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The Human Cystatin C (CST3) ELISA quantitates Hu Cystatin C in human serum, plasma, or cell culture medium. The assay will exclusively recognize both natural and recombinant Hu Cystatin C. Principle of the method The Human Cystatin C solid-phase sandwich ELISA (enzyme-linked immunosorbent assay) is designed to measure the amount of the target bound between a matched antibody pair. A target-specific antibody has been pre-coated in the wells of the supplied microplate. Samples, standards, or controls are then added into these wells and bind to the immobilized (capture) antibody. The sandwich is formed by the addition of the second (detector) antibody, a substrate solution is added that reacts with the enzyme-antibody-target complex to produce measurable signal. The intensity of this signal is directly proportional to the concentration of target present in the original specimen. Rigorous validation Each manufactured lot of this ELISA kit is quality tested for criteria such as sensitivity, specificity, precision, and lot-to-lot consistency. See manual for more information on validation.Cystatin C is a cysteine (thiol) protease inhibitor that belongs to the type II cystatin gene superfamily and is the most abundant extracellular inhibitor of cysteine proteases. Cystatin C is a constitutively secreted, amyloidogenic protein, which forms a two-fold symmetric dimer and modulates both cysteine protease activity and the expression of class II MHC molecules. Expression of cystatin C is an indicator of kidney function and glomerular filtration rate. Mutations in the cystatin C gene can lead to protein aggregates, which are implicated in hereditary amyloid angiopathy (HCCAA) and cerebral hemorrhage. Although both wild-type and mutant cystatin C are capable of forming concentration dependent inactive dimers, mutant cystatin C dimerizes at lower concentrations and is more susceptible to serine proteases, which may facilitate aggregation. In neuronal cells, oxidative stress stimulates expression of cystatin C, which may positively regulate apoptosis.
