S5439
Src human
≥80% (SDS-PAGE), recombinant, expressed in baculovirus infected insect cells, buffered aqueous glycerol solution, histidine-tagged
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recombinant
expressed in baculovirus infected insect cells
Assay
≥80% (SDS-PAGE)
form
buffered aqueous glycerol solution
mol wt
60 kDa
concentration
~0.58 mg/mL protein (Bradford assay)
UniProt accession no.
application(s)
cell analysis
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... SRC(6714)
General description
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.
Application
Human Src has been used to study the kinetics of Src entrapped in a series of different sol-gel derived materials.
Biochem/physiol Actions
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.
Unit Definition
One unit will phosphorylate one nmole of poly(Gly:Tyr) 4:1 per minute at pH 7.5 at 30°C.
Physical form
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.
Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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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
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
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)
Entrapment of Src Protein Tyrosine Kinase in Sugar-Modified Silica
Jorge A
Analytical Chemistry (2004)
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