Factor IX F9 Antibodies

Affinity Biologicals, Inc. manufactures a broad range of Factor IX F9 Antibodies which can be found in the listing below.   Further information about each individual Factor IX antibody is available by following the associated links.  Our Factor IX F9 Antibodies are excellent for use in immunoassays where high sensitivity is required and are frequently the preferred reagent for immunopreciptaion techniques and activity neutralization assays.  These antibodies have proven to be extremely useful in the preparation of immune-adsorbent resins for use in immuno-depletion of specific proteins from plasma as well as immuno-affinity purification of proteins.  Affinity’s Factor IX F9 Antibodies are manufactured for use in research applications.

Factor IX, HumanHostCatalogue No.Size
Purified IgGGoatGAFIX-IG10mg vial
Affinity Purified IgGGoatGAFIX-AP0.5mg vial
Peroxidase Conjugated, IgGGoatGAFIX-HRP0.2mg vial
Affinity Purified, HRP Conjugated IgGGoatGAFIX-APHRP0.1mg vial
Affinity Purified, FITC Conjugated IgGGoatGAFIX-APFTC0.1mg vial
Affinity Purified, Biotinylated IgGGoatGAFIX-APBIO0.1mg vial
Purified IgGSheepSAFIX-IG10mg vial
Affinity Purified IgGSheepSAFIX-AP0.5mg vial
Affinity Purified, HRP Conjugated IgGSheepSAFIX-APHRP0.1mg vial
Matched Pair Antibodies for EIAFIX-EIA5 plates
Complete ELISA KitFIX-AG1 plate

Factor IX, Canine Catalogue No.Size
Matched Pair Antibodies for EIACFIX-EIA4 plates

Listing of Factor IX F9 Antibodies

Description of Factor IX F9

Factor IX (FIX, Christmas Factor) is a vitamin K-dependent glycoprotein produced in the liver. Plasma concentration of FIX is normally around 5 μg/ml (87 nM) in plasma. The biological importance of FIX is demonstrated in Haemophilia B (Christmas disease), an X-linked congenital bleeding disease resulting from a quantitative (low activity and low antigen) or qualitative (low activity, normal antigen) defect in FIX function.

In its proenzyme or zymogen form FIX is a single chain molecule of 55,000 daltons. It contains two EGF-like domains and an amino-terminal domain containing 12 γ-carboxy-glutamic acid (Gla) residues. These Gla residues allow FIX to bind divalent metal ions and participate in calcium-dependent binding interactions. The activation of F.IX occurs by limited proteolysis in the presence of calcium by activated factor XI (FXIa) and/or by a complex of VIIa/tissue factor/phospholipid and activated Factor X between residues Arg146-Ala147 and between Arg180-Val181. The terminal activated product in either case is FIXaβ, a two-chain enzyme consisting of a heavy chain (28,000 daltons), a light chain (18,000 daltons) and an activation peptide product of 11,000 daltons. FIX can also be cleaved into inactive products by thrombin and by elastase.

The activity of FIXaβ in plasma is inhibited by antithrombin and this inhibition is accelerated 1000-fold in the presence of optimal concentrations of heparin 1-3.

References and Reviews

  1. Lawson, JH, Mann KG; Cooperative Activation of Human F.IX by the Human Extrinsic Pathway of Coagulation; JBC 266 pp11317-11327, 10991.
  2. Enfield DL, Thompson AR; Cleavage and Activation of Factor IX by Serine Proteases; Blood 64, pp 821-831, 1984.
  3. Limentani SA, Furie BC, Furie B, in Hemostasis and Thrombosis, 3rd Edition, eds. RW Colman, J Hirsh, VJ Marder and EW Salzman, pp. 94-108, J.B. Lippincott Co., Philadelphia PA, USA, 1994