Human Prostasin ELISA Kit is a Sandwich (quantitative) ELISA for the measurement of Human Prostasin in Human in Cell Culture Media, Biofluids samples.
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Prostasin, Channel-activating protease 1, Serine protease 8, CAP1, PRSS8
- sELISA
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Sandwich ELISA - Human Prostasin ELISA Kit (AB213817)
Human Prostasin ELISA Kit (ab213817) Standard Curve.
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The Human Prostasin Enzyme-Linked Immunosorbent Assay (ELISA) kit (ab213817) is designed for the quantitative measurement of Human Prostasin in cell culture supernatants, serum, plasma (heparin, EDTA) and urine.
The ELISA kit is based on standard sandwich enzyme-linked immunosorbent assay technology. A polyclonal antibody from sheep specific for Prostasin has been pre-coated onto 96-well plates. Standards (Expression system for standard: CHO; Immunogen sequence: A33-G319) and test samples are added to the wells, a biotinylated detection polyclonal antibody from sheep specific for Prostasin is added subsequently and then followed by washing with PBS or TBS buffer. Avidin-Biotin-Peroxidase Complex is added and unbound conjugates are washed away with PBS or TBS buffer. HRP substrate TMB is used to visualize HRP enzymatic reaction. TMB is catalyzed by HRP to produce a blue color product that changed into yellow after adding acidic stop solution. The density of yellow is proportional to the Human Prostasin amount of sample captured in plate.
Prostasin is a protein that in humans is encoded by the PRSS8 gene. It is a single-copy gene and mapped to 16p11.2. Prostasin is likely to be the more physiologically relevant protease. This gene encodes a trypsinogen, which is a member of the trypsin family of serine proteases. Co-expression of Prostasin with either Xenopus or rat ENaC in Xenopus oocytes resulted in a 60% to 80% increase in amiloride-sensitive sodium currents, and that the addition of aprotinin, a serine protease inhibitor, completely prevented this activation. This enzyme is highly expressed in prostate epithelia and is one of several proteolytic enzymes found in seminal fluid. The proprotein is cleaved to produce a light chain and a heavy chain which are associated by a disulfide bond. It is active on peptide linkages involving the carboxyl group of lysine or arginine.
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