Applications
WB;IHC;IF;FCM;ELISA
Antibody type
Monoclonal antibodies
Protein name
Adapter molecule crk
Immunogen
Purified recombinant fragment of human Crk II expressed in E. Coli.
Specificity
Crk II Monoclonal Antibody detects endogenous levels of Crk II protein.
Constitute
Ascitic fluid containing 0.03% sodium azide,0.5% BSA, 50%glycerol.
Dilution rate
Western Blot: 1/500 - 1/2000. Immunohistochemistry: 1/200 - 1/1000. Immunofluorescence: 1/200 - 1/1000. Flow cytometry: 1/200 - 1/400. ELISA: 1/10000. Not yet tested in other applications.
Purification process
Affinity purification
Other name
CRK; Adapter molecule crk; Proto-oncogene c-Crk; p38
Background
This gene encodes a member of an adapter protein family that binds to several tyrosine-phosphorylated proteins. The product of this gene has several SH2 and SH3 domains (src-homology domains) and is involved in several signaling pathways, recruiting cytoplasmic proteins in the vicinity of tyrosine kinase through SH2-phosphotyrosine interaction. The N-terminal SH2 domain of this protein functions as a positive regulator of transformation whereas the C-terminal SH3 domain functions as a negative regulator of transformation. Two alternative transcripts encoding different isoforms with distinct biological activity have been described. [provided by RefSeq, Jul 2008],
Function
domain:The C-terminal SH3 domain function as a negative modulator for transformation and the N-terminal SH3 domain appears to function as a positive regulator for transformation.,domain:The SH2 domain mediates interaction with SHB.,function:The Crk-I and Crk-II forms differ in their biological activities. Crk-II has less transforming activity than Crk-I. Crk-II mediates attachment-induced MAPK8 activation, membrane ruffling and cell motility in a Rac-dependent manner. Involved in phagocytosis of apoptotic cells and cell motility via its interaction with DOCK1 and DOCK4.,PTM:Phosphorylated on Tyr-221 upon cell adhesion. Results in the negative regulation of the association with SH2- and SH3-binding partners, possibly by the formation of an intramolecular interaction of phosphorylated Tyr-221 with the SH2 domain. This leads finally to the down-regulation of the Crk signaling pathway.,PTM:P
