (2003) J Biol Chem 278, 6936-41.

Wang YH et al. (2001) Am J Physiol Cell Physiol 281, C1667–75

Schmitt JM and Stork PJ (2002) Mol Cell 9, 85–94

Abrahamsen H et al. (2003) J Biol Chem 278, 17170–7

Kim M et al. (2004) Oncogene 23, 1645–55

Zhou S et al. (2004) J Biol Chem 279, 54463–9

Ren Y et al. (2004) J Biol Chem 279, 8497–505

Kim HP et al. (2004) Biochem J 379, 141–50

Feistritzer C et al. (2005) Exp Cell Res 305, 214–20

Daoud G et al. (2006) J Physiol 571, 537–53

Eichhorn PJ et al. (2007) PLoS Genet 3, e218

Zhu S et al. (2007) Cancer Res 67, 10129–37

Zhou, J. et al. (2003) J Biol Chem 278, 6936-41.

Wang YH et al. (2001) Am J Physiol Cell Physiol 281, C1667–75

Schmitt JM and Stork PJ (2002) Mol Cell 9, 85–94

Abrahamsen H et al. (2003) J Biol Chem 278, 17170–7

Kim M et al. (2004) Oncogene 23, 1645–55

Zhou S et al. (2004) J Biol Chem 279, 54463–9

Ren Y et al. (2004) J Biol Chem 279, 8497–505

Kim HP et al. (2004) Biochem J 379, 141–50

Feistritzer C et al. (2005) Exp Cell Res 305, 214–20

Daoud G et al. (2006) J Physiol 571, 537–53

Eichhorn PJ et al. (2007) PLoS Genet 3, e218

Zhu S et al. (2007) Cancer Res 67, 10129–37

Zhou, J. et al. (2003) J Biol Chem 278, 6936-41.


For Research Use Only. Not For Use In Diagnostic Procedures.
Cell Signaling Technology® is a trademark of Cell Signaling Technology, Inc.
U.S. Patent No. 5,675,063.