Recombinant Rabbit monoclonal primary
Recombinant Bcl-XL Monoclonal Antibody (ET1603-28)
Jurkat cell lysates, HepG2, Hela, MCF-7, human colon carcinoma tissue, human kidney tissue, human breast carcinoma tissue.
Store at +4C after thawing. Aliquot store at -20C or -80C. Avoid repeated freeze / thaw cycles.
1*TBS (pH7.4), 0.05% BSA, 40% Glycerol. Preservative: 0.05% Sodium Azide.
Protein A affinity purified.
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
Belongs to the Bcl-2 family.
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.
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.
Mitochondrion inner membrane, Mitochondrion outer membrane, Mitochondrion matrix, Cytoplasmic vesicle, Cytoplasm, Nucleus membrane.
The Bcl-2 gene was isolated at the chromosomal breakpoint of t(14;18) bearing follicular B cell lymphomas. Bcl-2 blocks cell death following a variety of stimuli and confers a death-sparing effect to certain hematopoietic cell lines following growth factor withdrawal. A second protein, designated Bcl-associated X protein (Bax) p21, has extensive amino acid homology with Bcl-2 and both homodimerizes and heterodimerizes with Bcl-2. Overexpression of Bax accelerates apoptotic death induced by cytokine deprivation in an IL-3-dependent cell line, and Bax also counters the death repressor activity of Bcl-2. Bcl-x, one of several additional proteins with sequence homology to Bcl-2, is expressed as Bcl-xL, a 233 amino acid protein with 43% sequence identity with Bcl-2 that suppresses cell death, and Bcl-xS, a shorter variant that is 178 amino acids in length and lacks a 63 amino acid region (amino acids 126-188) found in Bcl-xL and which functions as a dominant inhibitor of Bcl-2. A further apoptosis-inducing protein, Bad, dimerizes both with Bcl-xL and to a lesser extent with Bcl-2, thus displacing Bax and inducing apoptosis.