|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 PRSS7 ORF mammalian expression plasmid, C-GFPSpark tag||HG10733-ACG|
|Human PRSS7 ORF mammalian expression plasmid, C-OFPSpark / RFP tag||HG10733-ACR|
|Human PRSS7 ORF mammalian expression plasmid, C-Flag tag||HG10733-CF|
|Human PRSS7 ORF mammalian expression plasmid, C-His tag||HG10733-CH|
|Human PRSS7 ORF mammalian expression plasmid, C-Myc tag||HG10733-CM|
|Human PRSS7 ORF mammalian expression plasmid, C-HA tag||HG10733-CY|
|Human PRSS7 Gene cDNA clone plasmid||HG10733-M|
|Human PRSS7 ORF mammalian expression plasmid, N-Flag tag||HG10733-NF|
|Human PRSS7 ORF mammalian expression plasmid, N-His tag||HG10733-NH|
|Human PRSS7 ORF mammalian expression plasmid, N-Myc tag||HG10733-NM|
|Human PRSS7 ORF mammalian expression plasmid, N-HA tag||HG10733-NY|
|Human PRSS7 natural ORF mammalian expression plasmid||HG10733-UT|
|Learn more about expression Vectors|
Enterokinase, or Enteropeptidase is a type II transmembrane, which is a member of the trypsin family of serine proteases, and plays a key role in mammalian metabolism. It is synthesized as a zymogen (proenteropeptidase) that requires activation by another protease, either trypsin or possibly duodenase. Active enteropeptidase then converts the pancreatic precursor, trypsinogen, to trypsin by cleavage of the specific trypsinogen activation peptide, Asp-Asp-Asp-Asp-Lys- Ile that is highly conserved in vertebrates. The mature trypsin in turn activates other proenzymes including chymotrypsinogen, procarboxypeptidases, and proelastases. Enterokinase consists of two subunits linked by a disulfide bond. The heavy chain achors enterokinase in the intestinal brush border membrane and the light chain is the catalytic subunit, which has the same mechanism of action as trypsin and chymotrypsin. Enterokinase is the physiological activator of trypsinogen and has a specificity for the sequence (Asp)4-Lys-Ile. Because of its high specificity towards the amino acid sequence (Asp)(4)-Lys, enterokinase is a potential tool for the cleavage of fusion proteins, which are gaining more importance in biopharmaceutical production. In addition, Enterokinase is a tool protease widely utilized in the cleavage of recombinant fusion proteins.