|Detection of Human WARP by Western Blot. Western blot shows lysates of human prostate tissue. PVDF Membrane was probed with 2 µg/mL of Mouse Anti-Human WARP Monoclonal Antibody (Catalog # MAB6189) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF007). Specific bands were detected for WARP at approximately 50, 40 and 37 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
Von Willebrand factor A (vWFA) domain-related protein (WARP) is a 50 kDa glycoprotein member of the vWFA domain superfamily of extracellular matrix proteins. It is expressed in embryonic articular cartilage, skeletal muscle and basement membranes in the PNS. WARP forms disulfide-linked homodimers and multimers, and complexes with perlecan. Secreted human WARP contains a vWFA domain (aa 34‑213), two fibronectin type III domains (aa 211‑301 and 331‑421) that likely bind to the GAG modification of perlecan, and one potential site for N-linked glycosylation. There is one alternate start site at Met213. Mature human WARP shares 72% aa sequence identity with mature mouse and rat WARP.
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