Cayman Bcl-xL (human, recombinant)

Bcl-xL is an anti-apoptotic member of the Bcl-2 family of proteins and is the long isoform of the apoptosis regulator Bcl-x formed by alternative splicing. Bcl-xL is composed of a C-terminal helix that acts as a membrane anchor and four highly conserved Bcl-2 homology (BH) domains. The BH1, BH2, and BH3 domains form a hydrophobic cleft that facilitates Bcl-xL heterodimerization with the pro-apoptotic proteins Bax and Bak, resulting in their inhibition, whereas the BH4 domain regulates intracellular calcium levels.^, Bcl-xL is highly expressed during embryogenesis and neuron and lymphocyte development and is primarily localized to the mitochondrial outer membrane. It inhibits the intrinsic apoptotic pathway by inhibiting Bax- or Bak-induced pore formation in the outer mitochondrial membrane, maintaining the mitochondrial membrane potential, and preventing the release of cytochrome c into the cytosol and the induction of apoptosis. Increased Bcl-xL levels promote cell migration, invasion, and capillary-like structure formation in MXL90 melanoma and AXL42 glioblastoma cancer cells, which endogenously express high levels of Bcl-xL. Mutation of serine 62 (S62A) in Bcl-xL mimics its phosphorylation and abolishes apoptosis induced by the microtubule inhibitor vinblastine (Item No. ) in KB-3 cells. Caymans Bcl-xL (human, recombinant) protein can be used for binding assay applications. This protein consists of 212 amino acids and has a calculated molecular weight of 25.2 kDa. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is approximately 32 kDa.

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