Vitronectin Antibodies

Affinity Biologicals, Inc. manufactures a broad range of Vitronectin Antibodies which can be found in the listing below.   Further information about each individual Vitronectin Antibody is available by following the associated links.  Our Vitronectin 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 Vitronectin Antibodies are manufactured for use in research applications.

Vitronectin, HumanHostCatalogue No.SizeStatus
Purified IgGSheepSAVN-IG10mg vialSpecial Order
Affinity Purified IgGSheepSAVN-AP0.5mg vialStocked Item
Affinity Purified HRP Conjugated IgGSheepSAVN-APHRP0.1mg vialStocked Item

Listing of Vitronectin Antibodies

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 μg/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