Heat shock protein 47 is a member of the serpin superfamily of serine proteinase inhibitors. Its expression is induced by heat shock. The protein 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. Colligins are characterized by an amino acid structure that includes an N-terminal hydrophobic signal sequence and 2 putative N-linked oligosaccharide attachment sites (Clarke et al., 1991). Colligins also have a C-terminal RDEL sequence that acts as an endoplasmic reticulum (ER) retention sequence. Other features permit the colligin-binding protein of ER to be classified as a serpin (serine-arginine protease inhibitor).

Human Serpin H1 (SERPINH1) ELISA Kit employs a two-site sandwich ELISA to quantitate SERPINH1 in samples. An antibody specific for SERPINH1 has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and anySERPINH1 present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for SERPINH1 is added to the wells. After washing, Streptavidin conjugated Horseradish Peroxidase (HRP) is added to the wells. Following a wash to remove any unbound avidin-enzyme reagent, a substrate solution is added to the wells and color develops in proportion to the amount of SERPINH1 bound in the initial step. The color development is stopped and the intensity of the color is measured.

Human Serpin H1 (SERPINH1) ELISA Kit listed herein is for research use only and is not intended for use in human or clinical diagnosis. Suggested applications of our products are not recommendations to use our products in violation of any patent or as a license. We cannot be responsible for patent infringements or other violations that may occur with the use of this product.

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