Antitrypsin Activated Protein C (APC-AAT complexes, alpha1 Proteinase Inhibitor, alpha1 PI, native and denatured)

Protein C is a vitamin K-dependent serine protease produced in the liver and made up of 2 polypeptide chains. The 62kD proenzyme is activated by thrombin and the active enzyme cleaves factor Va and VIIIa and thus inhibits blood coagulation. The molecular weight of the active enzyme is 55kD and the normal concentrations in human plasma is approximately 1-3ng/ml because of the very fast turnover, the proenzyme concentration is approximately 3ug/ml. The activated protein C (APC) is inhibited by members of the serine protease inhibitor (serpin) family, of which a1-antitrypsin (AAT) and protein C inhibitor (PCI) are the most important.\n\nApplications: \nSuitable for use in ELISA. Other applications not tested.\n\nRecommended Dilution:\nELISA: 1:500\nOptimal dilutions to be determined by the researcher.\n\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. For long-term storage and to avoid repeated freezing and thawing, aliquot and add glycerol (40-50%). Freeze at -20 degrees C. Aliquots are stable for at least 12 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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SPECIFICATIONS

Catalog Number

A2298-38C

Size

100ul

Applications

ELISA

Hosts

Mouse

Reactivities

Hum

Form

Supplied as a liquid in PBS, pH 7.2, 15mM sodium azide.\n

P Type

Mab

Purity

Purified by Protein A/G affinity chromatography from culture supernatant.

Isotype

IgG1,k

References

1. Dahlback B, Villoutreix BO. Molecular recognition in the protein C anticoagulant pathway. J Thromb Haemost 2003; 1:1525-1534. 2. Strandberg K, Astermark J, Bjorgell O, Becker C, Nilsson PE, Stenflo J. Complexes between activated protein C and protein C inhibitor measured with a new method: comparison of performance with other markers of hypercoagulability in the diagnosis of deep vein thrombosis. Thromb Haemost 2001; 86:1400-1408.

Additional Info

Has specificity for a conformation-dependent neoepitope that is expressed in activated protein C upon complex-formation with a1-antitrypsin. No reaction is seen to non-complexed a1-antitrypsin and only very little cross reaction to protein C zymogen. Note that specificity is calcium dependent.\nReactivity:\nReacts strongly with APC-AAT complexes in ELISA. It can be used in sandwich ELISA in combination with a polyclonal anti-protein C antiserum. Note that the conformational neoepitope expressed in the APC-AAT complex can also be expressed in APC coated directly onto a high-binding microtiter plate.