| Product Name | Human Glia-derived nexin (SERPINE2) ELISA Kit |
|---|---|
| Description | Protease nexin I is a 44-kD thrombin and urokinase inhibitor released by human foreskin fibroblasts. PN-I shares several features with antithrombin III , an abundant plasma thrombin inhibitor. Both PN-I and AT-III have high affinities for heparin, and heparin accelerates their rate of thrombin inhibition. In addition, the published sequence of 28 amino acids at the N-terminus of PN-I is identical to the N-terminal amino acid sequence of a glial-derived neurite promoting factor. Two forms, designated alpha and beta, were identified. These differed only by the insertion of 3 nucleotides into the coding sequence, and apparently arose by utilization of an alternative splice acceptor site in the PN1 gene. In the resulting proteins, alpha-PN-I contains an arginine residue at position 310, whereas beta-PN-I contains threonine-lysine residues. This assay has high sensitivity and excellent specificity for detection of Human SERPINE2. No significant cross-reactivity or interference between Human SERPINE2 and analogues was observed. |
| Synonyms | GDN, PI7, PN1, PNI, OTTHUMP00000203766|glial-derived neurite promoting factor|glial-derived nexin 1|plasminogen activator inhibitor type 1, member 2|protease inhibitor 7 (protease nexin I)|serine (o |
| Method | Sandwich ELISA |
| Detection Range | 0.156-10 ng/mL |
| Sensitivity | 0.062 ng/mL |
| Reactivity | Human |
| Sample Types | Serum, Plasma, Other biological fluids. |
| Background | Protease nexin I is a 44-kD thrombin and urokinase inhibitor released by human foreskin fibroblasts. PN-I shares several features with antithrombin III , an abundant plasma thrombin inhibitor. Both PN-I and AT-III have high affinities for heparin, and heparin accelerates their rate of thrombin inhibition. In addition, the published sequence of 28 amino acids at the N-terminus of PN-I is identical to the N-terminal amino acid sequence of a glial-derived neurite promoting factor. Two forms, designated alpha and beta, were identified. These differed only by the insertion of 3 nucleotides into the coding sequence, and apparently arose by utilization of an alternative splice acceptor site in the PN1 gene. In the resulting proteins, alpha-PN-I contains an arginine residue at position 310, whereas beta-PN-I contains threonine-lysine residues. |
| Supplier | Abebio |
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