|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 SERPINA10 ORF mammalian expression plasmid, C-GFPSpark tag||HG10992-ACG|
|Human SERPINA10 ORF mammalian expression plasmid, C-OFPSpark / RFP tag||HG10992-ACR|
|Human SERPINA10 ORF mammalian expression plasmid, C-Flag tag||HG10992-CF|
|Human SERPINA10 ORF mammalian expression plasmid, C-His tag||HG10992-CH|
|Human SERPINA10 ORF mammalian expression plasmid, C-Myc tag||HG10992-CM|
|Human SERPINA10 ORF mammalian expression plasmid, C-HA tag||HG10992-CY|
|Human SERPINA10 natural ORF mammalian expression plasmid||HG10992-M-N|
|Human SERPINA10 ORF mammalian expression plasmid, N-Flag tag||HG10992-NF|
|Human SERPINA10 ORF mammalian expression plasmid, N-His tag||HG10992-NH|
|Human SERPINA10 ORF mammalian expression plasmid, N-Myc tag||HG10992-NM|
|Human SERPINA10 ORF mammalian expression plasmid, N-HA tag||HG10992-NY|
|Human SERPINA10 natural ORF mammalian expression plasmid||HG10992-UT|
|Learn more about expression Vectors|
Mouse protein Z-dependent protease inhibitor, also known as PZ-dependent protease inhibitor, SERPINA10 and ZPI, is a secreted protein which belongs to the serpin family. It is expressed by the liver and secreted in plasma. SERPINA10 / Serpin-A10 inhibits factor Xa activity in the presence of protein Z, calcium and phospholipid. Serpins are a group of proteins with similar structures that were first identified as a set of proteins able to inhibit proteases. The acronym serpin was originally coined because many serpins inhibit chymotrypsin-like serine proteases (serine protease inhibitors).Over 1000 serpins have now been identified, these include 36 human proteins, as well as molecules in plants, fungi, bacteria, archaea and certain viruses. Serpins are the largest and most diverse family of protease inhibitors. Most serpins control proteolytic cascades, certain serpins do not inhibit enzymes, but instead perform diverse functions such as storage (ovalbumin, in egg white), hormone carriage proteins (thyroxine-binding globulin, cortisol-binding globulin) and tumor suppressor genes (maspin). Most inhibitory serpins target chymotrypsin-like serine proteases. These enzymes are defined by the presence of a nucleophilic serine residue in their catalytic site. Some serpins inhibit other classes of protease. A number of such serpins have been shown to target cysteine proteases. These enzymes differ from serine proteases in that they are defined by the presence of a nucleophilic cysteine residue, rather than a serine residue, in their catalytic site.