Antibodies to Factor VIII

Factor VIII:C, human

Antibody Host Catalogue No. Size Product Insert
Purified IgG Sheep SAF8C-IG 10 mg
Affinity purified IgG Sheep SAF8C-AP 0.5 mg
Peroxidase conjugated IgG Sheep SAF8C-HRP 0.2 mg
Affinity purified, FITC conjugated IgG Sheep SAF8C-APFTC 0.1 mg
Affinity purified, biotinylated IgG Sheep SAF8C-APBIO 0.1 mg
Matched Pair Antibodies for EIA F8C-EIA 4 plates
Analyte Specific Reagents
– Peroxidase conjugated IgG Sheep SAF8C-HRP-ASR 0.2 mg

Factor VIII, canine

Antibody Host Catalogue No. Size Product Insert
Purified IgG Sheep SAC8C-IG 5 mg
Peroxidase Conjugated IgG Sheep SAC8C-HRP 0.2 mg
Matched Pair Antibodies for EIA CFVIII-EIA 4 plates

Description of Factor VIII (FVIII)

Factor VIII (formerly referred to as antihemophilic globulin and Factor VIII:C) is a large glycoprotein (320 kDa) that circulates in plasma at approximately 200 ng/ml. Synthesized in the liver, the majority of Factor VIII is cleaved during expression, resulting in a heterogeneous mixture of partially cleaved forms of FVIII ranging in size from 200-280 kDa. The FVIII is stabilized by association with von Willebrand Factor to form a FVIII-vWF complex required for the normal survival of FVIII in vivo (t1/2 of 8-12 hours).

F.VIII is a pro-cofactor that is activated through limited proteolysis by thrombin. In this process F.VIIIa dissociates from vWF to combine with activated Factor IX, calcium and a phospholipid surface where it is an essential cofactor in the assembly of the Factor X activator complex. Once dissociated from vWF, FVIIIa is susceptible to inactivation by activated Protein C and by non-enzymatic decay.

Hemophilia A is a congenital bleeding disorder resulting from an X-chromosome-linked deficiency of FVIII. The severity of the deficiency generally correlates with the severity of the disease. Some Hemophiliacs (~10%) produce a FVIII protein that is partially or totally inactive. The production of neutralizing antibodies to FVIII also occurs in 5-20% of Hemophiliacs 1-3.

References and Reviews
  1. Lollar P, Fay PJ, Fass DN; Factor VIII and Factor VIIIa. Methods in Enzymology, 222, pg 122, 1993.
  2. Hoyer, LW, Wyshock EG, Colman RW, in Hemostasis and Thrombosis, 3rd Edition, eds. RW Colman, J Hirsh, VJ Marder and EW Salzman, pp. 109-133, J.B. Lippincott Co., Philadelphia, 1994.
  3. Pittman DD, Kaufman RJ. Structure-Function Relationships of Factor VIII Elucidated through Recombinant DNA Technology. Thromb. Haemostas. 61:161-165, 1989.