Human SerpinI2 (His Tag) recombinant protein

Human SerpinI2 (His Tag) recombinant protein

• DataSheet
• Material Safety Data Sheets (MSDS)

Serpins are the largest and most diverse family of serine protease inhibitors which are involved in a number of fundamental biological processes such as blood coagulation, complement activation, fibrinolysis, angiogenesis, inflammation and tumor suppression and are expressed in a cell-specific manner. 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 been identified. Serpin-I2, also known as myoepithelium-derived serine protease inhibitor, Pancreas-specific protein TSA2004, Peptidase inhibitor 14, PI14, SERPINI2 and MEPI, is a secreted protein which belongs to the serpin family. It is expressed in pancreas and adipose tissues. SERPINI2 deficiency directly results in the acinar cell apoptosis and malabsorption.

cDNA FLJ56490, highly similar to Serpin I2

MEPI; SERPINI2; 1810006A24RIK; PI14; PANCPIN; SPI14; TSA2004

O75830

Human Cells

A DNA sequence encoding the human SERPINI2 (NP_006208.1) (Met 1-Leu 405) was expressed, with a polyhistidine tag at the C-terminus.

Human

The recombinant human SERPINI2 consists of 398 amino acids and predictes a molecular mass of 45.5 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rhSERPINI2 is approximately 45-55 kDa due to glycosylation.

> 90 % as determined by SDS-PAGE