Cell Signaling Technology

Product Pathways - Tyrosine Kinase/ Adaptors

Phospho-Src (Tyr527) Antibody #2105

Applications Reactivity MW (kDa) Source
W IHC-P H M R (C) 60 Rabbit

Applications Key:  W=Western Blotting  IHC-P=Immunohistochemistry (Paraffin)
Reactivity Key:  H=Human  M=Mouse  R=Rat  C=Chicken
Species enclosed in parentheses are predicted to react based on 100% sequence homology. Species cross-reactivity is determined by Western blot.

Specificity / Sensitivity

Phospho-Src (Tyr527) Antibody detects endogenous levels of Src only when phosphorylated at Tyr527. The antibody may cross-react with other Src family members such as Yes, Fyn, Fgr and Yrk when phosphorylated at the equivalent sites.

Source / Purification

Polyclonal antibodies are produced by immunizing rabbits with a synthetic phospho-peptide (KLH-coupled) corresponding to residues surrounding Tyr527 of human Src. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from NIH/3T3 cells, using Phospho-Src (Tyr527) Antibody (A,B) or v-Src antibody (C,D). The phospho-specificity of the antibody was confirmed by treating the membrane with calf intestinal alkaline phosphatase (CIP) (B,D) after Western transfer.

IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human breast carcinoma, showing membrane and cytoplasmic localization using Phospho-Src (Tyr527) Antibody.

Background

The Src family of protein tyrosine kinases (including 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. Phosphorylation of Tyr416 in the activation loop of the kinase domain by Csk upregulates enzyme activity, whereas phosphorylation of Tyr527 in the carboxy-terminal tail renders the enzyme less active (2).

  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.

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