Recombinant Human BCAR1 protein

BCAR1 (Breast Cancer Anti-estrogen Resistance 1), also known as p130Cas, is a scaffold protein implicated in cell signaling pathways regulating adhesion, migration, and survival. Initially identified for its role in conferring resistance to anti-estrogen therapies in breast cancer, BCAR1 has since been recognized as a critical adaptor molecule in diverse physiological and pathological processes. Structurally, it contains multiple protein interaction domains, including an N-terminal SH3 domain, a central substrate domain with tyrosine phosphorylation sites, a serine-rich region, and a C-terminal CAS family homology domain. These domains enable BCAR1 to interact with signaling molecules such as Src family kinases, focal adhesion kinase (FAK), and integrins, facilitating cross-talk between extracellular matrix signals and intracellular signaling cascades.

BCAR1 is a key mediator of integrin-mediated signaling, influencing cytoskeletal reorganization, cell proliferation, and epithelial-mesenchymal transition (EMT). Its phosphorylation status dynamically regulates downstream effectors like Crk, PI3K/Akt, and MAPK pathways, linking mechanical cues to transcriptional responses. Dysregulation of BCAR1 is associated with cancer progression, metastasis, and therapy resistance. Overexpression or hyperactivation of BCAR1 has been observed in breast, ovarian, and lung cancers, correlating with poor prognosis.

Recombinant BCAR1 protein is engineered for in vitro studies to dissect its molecular interactions, phosphorylation dynamics, and structural-functional relationships. Produced via bacterial or mammalian expression systems, it serves as a tool for investigating signaling mechanisms, screening therapeutic inhibitors, and developing diagnostic biomarkers. Research on recombinant BCAR1 continues to advance understanding of its role in cancer biology and its potential as a therapeutic target.