Natural and recombinant human Total Serpin E1 (active, latent, uPA, tPA, and Vitronectin complexed Serpin E1).
< 0.5% cross-reactivity observed with available related molecules.< 50% cross-species reactivity observed with species tested.
No significant interference observed with available related molecules.
The Quantikine Human Total Serpin E1/PAI-1 Immunoassay is a 4.5 hour solid-phase ELISA designed to measure human Serpin E1 in cell culture supernates, serum, and plasma. It contains Sf 21-expressed recombinant human Serpin E1 and has been shown to accurately quantitate the recombinant factor free and in complex with uPA, tPA, or vitronectin. Results obtained using natural human Serpin E1 showed linear curves that were parallel to the standard curves obtained using the Quantikine kit standards. These results indicate that this kit can be used to determine relative mass values for naturally occurring human Serpin E1.
Intra-Assay Precision (Precision within an assay) Three samples of known concentration were tested twenty times on one plate to assess intra-assay precision.
Inter-Assay Precision (Precision between assays) Three samples of known concentration were tested in twenty separate assays to assess inter-assay precision. Assays were performed by at least three technicians using two lots of components.
The recovery of human Total Serpin E1 spiked to levels throughout the range of the assay in various matrices was evaluated.
Average % Recovery
Cell Culture Media (n=4)
Citrate Plasma (n=4)
EDTA Plasma (n=4)
Heparin Plasma (n=4)
To assess the linearity of the assay, samples containing high concentrations of human Serpin E1 were serially diluted with Calibrator Diluent to produce samples with values within the dynamic range of the assay. All samples were diluted prior to assay.
Preparation and Storage
Store the unopened product at 2 - 8 °C. Do not use past expiration date.
Background: Serpin E1/PAI-1
The human serpin superfamily consists of at least 35 members that target not only serine proteases, but also selected cysteine proteases and non-protease proteins. Serpins bind the protease active site resulting in a major conformational rearrangement that traps the enzyme in a covalent acyl-enzyme intermediate. As protease inhibitors, serpins have an array of functions including regulating blood clotting, the complement pathway, extracellular matrix remodeling, and cell motility. They are also involved in activities that extend beyond their ability to inhibit proteases. For instance, they may also regulate blood pressure, angiogenesis, or act as storage/transport proteins.
Plasminogen Activator Inhibitor
Entrez Gene IDs
5054 (Human); 18787 (Mouse);
Endothelial plasminogen activator inhibitor; Nexin; PAI1; PAI-1; PAI1PAI-1; PAISerpin E1; PLANH1; PLANH1plasminogen activator inhibitor 1; serine (or cysteine) proteinase inhibitor, clade E (nexin, plasminogenactivator inhibitor type 1), member 1; serpin peptidase inhibitor, clade E (nexin, plasminogen activator inhibitortype 1), member 1;