Update: 28 September, 2023
Hsp47 is a 47 kDa glycoprotein that is widely distributed and highly conserved. It is a collagen-specific molecular chaperone found in the endoplasmic reticulum. Like other chaperones, it assists in protein folding both in vivo and in vitro, as well as protecting proteins from unfolding due to external stress. Collagen is the most abundant fibrous protein in the body, therefore its correct biosynthesis and exocytosis is essential. Hsp47 has been recognized as a vital component of the collagen fibril formation pathway. Hsp47 is a non-inhibitory member of the serine protease inhibitor (serpin) superfamily of proteins. These biomolecules are known to undergo structural conformational changes under different conditions and various conformations of the protein have been identified, each exhibiting different substrate binding and biological activity characteristics. Native Hsp47 possesses low stability and is prone to degradation and aggregation, producing molecules of lower and higher molecular weights. Monitoring of the molecular weight of native Hsp47 therefore allows differentiation between the conformation(s) present in the sample and also reveals the oligomerization state of the protein. SEC with UV detection can be used to determine the molecular weights of proteins such as Hsp47. The native form of mouse Hsp47 was analyzed for id
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MD5 Checksum: 2A2DFD77D89EDDD9550B485E293300A2
Publication date: 11 June, 2012
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PDF Link: Agilent Analysis of Hsp47 a Collagen Chaperone by Size Exclusion Chromatography (SEC) Manual PDF