Abcam, ab242006, Anti-Hsp47 antibody [1C4-1A6]

Size: 100µg
Mouse Monoclonal Hsp47 antibody. Suitable for WB, ICC/IF and reacts with Human samples. Cited in 1 publication. Immunogen corresponding to Recombinant Full Length Protein corresponding to Human SERPINH1.
Key facts
Host species:Mouse,
Clonality:Monoclonal,
Clone number:1C4-1A6,
Isotype:IgG1,
Light chain type:kappa,
Carrier free:No,
Reacts with:Human,
Applications:WB, ICC/IFSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Immunogen:Recombinant Full Length Protein corresponding to Human SERPINH1.P50454

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Protein G, Purification notes-Purified from TCS., Storage buffer-Preservative: 0.09% Sodium azideConstituents: PBS, 50% Glycerol (glycerin, glycerine), Shipped at conditions-Blue Ice, Appropriate short-term storage duration-1-2 weeks, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions--20°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

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.