Anti-Hsp47 antibody

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Hsp47 also known as the heat shock protein 47 is a molecular chaperone with a molecular weight of approximately 47 kDa. It mainly resides in the endoplasmic reticulum and participates in collagen synthesis. Hsp47 binds specifically to unfolded procollagen chains ensures their proper folding and prevents premature aggregation. Due to its specialized function Hsp47 is highly expressed in collagen-producing cells like fibroblasts. Researchers commonly study this protein using techniques like Hsp47 ELISA to measure its expression or activity levels.

Biological function summary

Hsp47 ensures the quality control of collagen within the secretory pathway. It does not form part of any large protein complexes but operates closely with collagen molecules. By stabilizing procollagen's triple-helix structure Hsp47 plays an important role in collagen biosynthesis. Dysfunctional collagen processes can arise without this protein's presence potentially leading to cellular stress or structural weaknesses within tissues rich in collagen.

Pathways

Hsp47's activity integrates into the collagen synthesis and secretion pathways. This protein is related to other molecular chaperones such as Hsp70 that assist in maintaining protein homeostasis within the cell. Hsp47’s function links to fibrosis pathways because of its role in collagen maturation. In terms of fibrotic pathologies this involvement makes the chaperoning of procollagen a critical control point.

Disrupted Hsp47 function frequently associates with fibrotic conditions and osteogenesis imperfecta. Fibrosis results from excessive collagen deposition in which Hsp47 is deeply implicated. Additionally certain cancer types have shown altered Hsp47 expression correlating with increased cancer cell invasiveness due to extracellular matrix remodeling. Studies have noted interactions between Hsp47 and TGF-beta signaling in fibrotic tissues reinforcing its role in pathological collagen turnover.