Detect Range:0.78 ng/mL - 50 ng/mL
Sensitivity:0.39 ng/mL
Sample Type:Serum, Plasma, Other biological fluids
Sample Volume: 1-200 uL
Assay Time:1-4.5h
Detection wavelength:450 nm

Detection Method:Sandwich
Test principle:This assay employs a two-site sandwich ELISA to quantitate PDIA4 in samples. An antibody specific for PDIA4 has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and anyPDIA4 present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for PDIA4 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 PDIA4 bound in the initial step. The color development is stopped and the intensity of the color is measured.
Product Overview:Protein Disulfide Isomerase A4is 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. The reduced (dithiol) form of PDI is able to catalyse a reduction of mispaired thiol residues of a particular substrate, acting as an isomerase. Therefore, PDI is capable of catalyzing the posttranslational modification disulfide exchange. Such exchange reactions can occur intramolecularly, leading to the rearrangement of disulfide bonds in a single protein.