Insulin-like Growth Factor-Binding Protein-1 (IGFBP-1) (Mouse)
- SKU:
- BE69143
- Bulk Pricing:
-
- Buy 5 - 20 and get 5% off
- Buy 21 - 30 and get 10% off
- Buy 31 - 50 and get 15% off
- Buy 51 or more – call for best pricing
The cookie settings on this website are set to 'allow all cookies' to give you the very best experience. Please click Accept Cookies to continue to use the site.
Sandwich enzyme-linked immune-sorbent assay (ELISA) for the determination of IGFBP-1 concentrations in serum, body fluids, tissue homogenate or cell culture supernatants from mice. For research use only, not for use in diagnostic procedures.<br><br>
Insulin-like growth factor-binding protein 1 (IGFBP-1) also known as placental protein 12 (PP12) is a member of the Insulin-like growth factor-binding protein (IGFBP) family. It is synthesized in liver, secretory endometrium, and decidua. The IGFBP1 gene has 4 exons, spans 5.9 kb, and mapped to 7p13-p12. This protein has an IGFBP domain and a type-I thyroglobulin domain. It binds both insulin-like growth factors (IGFs) I and II and circulates in the plasma. Binding of this protein prolongs the half-life of the IGFs and alters their interaction with cell surface receptors. Leu and George (2007) concluded that IGFBP1 is a negative regulator of the p53/BAK-dependent pathway of apoptosis.
Sandwich enzyme-linked immune-sorbent assay (ELISA) for the determination of IGFBP-1 concentrations in serum, body fluids, tissue homogenate or cell culture supernatants from mice. For research use only, not for use in diagnostic procedures.<br><br>
Insulin-like growth factor-binding protein 1 (IGFBP-1) also known as placental protein 12 (PP12) is a member of the Insulin-like growth factor-binding protein (IGFBP) family. It is synthesized in liver, secretory endometrium, and decidua. The IGFBP1 gene has 4 exons, spans 5.9 kb, and mapped to 7p13-p12. This protein has an IGFBP domain and a type-I thyroglobulin domain. It binds both insulin-like growth factors (IGFs) I and II and circulates in the plasma. Binding of this protein prolongs the half-life of the IGFs and alters their interaction with cell surface receptors. Leu and George (2007) concluded that IGFBP1 is a negative regulator of the p53/BAK-dependent pathway of apoptosis.