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 Coagulation Factor IX

DOMAIN STRUCTURE OF FACTOR IX The domain structure of factor IX is represented, where: GLA=region containing γ-carboxyglutamic acid residues, EGF=region containing sequences homologous to human epidermal growth factor, AP=activation peptide released upon conversion of the zymogen to the active serine protease, and CATALYTIC DOMAIN=region containing the serine protease catalytic triad. Arrows indicate the sites which are proteolytically cleaved by factor XIa during activation of the zymogen, with arrow A being cleaved first.

PURCHASING AND PRODUCT INFORMATION

Catalog Number HCIX-0040 BCIX-1040 MCIX-5040*	Description Human Factor IX Bovine Factor IX Mouse Factor IX	Size 100 µg 100 µg 50 µg	Formulation 50% (vol/vol) glycerol/H2O same same
Storage -20oC	Purity >95% by SDS-PAGE	Activity Determination Clotting assay	Shelf Life (properly stored) 12 months
	Sample Gel Information: Gel: Novex 4-12% Bis-Tris Load: Human Factor IX, 1 µg per lane Buffer: MOPS Standard: SeeBluePlus 2; Myosin (191 kDa), Phosphorylase B (97 kDa), BSA (64 kDa), Glutamic Dehydrogenase (51 kDa), Alcohol Dehydrogenase (39 kDa), Carbonic Anhydrase (28 kDa), Myoglobin Red (19 kDa), Lysozyme (14 kDa)
U.S. Pricing	Product inquiry	SAMPLE DATA SHEET	ORDER NOW!

*Due to mouse plasma quality issues our mouse proteins are not being sold until further notice.  At the present time we cannot give a completion date.  Thank you.

Overview of Factor IX

The zymogen factor IX is a single chain vitamin K-dependent glycoprotein which is synthesized in the liver (1-3). The domain structure of factor IX is similar to that of the other vitamin K dependent coagulation factors. The NH₂-terminal region contains 12 γ-carboxyglutamic acid (gla) residues which facilitate the calcium dependent binding of factor IX to negatively charged phospholipid surfaces. Two domains which are homologous to epidermal growth factor (EGF) span the region between the NH₂-terminal gla domain and the activation peptide (Ala-146 to Arg-180). 
Factor IX is activated by either factor XIa or the factor VIIa/tissue factor/phospholipid complex. Cleavage at site A (see figure) yields the intermediate IXa which is subsequently converted to the fully active form IXaβ by cleavage at site B. The NH2-terminal light chain (GLA and EGF domains) remains covalently attached to the COOH-terminal heavy chain by a disulfide bond. The serine protease catalytic triad (Ser-365, His 221, Asp-269) is located in the heavy chain. Factor IXaβ is the catalytic component of the "intrinsic factor Xase complex" (factor VIIIa/IXa/Ca²⁺/phospholipid) which proteolytically activates factor X to factor Xa.

Human factor IX is prepared from fresh frozen plasma by a combination of conventional procedures (4) and immunoaffinity chromatography (5). Bovine factor IX is prepared from fresh citrated bovine plasma by a modification of the method described by Fujikawa et al. (6). The purified proteins are supplied in 50% (vol/vol) glycerol/H₂O and should be stored at -20^oC. Purity is determined by SDS-PAGE analysis and activity is measured using a factor IX clotting assay. 

Properties of Factor IX

PURCHASING AND PRODUCT INFORMATION

References 
1. Thompson, A.R., Blood, 67, 565 (1986). 
2. Hedner, U., et al., In Hemostasis and Thrombosis, 2nd edition, ed. R.W. Colman, J. Hirsh, V.J. Marder, E.W. 3. Salzman, pp. 39-47. J.P. Lippincott Co, Philadelphia, 1987. 
4. Fujikawa, K., Davie, EW., Methods in Enzymology, 45, 74 (1976). 
5. Bajaj, S.P., et al., Prep. Biochem., 11, 397 (1981). 
6. Jenny, R.J., et al., Prep. Biochem., 16, 227 (1986). 
7. Fujikawa, K., et al., Biochemistry, 12, 4938 (1973). 
8. Discipio, R.G., et al., Biochemistry, 16, 698 (1977). 
9. Osterud, B., et al., J. Biol. Chem., 253, 5946 (1978). 
10.McMullen, B.A., et al., BBRC, 115, 8 (1983).