|Datasheet||Specific References||Reviews||Related Products||Protocols|
|Vector Type||Mammalian Expression Vector|
|Expression Method||Constiutive, Stable / Transient|
|Selection In Mammalian Cells||Hygromycin|
Human influenza hemagglutinin (HA) is a surface glycoprotein required for the infectivity of the human virus. The HA tag is derived from the HA-molecule corresponding to amino acids 98-106 has been extensively used as a general epitope tag in expression vectors. Many recombinant proteins have been engineered to express the HA tag, which does not appear to interfere with the bioactivity or the biodistribution of the recombinant protein. This tag facilitates the detection, isolation, and purification of the proteins.
The actual HA tag is as follows: 5' TAC CCA TAC GAT GTT CCA GAT TAC GCT 3' or 5' TAT CCA TAT GAT GTT CCA GAT TAT GCT 3' The amino acid sequence is: YPYDVPDYA.
|Human CSK ORF mammalian expression plasmid, C-GFPSpark tag||HG10740-ACG|
|Human CSK ORF mammalian expression plasmid, C-OFPSpark / RFP tag||HG10740-ACR|
|Human CSK ORF mammalian expression plasmid, N-GFPSpark tag||HG10740-ANG|
|Human CSK ORF mammalian expression plasmid, N-OFPSpark / RFP tag||HG10740-ANR|
|Human CSK ORF mammalian expression plasmid, C-Flag tag||HG10740-CF|
|Human CSK ORF mammalian expression plasmid, C-His tag||HG10740-CH|
|Human CSK ORF mammalian expression plasmid, C-Myc tag||HG10740-CM|
|Human CSK ORF mammalian expression plasmid, C-HA tag||HG10740-CY|
|Human CSK Gene cDNA clone plasmid||HG10740-M|
|Human CSK ORF mammalian expression plasmid, N-Flag tag||HG10740-NF|
|Human CSK ORF mammalian expression plasmid, N-His tag||HG10740-NH|
|Human CSK ORF mammalian expression plasmid, N-Myc tag||HG10740-NM|
|Human CSK ORF mammalian expression plasmid, N-HA tag||HG10740-NY|
|Human CSK natural ORF mammalian expression plasmid||HG10740-UT|
|Learn more about expression Vectors|
The tyrosine kinase c-Src has been implicated as a modulator of cell proliferation, spreading, and migration. These functions are also regulated by Met. The structure of a large fragment of the c-Src kinase comprises the regulatory and kinase domains and the carboxy-terminal tall. c-Src kinase interactions among domains and is stabilized by binding of the phosphorylated tail to the SH2 domain. This molecule is locked in a conformation that simultaneously disrupts the kinase active site and sequesters the binding surfaces of the SH2 and SH3 domains. The structure shows how appropriate cellular signals, or transforming mutations in v-Src, could break these interactions to produce an open, active kinase. The protein-tyrosine kinase activity of c-Src kinase is inhibited by phosphorylation of tyr527, within the c-Src c-terminal tail. Genetic and biochemical data have suggested that this negative regulation requires an intact Src homology 2 (SH2) domain. Since SH2 domains recognize phosphotyrosine, it is possible that these two non-catalytic domains associate, and thereby repress c-Src kinase activity. Experiments have suggested that c-Src kinase plays a role in the biological behaviour of colonic carcinoma cells induced by migratory factors such as EGF, perhaps acting in conjunction with FAK to regulate focal adhesion turnover and tumour cell motility. Furthermore, although c-Src kinase has been implicated in colonic tumour progression, in the adenoma to carcinoma in vitro model c-Src is not the driving force for this progression but co-operates with other molecules in carcinoma development.