Bcl-XL Recombinant Rabbit Monoclonal Antibody [SZ3-03] (ET1603-28)

UNIPROT #

Q07817

PROTEIN NAME

Bcl-XL

SYNONYMS

Apoptosis regulator Bcl X antibody;Apoptosis regulator Bcl-X antibody;Apoptosis regulator BclX antibody;B cell lymphoma 2 like antibody;B2CL1_HUMAN antibody;Bcl 2 like 1 protein antibody;Bcl X antibody;Bcl xL antibody;BCL XL/S antibody;Bcl xS antibody;Bcl-2-like protein 1 antibody;Bcl2 Like 1 antibody;Bcl2 related gene antibody;Bcl2-L-1 antibody;BCL2L antibody;Bcl2l1 antibody;BCLX antibody;BclXL antibody;BclXs antibody;DKFZp781P2092 antibody;PPP1R52 antibody;Protein phosphatase 1 regulatory subunit 52 antibody

SEQUENCE SIMILARITIES

Belongs to the Bcl-2 family.

TISSUE SPECIFICITY

Bcl-X(S) is expressed at high levels in cells that undergo a high rate of turnover, such as developing lymphocytes. In contrast, Bcl-X(L) is found in tissues containing long-lived postmitotic cells, such as adult brain.

POST-TRANSLATIONAL MODIFICATION

Proteolytically cleaved by caspases during apoptosis. The cleaved protein, lacking the BH4 motif, has pro-apoptotic activity.; Phosphorylated on Ser-62 by CDK1. This phosphorylation is partial in normal mitotic cells, but complete in G2-arrested cells upon DNA-damage, thus promoting subsequent apoptosis probably by triggering caspases-mediated proteolysis. Phosphorylated by PLK3, leading to regulate the G2 checkpoint and progression to cytokinesis during mitosis. Phosphorylation at Ser-49 appears during the S phase and G2, disappears rapidly in early mitosis during prometaphase, metaphase and early anaphase, and re-appears during telophase and cytokinesis.; Ubiquitinated by RNF183 during prolonged ER stress, leading to degradation by the proteosome.

SUBCELLULAR LOCATION

Mitochondrion inner membrane, Mitochondrion outer membrane, Mitochondrion matrix, Cytoplasmic vesicle, Cytoplasm, Nucleus membrane.

FUNCTION

It is a well-established concept in the field of apoptosis that relative amounts of pro- and anti-survival Bcl-2 family of proteins determine whether the cell will undergo cell death; if more Bcl-xL is present, then pores are non-permeable to pro-apoptotic molecules and the cell survives. However, if Bax and Bak become activated, and Bcl-xL is sequestered away by gatekeeper BH3-only factors (e.g. Bim) causing a pore to form, cytochrome c is released leading to initiation of caspase cascade and apoptotic events. While the exact signaling pathway of Bcl-xL is still not known, it is believed that Bcl-xL differs highly from Bcl-2 in their mechanism of inducing apoptosis. Bcl-xL is about ten times more functional than Bcl-2 when induced by the chemotherapy drug, Doxorubicin and can specifically bind to cytochrome C residues, preventing apoptosis. It can also prevent the formation of Apaf-1 and Caspase 9 complex by acting directly upon Apaf-1 rather than Caspase 9, as shown in nematode homologs.