|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 EREG ORF mammalian expression plasmid, C-GFPSpark tag||HG10677-ACG|
|Human EREG ORF mammalian expression plasmid, C-OFPSpark / RFP tag||HG10677-ACR|
|Human EREG ORF mammalian expression plasmid, C-Flag tag||HG10677-CF|
|Human EREG ORF mammalian expression plasmid, C-His tag||HG10677-CH|
|Human EREG ORF mammalian expression plasmid, C-Myc tag||HG10677-CM|
|Human EREG ORF mammalian expression plasmid, C-HA tag||HG10677-CY|
|Human EREG Gene cDNA clone plasmid||HG10677-M|
|Human EREG ORF mammalian expression plasmid, Flag tag||HG10677-M-F|
|Human EREG ORF mammalian expression plasmid, N-Flag tag||HG10677-NF|
|Human EREG ORF mammalian expression plasmid, N-His tag||HG10677-NH|
|Human EREG ORF mammalian expression plasmid, N-Myc tag||HG10677-NM|
|Human EREG ORF mammalian expression plasmid, N-HA tag||HG10677-NY|
|Human EREG natural ORF mammalian expression plasmid||HG10677-UT|
|Learn more about expression Vectors|
Epiregulin (EREG) is a member of the epidermal growth factor family. Epiregulin (EREG) can function as a ligand of EGFR (epidermal growth factor receptor), as well as a ligand of most members of the ERBB (v-erb-b2 oncogene homolog) family of tyrosine-kinase receptors. Epiregulin (EREG) exhibit bifunctional regulatory properties: it inhibit the growth of several epithelial tumor cells and stimulated the growth of fibroblasts and various other types of cells. Epiregulin (EREG) bound to the EGF receptors of epidermoid carcinoma A431 cells much more weakly than did EGF, but was nevertheless much more potent than EGF as a mitogen for rat primary hepatocytes and Balb/c 3T3 A31 fibroblasts. These findings suggest that epiregulin (EREG) plays important roles in regulating the growth of epithelial cells and fibroblasts by binding to receptors for EGF-related ligands. Epiregulin (EREG) is the broadest specificity EGF-like ligand so far characterized: not only does it stimulate homodimers of both ErbB-1 and ErbB-4, it also activates all possible heterodimeric ErbB complexes.