Cell Signaling Technology

Product Pathways - Tyrosine Kinase / Adaptors

Csk (C74C1) Rabbit mAb #4980

Applications Reactivity Sensitivity MW (kDa) Isotype
W H M R Mk Pg Endogenous 50 Rabbit IgG

Applications Key:  W=Western Blotting
Reactivity Key:  H=Human  M=Mouse  R=Rat  Mk=Monkey  Pg=Pig
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

Csk (C74C1) Rabbit mAb detects endogenous levels of total Csk protein. This antibody does not cross-react with other proteins.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding amino acid residue Val399 of human Csk.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell lines using Csk (C74C1) Rabbit mAb.

Background

Carboxy-terminal Src kinase (Csk) is a ubiquitously expressed nonreceptor tyrosine kinase that negatively regulates the Src family kinases (SFKs) by phosphorylation of the SFK carboxy-terminal tyrosine (1,2). Phosphorylated carboxy-terminal tyrosine binds to the SH2 domain of SFK intramolecularly and leads to folding and inactivation of the SFK (3). This Csk-catalyzed SFK tyrosine phosphorylation is highly specific and exclusive. The SFK carboxy-terminal tyrosine is the only known physiological substrate of Csk (4).Csk consists of an SH2, an SH3, and a kinase domain. There is evidence that the SH2 and SH3 domains are essential for the regulation of SFK, and Csk can be recruited to the membrane where SFKs are in an active state. This process is mediated by a Csk-binding protein (Cbp, also called PAG), which binds tightly to the SH2 domain of Csk (5). Activation of SFK by extracellular stimuli leads to the tyrosine phosphorylation of Cbp, generating docking sites for Csk. The recruitment of Csk forms a feedback mechanism for termination of SFK function (6).

  1. Nada, S. et al. (1991) Nature 351, 69-72.
  2. Nada, S. et al. (1993) Cell 73, 1125-1135.
  3. Lee, S. et al. (2003) Proc. Natl. Acad. Sci. USA 100, 14707-14712.
  4. Imamoto, A. and Soriano, P. (1993) Cell 73, 1117-1124.
  5. Kawabuchi, M. et al. (2000) Nature 404, 999-1003.
  6. Matsuoka, H. et al. (2004) J. Biol. Chem. 279, 5975-5983.

Application References

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For Research Use Only. Not For Use In Diagnostic Procedures.

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