|Detection of Human/Mouse/Rat CD2AP by Western Blot. Western blot shows lysates of MOLT‑4 human acute lymphoblastic leukemia cell line, Ramos human Burkitt's lymphoma cell line, KG‑1 human acute myelogenous leukemia cell line, M1 mouse myeloid leukemia cell line, and Y3‑Ag rat myeloid cell line. PVDF membrane was probed with 0.2 µg/mL of Human/Mouse/Rat CD2AP Antigen Affinity‑purified Polyclonal Antibody (Catalog # AF4474) followed by HRP-conjugated Anti‑Sheep IgG Secondary Antibody (Catalog # HAF016). A specific band was detected for CD2AP at approximately 80 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
CD2AP (CD2-associated protein; also known as CMS) is an 80 kDa member of the CIN85/CD2AP family of adaptor proteins. Although CD2AP is ubiquitously expressed, it is often associated with glomerular podocytes. CD2AP serves as a scaffold between membrane proteins and the cytoskeleton. Through a Pro-rich region and SH3 domains, it is known to bind to such proteins as CD2, c-CBL, and p130Cas. Human CD2AP is 639 amino acids (aa) in length. It contains three SH3 homology domains (aa 4‑324), one Pro-rich region (aa 336‑422) and a C-terminal coiled-coil region that mediates homodimerization. Over aa 423‑580, human CD2AP shares 96% and 79% aa identity with dog and mouse CD2AP, respectively.
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