The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Application notesRIA: Use at a concentration of 5 µg/ml.
EIA: Use at a concentration of 5 µg/ml.
WB: Use at an assay dependent dilution. Predicted molecular weight: 52 kDa.
Not yet tested in other applications.
Optimal dilutions/concentrations should be determined by the end user.
FunctionFactor 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.
Tissue specificitySynthesized primarily in the liver and secreted in plasma.
Involvement in diseaseDefects 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.
DomainCalcium binds to the gamma-carboxyglutamic acid (Gla) residues and, with stronger affinity, to another site, beyond the Gla domain.
Post-translational modificationsActivated 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.