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H8035

Sigma-Aldrich

Heat Shock Protein 47 from rat

≥90% (SDS-PAGE), recombinant, expressed in E. coli, aqueous glycerol solution

Synonym(s):

HSP 47

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.32

biological source

rat

Quality Level

recombinant

expressed in E. coli

assay

≥90% (SDS-PAGE)

form

aqueous glycerol solution

concentration

≥0.6 mg protein/mL

UniProt accession no.

shipped in

dry ice

storage temp.

−70°C

Gene Information

General description

Hsp47 (heat shock protein 47), which is also to referred as serpinh-1 (serpin peptidase inhibitor, clade H (heat shock protein 47), member 1), is a collagen-binding glycoprotein. It is present in the endoplasmic reticulum and is induced in the presence of cytosolic stress. Hsp47 is from the serine protease inhibitor (serpin) superfamily.

Biochem/physiol Actions

Upregulation of Hsp47 (heat shock protein 47) protects cells from high temperatures, heavy metals and oxidative stress. It might also promote wound healing by controlling collagen generation and release. Hsp47 is involved in the folding and stabilization of triple-helical procollagen. Human HSP47 is associated with the pathogenesis of chronic renal fibrosis. In rats, it also participates in the progression of peritoneal fibrosis.

Physical form

Solution in 30 mM Tris (pH 8.0), 100 mM NaCl, 1 mM DTT and 0.4 M arginine

Storage Class

10 - Combustible liquids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


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A Abdelnasir et al.
Genetics and molecular research : GMR, 13(4), 10787-10802 (2014-12-20)
The aim of the present study was to identify the correlation between expression of heat shock protein 47 (Hsp47) and stress injury in heat-stressed myocardial cells and to compare variations in Hsp47 expression in rat myocardial cells exposed to different
T Koide et al.
The Journal of biological chemistry, 274(49), 34523-34526 (1999-11-27)
Prior to secretion, procollagen molecules are correctly folded to triple helices in the endoplasmic reticulum (ER). HSP47 specifically associates with procollagen in the ER during its folding and/or modification processes and is thought to function as a collagen-specific molecular chaperone
M S Razzaque et al.
Histology and histopathology, 14(4), 1199-1212 (1999-10-03)
Colligin or heat shock protein 47 (HSP47) is a stress protein that resides in the endoplasmic reticulum and is thought to participate in intracellular processing, folding, assembly and secretion of procollagens. Irrespective of the tissue site and organ, induction of
Hong-bo Xiao et al.
American journal of physiology. Renal physiology, 303(5), F757-F765 (2012-06-22)
Heat shock protein (HSP)47 is a collagen-specific molecular chaperone that is essential for the biosynthesis of collagen molecules. It is likely that increased levels of HSP47 contribute to the assembly of procollagen and thereby cause an excessive accumulation of collagens
Tomoya Nishino et al.
Kidney international, 64(3), 887-896 (2003-08-13)
Peritoneal fibrosis is a serious complication in patients on continuous ambulatory peritoneal dialysis (CAPD), but the molecular mechanism of this process remains unclear. Heat shock protein 47 (HSP47), a collagen-specific molecular chaperone, is essential for biosynthesis and secretion of collagen

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