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一般說明
SRC proto-oncogene, non-receptor tyrosine kinase (SRC) belongs to the family of non-receptor tyrosine kinases. It contains an amino-terminal domain, conserved Src-homology domains (SH2 and SH3), a tyrosine kinase domain and the carboxyl-terminus. The gene encoding this protein is localized on human chromosome 20q11.23.
應用
Human Src has been used to study the kinetics of Src entrapped in a series of different sol-gel derived materials.
生化/生理作用
SRC proto-oncogene, non-receptor tyrosine kinase (SRC) phosphorylates membrane proteins and nucleoproteins and activates various intracellular signaling cascades. It has been associated with a number of human malignancies and cancers.
單位定義
One unit will phosphorylate one nmole of poly(Gly:Tyr) 4:1 per minute at pH 7.5 at 30°C.
外觀
Solution in 50 mM Tris pH 7.5, 0.05 mM EDTA, 1 mM DTT, 100 mM NaCl, 0.05% NP-40, and 50% glycerol.
儲存類別代碼
12 - Non Combustible Liquids
水污染物質分類(WGK)
WGK 1
閃點(°F)
Not applicable
閃點(°C)
Not applicable
The Tyrosine Kinase c-Src Specifically Binds to the Active Integrin aIIb?3 to Initiate Outside-in Signaling in Platelets.
Wu Y
The Journal of Biological Chemistry (2015)
T R Lee et al.
The Journal of biological chemistry, 270(10), 5375-5380 (1995-03-10)
We report the first active site substrate specificity analysis of a tyrosine-specific protein kinase, namely pp60c-src. Like the cAMP-dependent protein kinase and protein kinase C, pp60c-src will phosphorylate an assortment of achiral residues attached to active site-directed peptides. Furthermore, pp60c-src
J D Bjorge et al.
The Journal of biological chemistry, 270(41), 24222-24228 (1995-10-13)
Two activated transforming mutants of human pp60c-src were found to possess single point mutations within the regulatory carboxyl terminus (E527K in CY CST201) and the kinase domain (E381G in WO CST1), respectively, that do not directly interfere with either the
Subcellular and Dynamic Coordination between Src Activity and Cell Protrusion in Microenvironment.
Zhuo Y
Scientific Reports (2015)
SH3 domain of c-Src governs its dynamics at focal adhesions and the cell membrane.
Machiyama H
FEBS Journal (2015)
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