Description

Vitronectin Polyclonal Antibody – Affinity Purified – HRP Conjugated

Affinity’s Vitronectin Polyclonal Antibody – Affinity Purified – HRP Conjugated is the highest level of our horseradish peroxidase conjugated Vitronectin antibodies.  During the Antigen Affinity Purification process the IgG has had any non-specific immunoglobulin fraction eliminated which enriches the specificity of the remaining immunoglobulin towards the target antigen.  The result is a very high-purity product with a substantially higher titre than whole or purified IgG.  Our Vitronectin Polyclonal Antibody – Affinity Purified – HRP Conjugated is provided in a solution of HEPES buffered saline containing 50% glycerol (v/v) and has been conjugated with Horseradish Peroxidase as an enzyme reporter.  This antibody is generally intended for use as labeled primary antibodies in applications such as immunoassay and immunoblotting.

Product Code: SAVN-APHRP

Retail Product Size: 0.1mg vial

Host Animal: Sheep Anti-Human Vitronectin Polyclonal Antibody – Affinity Purified – HRP Conjugated

Species Cross Reactivity: View Chart

Product Datasheet: Vitronectin Polyclonal Antibody, affinity purified hrp conjugated anti-human sheep IgG1

Description of Vitronectin (VN)

Vitronectin (VN), previously known as serum-spreading factor or S-protein, is a plasma and serum glycoprotein with a normal concentration ranging from 200 – 400 ug/ml. It exists in both a 75 kDa single-chain form and a 65 + 10 kDa two-chain form. Vitronectin can exist in a least two different conformational forms. The majority of VN found in the circulation is present in the native (“closed”) form. In this form, most of the binding sites for other ligands are cryptic. The second form of VN, the denatured (“open”, multimeric) form, is a result of a conformational change in the native protein induced by denaturants such as urea, adsorption onto surfaces, low pH or reduction and alkylation. This conformational change leads to exposure of the heparin binding site, formation of disulfide-bonded multimers and rupture of the disulfide bond that links the 10 kDa light chain to the 65 kDa heavy chain of the two chain form. The liver is the primary site of VN synthesis, however, Vn is also found in platelets, megakaryocytes, monocytes and macrophages. VN plays an important role in a number of physiological and pathophysiological processes. It promotes the adhesion and spreading of a wide variety of cell types and is a subcomponent of the soluble SC5b-9 complex of complement where it protects bystander cells from cytolysis. VN also plays an important role in fibrinolysis by stabilizing PAI-1 in its active conformation which otherwise rapidly converts to a latent form.^1-3

References and Reviews

1. Tomasini, B.R., and Mosher, D.F. Vitronectin. Prog. Hemost. Thromb., 10:269-305, 1991.
2. Hess, S., Stockmann, A., Voler, W., and Preissner, K.T. Multimeric vitronectin: structure and function. In: Biology of Vitronectins and their Receptors, Elsevier Science Publishers, Amsterdam, p. 21-29, 1993.
3. Preissner, K.T., and Jenne, D. Vitronectin: a new molecular connection in haemostasis. Thrombo. Haemost., 66(2):189-194, 1991