von Willebrand Factor, canine

For Research Use Only. Not for use in diagnostic procedures.

Chromosome: 27; NC_006609.2 (41865033..42002564)

Polyclonal

Sheep

This antibody is specific for canine vWF as demonstrated by immunoelectrophoresis and ELISA.

Purified IgG.
Vial containing 1ml of whole IgG representing approximately 1 ml of antiserum. Total protein is 5 mg.

Whole IgG, clear liquid.

IgG concentration is 5 mg/ml, determined by absorbance using an extinction coefficient (E1%280) of 13.4. (lot specific)

Store between -10 to -20 degree C. Product will become viscous but will not freeze. Avoid storage in frost-free freezers. Keep vial tightly capped. Allow product to warm to room temperature and gently mix before use.

Small volumes of anti-VWF antibody vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

von Willebrand Factor (vWF, also previously referred to as Factor VIII related antigen) is a large adhesive protein produced in endothelial cells and megakaryocytes. There are two critical functions of vWF, the first being its involvement in the process of platelet adhesion and aggregation through interaction with platelet receptor glycoprotein Ib, the second being the binding and stabilization of Factor VIII (antihemophilic factor) for secretion and transport in plasma. The vWF precursor protein is synthesized with a 95,000 dalton propeptide (also known as vWF antigen-II), believed to be involved in the intracellular multimerization of the vWF subunits. The mature vWF multimers are then packed into storage organelles within the cell (Weibel-Palade bodies) after which the propeptide is cleaved and released. vWF circulates as multimers of disulphide linked 220,000 dalton subunits and the molecular weight of these multimers ranges from 0.5- 20 million daltons. The concentration of vWF in human plasma is typically 10 ug/ml, but increased levels are often observed in pregnancy and other conditions of physiological stress. von Willebrand's disease (vWD) is perhaps the most common inherited bleeding disorder in humans and is the result of either quantitative deficiencies of vWF (vWD Types I & III), or one of a number of qualitative disorders of vWF structure and function (vWD Type II).

Suitable for use as a source of antibodies to canine vWF.

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von Willebrand factor

von Willebrand factor

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VWF_CANFA

Function: Important in the maintenance of hemostasis, it promotes adhesion of platelets to the sites of vascular injury by forming a molecular bridge between sub-endothelial collagen matrix and platelet-surface receptor complex, glycoprotein Ibalpha/IX/V. Also acts as a chaperone for coagulation factor VIII, delivering it to the site of injury, stabilizing its heterodimeric structure and protecting it from premature clearance from plasma

Subunit structure: Multimeric. Interacts with F8. Ref.2

Subcellular location: Secreted. Secreted ? extracellular space ? extracellular matrix. Note: Localized to storage granules. Ref.2

Tissue specificity: Plasma.

Domain: The propeptide is required for multimerization of vWF and for its targeting to storage granules.

Post-translational modification: All cysteine residues are involved in intrachain or interchain disulfide bonds

By similarity.N- and O-glycosylated

Involvement in disease: Note=Defects in VWF are the cause of von Willebrand disease (VWD) in the Scottish Terrier. VWD is characterized by frequent bleeding. Type I VWD is associated with a deficiency of VWF; type II by normal to decreased plasma level of VWF; type III by a virtual absence of VWF. Ref.4

Sequence similarities: Contains 1 CTCK (C-terminal cystine knot-like) domain.Contains 4 TIL (trypsin inhibitory-like) domains.Contains 3 VWFA domains.Contains 3 VWFC domains.Contains 4 VWFD domains.

1. Montgomery RR, Coller BS, in Hemostasis and Thrombosis, 3rd Edition, eds. RW Colman, J Hirsh, VJ Marder and EW Salzman, pp. 134-168, J.B. Lippincott Co., Philadelphia PA, USA, 1994.
2. Sadler JE; von Willebrand Factor (Minireview); JBC 266:34, pp 22777- 22780, 1991.

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