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     Gel: 6%SDS-PAGE, Lysate: 40 μg, Lane 1-2: Mouse thymus tissue, Raji cell lysates, Primary antibody: P11611(CBL Antibody) at dilution 1/1000, Secondary antibody: Goat anti rabbit IgG at 1/5000 dilution, Exposure time: 1 minute    

  
  

The Casitas B-lineage lymphoma (CBL) family of proteins, including CBL, CBL-B, and CBL-C, are evolutionarily conserved E3 ubiquitin ligases that play critical roles in regulating intracellular signaling pathways. Initially identified as proto-oncogenes, CBL proteins function as negative regulators of tyrosine kinase signaling by tagging activated receptor tyrosine kinases (RTKs) and other signaling intermediates with ubiquitin molecules, marking them for proteasomal degradation or endosomal sorting. This activity helps maintain signal transduction homeostasis. Structurally, CBL proteins contain a tyrosine kinase-binding domain, a RING finger domain essential for E3 ligase activity, and proline-rich regions mediating protein interactions.

Dysregulation of CBL proteins, particularly through somatic mutations or deletions, has been implicated in various malignancies. Loss-of-function mutations in CBL genes disrupt their ubiquitin ligase activity, leading to sustained activation of oncogenic pathways like RAS/MAPK and PI3K/AKT, contributing to leukemogenesis and solid tumors. Germline CBL mutations are associated with developmental disorders such as Noonan syndrome-like conditions.

CBL antibodies have become valuable tools in biomedical research, enabling the detection of CBL expression levels, post-translational modifications, and subcellular localization in normal and pathological states. In diagnostics, they aid in identifying CBL mutations in cancer patients, while therapeutic applications explore targeting CBL-mediated pathways. However, functional redundancy among CBL family members and context-dependent roles in different cell types continue to present challenges in fully understanding their therapeutic potential.