Factor X F10 Antibodies
Affinity Biologicals, Inc. manufactures a broad range of Factor X F10 Antibodies which can be found in the listing below. Further information about each individual Factor X antibody is available by following the associated links. Our Factor X F10 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 X F10 Antibodies are manufactured for use in research applications.
|Factor X, Human||Host||Catalogue No.||Size|
|Purified IgG||Goat||GAFX-IG||10mg vial|
|Affinity Purified, IgG||Goat||GAFX-AP||0.5mg vial|
|Peroxidase Conjugated IgG||Goat||GAFX-HRP||0.2mg vial|
|Affinity Purified IgG||Sheep||SAFX-AP||0.5mg vial|
|Affinity Purified, FITC Conjugated IgG||Sheep||SAFX-APFTC||0.1mg vial|
|Affinity Purified, Biotinylated IgG||Sheep||SAFX-APBIO||0.1mg vial|
|Peroxidase Conjugated IgG||Rabbit||RAFX-HRP||0.2mg vial|
|Matched Pair Antibodies for EIA||FX-EIA||5 plates|
|Factor X, Murine||Catalogue No.||Size|
|Matched Pair Antibodies for EIA||MFX-EIA||4 plates|
Listing of Factor X F10 Antibodies
GAFX-IG – Goat anti human Factor X, purified IgG (10mg vial)
SAFX-APFTC – Sheep anti human Factor X, affinity purified, FITC conjugated IgG (0.1 mg vial)
GAFX-HRP – Goat anti human Factor X, peroxidase conjugated IgG (0.2 mg vial)
SAFX-APBIO – Sheep anti human Factor X, affinity purified, Biotinylated IgG (0.1 mg vial)
RAFX-HRP – Rabbit anti human Factor X, peroxidase conjugated IgG (0.2 mg vial)
GAFX-AP – Goat anti human Factor X, affinity purified IgG (0.5 mg vial)
SAFX-AP – Sheep anti human Factor X, affinity purified IgG (0.5 mg vial)
FX-EIA – Factor X Paired Antibody Set – 5 plate set
MFX-EIA – Murine Factor X Antibody Set – 4 plate set
FX-AG – Complete Factor X Antigen ELISA Kit – 1 plate/kit
Description of Factor X F10
Factor X (FX, Stuart Factor) is a vitamin K-dependent glycoprotein produced in the liver. The concentration of FX in plasma is ~10 μg/ml (~170 nM). Factor X is expressed as a two-chain molecule with a molecular weight of 59 kDa. The light chain (17 kDa) of FX contains a calcium-binding domain consisting of one hydroxy-aspartic acid and 11 γ-carboxyglutamic acid (gla) residues. These residues allow F.X to bind to membranes that contain acidic phospholipids in a calcium dependent manner. This is followed by two EGF-like domains. The heavy chain of FX (42 kDa) consists of the catalytic domain, carbohydrate and the activation peptide. Activation of FX to the active enzyme (FXa) results from cleavage at residue Arg52 in the heavy chain of F.X by a complex of F.IXa, cofactor VIIIa, calcium and negatively charged phospholipid surface (the tenase complex), or by the F.VIIa-tissue factor complex. Both activation pathways result in the release of the activation peptide from the N-terminal of the heavy chain. The FXa generated is a serine protease responsible for the activation of prothrombin to thrombin in the presence of a phospholipid membrane, calcium and cofactor Va. The activity of FXa in plasma is inhibited by antithrombin (ATIII), α1antitrypsin, α2macroglobulin and tissue factor pathway inhibitor (TFPI). The inhibitory activity of ATIII is stimulated approximately 1000-fold by heparin1-3.
References and Reviews
- Ichinose A, Davie EW; The Blood Coagulation Factors: Their cDNAs, Genes, and Expression; in Hemostasis and Thrombosis, 3rd Edition, eds. RW Colman, J Hirsh, VJ Marder and EW Salzman, pp 19-54, J.B. Lippincott Co., Philadelphia PA, USA, 1994.
- Steinberg M, Nemerson Y; The Activation of Factor X; in Hemostasis and Thrombosis, eds. RW Colman, J Hirsh, VJ Marder and EW Salzman, pp 91-99, J.B. Lippincott Co., Philadelphia PA, USA, 1982.
- Ellis V, Scully M, MacGregor I, Kakkar V; Inhibition of Human Factor Xa by Various Plasma Protease Inhibitors; Biochimica et Biophysica Acta 701, pp 24-31, 1982.