|Detection of Human CBL by Western Blot. Western blot shows lysates of MCF‑7 human breast cancer cell line, K562 human chronic myelogenous leukemia cell line, and Raji human Burkitt's lymphoma cell line. PVDF Membrane was probed with 0.5 µg/mL of Goat Anti-Human/Mouse CBL Antigen Affinity-purified Polyclonal Antibody (Catalog # AF5998) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF109). A specific band was detected for CBL at approximately 120 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
CBL (Lake Casitas, California mouse B-lineage Lymphoma; also RING finger protein 55) is a 120‑125 kDa cytosolic member of the CBL family of proteins. It is widely expressed, being found in cells such as fibroblasts, adipocytes, osteoclasts, podocytes and mammary epithelium. CBL negatively regulates RTK signaling by acting as an E3 ubiquitin ligase. Following activation via phosphorylation, CBL will interact with multiple signaling molecules such as Src, ZAP-70, EGFR and SHP1. Human CBL is 906 amino acids (aa) in length. It contains an N-terminal phosphoTyr-binding region that consists of one alpha -helix bundle, an EF hand segment, and an SH2 domain (aa 47‑342), a RING finger domain that interacts with E2 enzymes (aa 381‑423) a Pro-rich SH3 domain (aa 477‑688), and a Leu‑zipper/Ubiquitin‑associated region (aa 861‑892). There is one potential alternative start site at Met55. Over aa 775‑906, human CBL shares 91% aa identity with mouse CBL.
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