Human Serpin I2 (SERPINI2) Protein
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Description
Serpin I2 (SERPINI2) protein is a recombinant Human protein expressed in HEK293 cells.
Documents del producto
Product specifications
| Category | Proteins and Peptides |
| Immunogen Target | Serpin I2 (SERPINI2) |
| Host | HEK293 cells |
| Assay Type | Activity: Not tested Sequence Fragment: Ser19-Leu405 Tag: C-terminal 6 His tag |
| Origin | Human |
| Observed MW | Calculated MW: 45.1 kDa Observed MW (SDS-PAGE): 44-60 kDa |
| Expression | Recombinant |
| Purity | > 95% (SDS-PAGE) |
| Purification | 0.2 µm filtered prior to lyophilization. |
| Size 1 | 10 µg |
| Size 2 | 50 µg |
| Form | Lyophilized |
| Tested Applications | SDS-PAGE |
| Buffer | Prior to lyophilization: 20 mM PBS,150 mM NaCl,pH 7.4, containing 5%-8% Trehalose, Mannitol and 0.01% Tween 80. |
| Availability | Shipped within 5-15 working days. |
| Storage | Storage: Store lyophilized between -20 °C and -80°C. Stability: Stable when stored reconstituted at 2-8°C for up to 1 week. Reconstituted aliquots are stable at -20°C for up to 3 months. Shelf Life: 12 months. |
| Dry Ice | No |
| UniProt ID | O75830 |
| Gene ID | 5276 |
| OMIM | 605587 |
| Alias | MEPI,PI14,PANCPIN,TSA2004,Serpin I2,Myoepithelium-derived serine protease inhibitor,Pancpin,Peptidase inhibitor 14 |
| Background | Protein SERPINI2 |
| Status | RUO |
| Note | THIS PRODUCT IS FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC, THERAPEUTIC OR COSMETIC PROCEDURES. NOT FOR HUMAN OR ANIMAL CONSUMPTION. Reconstitute in sterile H2O to prepare a stock solution of concentration 0.25 mg/ml. Do not vortex. Endotoxin Level: < 1.0 EU per µg (LAL method). |
Descripción
SERPINI2 is a member of the serine protease inhibitor (serpin) family and is encoded by the SERPINI2 gene located on chromosome 3. The serpin superfamily comprises a large group of proteins that inhibit proteolytic enzymes, playing crucial roles in various biological processes such as blood coagulation, fibrinolysis, immune response, and tissue remodeling. Like other serpins, SERPINI2 regulates the activity of proteases by acting as a suicide substrate, forming a stable complex with the target protease, which leads to its irreversible inhibition. Although SERPINI2 is not as well-studied as other members of the serpin family, recent studies suggest that it is involved in the regulation of proteolysis in various tissues, with significant expression observed in pancreatic, hepatic, and other glandular tissues.
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