C3G Background Information C3G is a guanine nucleotide exchange factor for Rap1 and is regulated by the expression of Crk adaptor proteins. C3G was originally isolated as one of the two major proteins bound to the SH3 domain of the Crk adaptor protein. Phosphorylation of Crk renders the SH3 domain inaccessible to C3G. C3G is dependent on Crk for phosphorylation and activation. Many kinds of stimulation induce binding of the Crk-C3G complex to a variety of phosphotyrosine-containing proteins, such as receptor tyrosine kinases. Crk activates C3G through phosphorylation on Tyrosine 504, which represses the cis-acting negative regulatory domain outside the catalytic region.
p-C3G (Tyr 504) Product Citations
See how others have used p-C3G (Tyr 504): sc-12926 antibody and or p-C3G (Tyr 504) antibody conjugates.
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p-C3G (Tyr 504)
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Western blot analysis of C3G phosphorylation in untreated (A,C) and lambda protein phosphatase (sc-200312A) treated (B,D) K-562 whole cell lysates. Antibodies tested include p-C3G (Tyr 504)-R: sc-12926-R (A,B) and C3G (H-300): sc-15359 (C,D).
