SerpinA10 cDNA ORF Clone, Human, N-HA tag General Information
Full length Clone DNA of Human serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 10 with N terminal HA tag.
Enhanced CMV promoter
HA Tag Sequence: TATCCTTACGACGTGCCTGACTACGCC
T7( 5' TAATACGACTCACTATAGGG 3' )
BGH( 5' TAGAAGGCACAGTCGAGG 3' )
The plasmid is confirmed by full-length sequencing.
Antibiotic in E.coli
Antibiotic in Mammalian cell
Stable or Transient mammalian expression
Storage & Shipping
Each tube contains lyophilized plasmid.
The lyophilized plasmid can be stored at ambient temperature for three months.
**Sino Biological guarantees 100% sequence accuracy of all synthetic DNA constructs we deliver, but we do not guarantee protein expression in your experimental system. Protein expression is influenced by many factors that may vary between experiments or laboratories.**
SerpinA10 cDNA ORF Clone, Human, N-HA tag Alternative Names
PZI cDNA ORF Clone, Human;ZPI cDNA ORF Clone, Human
SerpinA10 Background Information
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.
serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 10
Han X, et al., 1998, Proc Natl Acad Sci. USA 95: 9250-5. Han X, et al., 2000, Blood 96: 3049-55. Irving JA, et al.,2000, Genome Res. 10 (12): 1845-64. Irving J, et al.,2002, Mol Biol Evol. 19 (11): 1881-90. Rawlings ND, et al.,2004, Biochem J. 378 (Pt 3): 705-16. Water N, et al., 2004, Br J Haematol. 127:190-4. Wei Z, et al., 2009, Blood 114 (17): 3662-7. Whisstock JC, et al.,2010, J Biol Chem. 285 (32): 24307-12.