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VWA1 belongs to the von Willebrand factor (VWF\; MIM 613160) A (VWFA) domain superfamily of extracellular matrix proteins and appears to play a role in cartilage structure and function (Fitzgerald et al., 2002 [PubMed 12062410]).[supplied by OMIM, Nov 2010].. Additionally we are shipping VWA1 Antibodies (24) and VWA1 Kits (6) and many more products for this protein.
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Our results reveal the molecular mechanism of collagen-regulated, A1-mediated platelet adhesion enhancement.
The VWA1 domain of matrilin-3 is primarily responsible for the induction of IL-6 release from primary human chondrocytes.
WARP is ideally placed to function as an adapter protein in the cartilage pericellular matrix.
The distinct localization of WARP in the human and mouse inner ear blood vessels suggests an important role maintaining the integrity of the vasculature.
Evolutionary relationship between von Willebrand factor A domain-related protein (WARP), and the fibril-associated collagen with interrupted triple helix (FACIT) and FACIT-like subfamilies of collagens.
WARP forms macromolecular structures that interact with perlecan to contribute to the assembly and/or maintenance of "permanent" cartilage structures during development and in mature cartilages
Urea was used as a surrogate for shear to study denaturation of the individual VWF recombinant A domains, A1, A2, and A3, and the domain triplet, A1-A2-A3.
VWA1 belongs to the von Willebrand factor (VWF\; MIM 613160) A (VWFA) domain superfamily of extracellular matrix proteins and appears to play a role in cartilage structure and function (Fitzgerald et al., 2002
von Willebrand factor A domain containing 1
, von Willebrand factor A domain-containing protein 1
, von Willebrand factor A domain-related protein