Anti-HSP47

0.5mg/ml if reconstituted with 0.2ml sterile DI water. Heat shock protein 47, also known as SERPINH1, is a serpin which serves as a human chaperone protein for collagen. It is a member of the serpin superfamily of serine proteinase inhibitors. Its expression is induced by heat shock. HSP47 localizes to the endoplasmic reticulum lumen and binds collagen, thus it is thought to be a molecular chaperone involved in the maturation of collagen molecules. Autoantibodies to this protein have been found in patients with rheumatoid arthritis. It has been found that HSP47 monitors the integrity of the triple helix of type I procollagen at the ER/cis-Golgi boundary and, when absent, the rate of transit from the ER to the Golgi is increased and the helical structure is compromised. Protein function: Binds specifically to collagen. Could be involved as a chaperone in the biosynthetic pathway of collagen. [The UniProt Consortium]