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- Email: info@nsjbio.com
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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.
The stated application concentrations are suggested starting amounts. Titration of the HSP47 antibody may be required due to differences in protocols and secondary/substrate sensitivity.
Human partial recombinant protein (AA 247-418) was used as the immunogen for this HSP47 antibody.
After reconstitution, the HSP47 antibody can be stored for up to one month at 4oC. For long-term, aliquot and store at -20oC. Avoid repeated freezing and thawing.
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