SERPINB8 Polyclonal Antibody Store at -20°C
SKU: E-AB-15386-200
SERPINB8 Polyclonal Antibody Store at -20°C
| SKU # | E-AB-15386 |
| Reactivity | Human |
| Host | Rabbit |
| Applications | IHC |
Product Details
| Isotype | IgG |
| Host | Rabbit |
| Reactivity | Human |
| Applications | IHC |
| Clonality | Polyclonal |
| Immunogen | Recombinant protein of human SERPINB8 |
| Abbre | SERPINB8 |
| Synonyms | CAP 2, CAP-2, CAP2, Cytoplasmic antiproteinase 2, OTTHUMP00000067000, OTTHUMP00000067001, PI 8, PI-8, PI8, Peptidase inhibitor 8, Protease inhibitor 8 (ovalbumin type), Serine (or cysteine) proteinase inhibitor clade B (ovalbumin) member 8, Serpin B8, Serpin peptidase |
| Swissprot | |
| Cellular Localization | Cytoplasm. |
| Concentration | 0.6 mg/mL |
| Buffer | Phosphate buffered solution, pH 7.4, containing 0.05% stabilizer and 50% glycerol. |
| Purification Method | Affinity purification |
| Research Areas | Cell Biology, Cardiovascular |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | The product is shipped with ice pack,upon receipt,store it immediately at the temperature recommended. |
Related Reagents
| Applications | Recommended Dilution |
| IHC | 1:30-1:150 |
Background
The superfamily of high molecular weight serine proteinase inhibitors (serpins) regulate a diverse set of intracellular and extracellular processes such as complement activation, fibrinolysis, coagulation, cellular differentiation, tumor suppression, apoptosis, and cell migration. Serpins are characterized by well-conserved a tertiary structure that consists of 3 beta sheets and 8 or 9 alpha helices (Huber and Carrell, 1989 [PubMed 2690952]). A critical portion of the molecule, the reactive center loop connects beta sheets A and C. Protease inhibitor-8 (PI8; SERPINB8) is a member of the ov-serpin subfamily, which, relative to the archetypal serpin PI1 (MIM 107400), is characterized by a high degree of homology to chicken ovalbumin, lack of N- and C-terminal extensions, absence of a signal peptide, and a serine rather than an asparagine residue at the penultimate position