Serpins are the largest and most diverse family of serine protease inhibitors which are involved in some 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 1 serpins have been identified.Serpin-I2, also known as myoepithelium-derived serine protease inhibitor, Pancreas-specific protein TSA24, Peptidase inhibitor 14, PI14, SERPINI2 and MEPI, is a secreted protein that belongs to the serpin family. It is expressed in pancreas and adipose tissues. SERPINI2 deficiency directly results in the acinar cell apoptosis and malabsorption.
Pack Size | Availability | Price/USD | Quantity |
---|---|---|---|
100 μg | 5 days | $ 700.00 |
Description | Serpins are the largest and most diverse family of serine protease inhibitors which are involved in some 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 1 serpins have been identified.Serpin-I2, also known as myoepithelium-derived serine protease inhibitor, Pancreas-specific protein TSA24, Peptidase inhibitor 14, PI14, SERPINI2 and MEPI, is a secreted protein that belongs to the serpin family. It is expressed in pancreas and adipose tissues. SERPINI2 deficiency directly results in the acinar cell apoptosis and malabsorption. |
Species | Human |
Expression System | HEK293 |
Tag | His |
Accession Number | O75830 |
Synonyms | PI14, TSA2004, PANCPIN, MEPI, Serpin I2, serpin peptidase inhibitor, clade I (pancpin), member 2 |
Construction | A DNA sequence encoding the human SERPINI2 (NP_006208.1) (Met 1-Leu 405) was expressed, with a polyhistidine tag at the C-terminus. |
Protein Purity | > 90 % as determined by SDS-PAGE |
Molecular Weight | Approxiamtely 45.5 kDa |
Endotoxin | < 1.0 EU per μg of the protein as determined by the LAL method |
Formulation | Lyophilized from sterile PBS, pH 7.4. Please contact us for any concerns or special requirements. Normally 5 % - 8 % trehalose, mannitol and 0. 01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hard copy of CoA. |
Reconstitution | A hardcopy of datasheet with reconstitution instructions is sent along with the products. Please refer to it for detailed information. |
Stability & Storage |
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles. |
Shipping |
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise. |
Research Background | Serpins are the largest and most diverse family of serine protease inhibitors which are involved in some 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 1 serpins have been identified.Serpin-I2, also known as myoepithelium-derived serine protease inhibitor, Pancreas-specific protein TSA24, Peptidase inhibitor 14, PI14, SERPINI2 and MEPI, is a secreted protein that belongs to the serpin family. It is expressed in pancreas and adipose tissues. SERPINI2 deficiency directly results in the acinar cell apoptosis and malabsorption. |
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Please read the User Guide of Recombinant Proteins for more specific information.
Serpin I2 Protein, Human, Recombinant (His) PI14 TSA2004 PI 14 PI-14 TSA 2004 PANCPIN TSA-2004 MEPI Serpin I2 serpin peptidase inhibitor, clade I (pancpin), member 2 recombinant recombinant-proteins proteins protein