| Product Name | Human Serpin H1 (SERPINH1) ELISA Kit |
|---|---|
| Description | Heat shock protein 47 is a member of the serpin superfamily of serine proteinase inhibitors. Its expression is induced by heat shock. The protein localizes to the endoplasmic reticulum lumen and binds collagen; thus it is thought to be a molecular chaperone involved in the maturation of collagen molecules. Autoantibodies to this protein have been found in patients with rheumatoid arthritis. Colligins are characterized by an amino acid structure that includes an N-terminal hydrophobic signal sequence and 2 putative N-linked oligosaccharide attachment sites (Clarke et al., 1991). Colligins also have a C-terminal RDEL sequence that acts as an endoplasmic reticulum (ER) retention sequence. Other features permit the colligin-binding protein of ER to be classified as a serpin (serine-arginine protease inhibitor). This assay has high sensitivity and excellent specificity for detection of Human SERPINH1. No significant cross-reactivity or interference between Human SERPINH1 and analogues was observed. |
| Synonyms | AsTP3, CBP1, CBP2, HSP47, PIG14, PPROM, RA-A47, SERPINH2, gp46, arsenic-transactivated protein 3|colligin-1|colligin-2|proliferation-inducing gene 14|rheumatoid arthritis antigen A-47|serine (or cys |
| Method | Sandwich ELISA |
| Detection Range | 125.00-8000 pg/mL |
| Sensitivity | 50 pg/mL |
| Reactivity | Human |
| Sample Types | Serum, Plasma, Other biological fluids. |
| Background | Heat shock protein 47 is a member of the serpin superfamily of serine proteinase inhibitors. Its expression is induced by heat shock. The protein localizes to the endoplasmic reticulum lumen and binds collagen; thus it is thought to be a molecular chaperone involved in the maturation of collagen molecules. Autoantibodies to this protein have been found in patients with rheumatoid arthritis. Colligins are characterized by an amino acid structure that includes an N-terminal hydrophobic signal sequence and 2 putative N-linked oligosaccharide attachment sites (Clarke et al., 1991). Colligins also have a C-terminal RDEL sequence that acts as an endoplasmic reticulum (ER) retention sequence. Other features permit the colligin-binding protein of ER to be classified as a serpin (serine-arginine protease inhibitor). |
| Supplier | Abebio |
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