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Human HSP47 Recombinant


accession:  P50454
   Size A     10ug   $ 160
   Size B      50ug  $550
   Size C      200ug  $ 1950
Domain  : 
Gene  :  SERPINH1
Catalog no. :  RKP50454



Optimized DNA sequence encoding Human heat shock protein - HSP47/SERPINH1 (ALA19 - LEU418) extracellular domain including a C-terminal His tag was expressed in HEK293 cells.

Molecular weight:

Recombinant Human heat shock protein 47 (HSP47) is a protein consisting of 407 amino acid residue subunits,due to glycosylation migrates as an approximately as 47kDa band protein on reduced SDS-PAGE.

>95%, as determined by SDS-PAGE and HPLC
Endotoxin content was assayed using a LAL gel clot method.
Endotoxin level was found to be less than 0.1 ng/µg(1EU/µg).

Recombinant Heat shock protein 47 (HSP47) is lyophilized  from 0.2 μm filtered PBS solution,  pH7.2 ,  5% Trehalose.

A quick spin of the vial followed by reconstitution in distilled water to a concentration not less than 0.1 mg/mL. This solution can then be diluted into other buffers.

Recombinant Human heat shock protein 47 (SERPINH1) can be stored in working aliquots at 2° - 8° C for one month, or at -20°C to -70°C for twelve months.

Avoid repeated freeze/thaw cycles.

This product is for research purposes only.It may not be used for therapeutics or diagnostic purposes.


heat shock protein 47

Heat shock protein 47 (HSP47) is a single-substrate molecular chaperone crucial for collagen biosynthesis. Heat shock protein 47 (HSP47) is a 47-kDa stress glycoprotein that resides in the endoplasmic reticulum of collagen-secreting cells. It functions as a collagen- specific molecular chaperone in the folding, and assemblies of procollagen molecules are well- documented. It interacts with various collagens, including types I to V and is required for the formation of correct triple- helical structure.

Related Publications:
involvement of interleukin-17a-induced expression of heat shock protein 47 in intestinal fibrosis in crohn's disease
Gut, Feb 2014; 10.1136/gutjnl-2013-305632.
the ph sensitivity of murine heat shock protein 47 (hsp47) binding to collagen is affected by mutations in the breach histidine cluster
J. Biol. Chem., Feb 2013; 288: 4452 - 4461.
heat shock protein 47: a new platelet collagen receptor
Blood (ASH Annual Meeting Abstracts), Nov 2010; 116: 158.
treatment of idiopathic myelofibrosis employing sirna for heat shock protein 47 (sirna/hsp47) encapsulated in liposomes.
Blood (ASH Annual Meeting Abstracts), Nov 2007; 110: 4646.
role of heat shock protein 47, a collagen-binding chaperone, in lacrimal gland pathology in patients with cgvhd
Invest. Ophthalmol. Vis. Sci., Mar 2007; 48: 1079 - 1086.

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