Protein Disulfide Isomerase A5is an enzyme in the endoplasmic reticulum in eukaryotes or periplasmic space of prokaryotes that catalyzes the formation and breakage of disulfide bonds between cysteine residues within proteins as they fold. This allows proteins to quickly find the correct arrangement of disulfide bonds in their fully-folded state, and therefore the enzyme acts to catalyze protein folding.In the chloroplasts of the unicellular algae Chlamydomonas reinhardtii the PDI RB60 serves as a redox sensor component of an mRNA binding protein complex implicated in the photo-regulation of the translation of psbA, the RNA encoding for the photoisystem II core protein D1. PDI has also been suggested to play a role in the formation of regulatory disulfide bonds in chloroplasts
Human Protein disulfide-isomerase A5 (PDIA5) ELISA Kit employs a two-site sandwich ELISA to quantitate PDIA5 in samples. An antibody specific for PDIA5 has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and anyPDIA5 present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for PDIA5 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 PDIA5 bound in the initial step. The color development is stopped and the intensity of the color is measured.
Human Protein disulfide-isomerase A5 (PDIA5) 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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