The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
17.7 U/mg (One unit is equivalent to the Factor IX activity in one milliliter of normal human plasma.) Activity is measured using a Factor IX clotting assay.
% SDS-PAGE. ab95131 is prepared from fresh frozen plasma by a combination of conventional procedures and immunoaffinity chromatography.
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Shipped at 4°C. Store at -20°C. Stable for 12 months at -20°C.
Constituents: 50% Glycerol
This product is an active protein and may elicit a biological response in vivo, handle with caution.
Coagulant factor IX
Coagulation factor 9
Coagulation factor IX
Coagulation factor IXa heavy chain
Factor IX Deficiency
Plasma Thromboplastic Component
Plasma thromboplastin component
Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca(2+) ions, phospholipids, and factor VIIIa.
Synthesized primarily in the liver and secreted in plasma.
Defects in F9 are the cause of recessive X-linked hemophilia B (HEMB) [MIM:306900]; also known as Christmas disease. Note=Mutations in position 43 (Oxford-3, San Dimas) and 46 (Cambridge) prevents cleavage of the propeptide, mutation in position 93 (Alabama) probably fails to bind to cell membranes, mutation in position 191 (Chapel-Hill) or in position 226 (Nagoya OR Hilo) prevent cleavage of the activation peptide. Defects in F9 are the cause of thrombophilia due to factor IX defect (THR-FIX) [MIM:300807]. A hemostatic disorder characterized by a tendency to thrombosis.
Belongs to the peptidase S1 family. Contains 2 EGF-like domains. Contains 1 Gla (gamma-carboxy-glutamate) domain. Contains 1 peptidase S1 domain.
Calcium binds to the gamma-carboxyglutamic acid (Gla) residues and, with stronger affinity, to another site, beyond the Gla domain.
Activated by factor XIa, which excises the activation peptide. The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.