Human Bcl-XL No cross-reactivity in ELISA with E.coli cell lysate
Recombinant Human Bcl-XL / BCL2L1 protein (Catalog#10455-H08E)
This antibody was produced from a hybridoma resulting from the fusion of a mouse myeloma with B cells obtained from a mouse immunized with purified, recombinant Human Bcl-XL / BCL2L1 (rh Bcl-XL / BCL2L1; Catalog#10455-H08E; NP_612815.1; Met 1-Arg 212). The IgG fraction of the cell culture supernatant was purified by Protein A affinity chromatography.
Monoclonal Mouse IgG1 Clone #07
0.2 μm filtered solution in PBS
This antibody is shipped as liquid solution at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
This antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -80℃. Preservative-Free. Avoid repeated freeze-thaw cycles.
Anti-Bcl-XL Antibody, Mouse Monoclonal 经验证的应用
Please Note: Optimal concentrations/dilutions should be determined by the end user.
Anti-Bcl-XL Antibody, Mouse Monoclonal 图片
Flow cytometric analysis of Purified anti-Human BCL2L1 (Bcl-xL) on HeLa cells. HeLa cells were treated according to manufacturer’s manual (BD Pharmingen™ Cat. No. 554714), and stained with Purified Mouse anti-BCL2L1 (Bcl-xL) (Bold line hisgram), then stained with a FITC-conjugated second step antibody. To demonstrate specificity of staining the binding of 10455-MM07 was blocked by the preincubation of the purified antibody with molar excess of recombinant human BCL2L1 (Bcl-xL) (5 µg, Cat. No. 10455-H08E) for 1 hour (dashed line hisgram).
B-cell lymphoma-extra large (Bcl-xl) is a transmembrane molecule in the mitochondria. Bcl-xL (BCL2L1), belongs to the Bcl-2 family. Members of the bcl-2 family encode proteins that function either to promote or to inhibit apoptosis. Antiapoptotic members such as Bcl-2 and Bcl-xL prevent PCD in response to a wide variety of stimuli to take part in cancer survival. Conversely, proapoptotic proteins, exemplified by Bax and Bak, can accelerate death and in some instances are sufficient to cause apoptosis independent of additional signals. The crystal and solution structures of a Bcl-2 family member, Bcl-xL is like this: The structures consist of two central, primarily hydrophobic α-helices, which are surrounded by amphipathic helices. A 60-residue loop connecting helices αl and α2 was found to be flexible and non-essential for anti-apoptotic activity. Bcl-xL is characterized as an important factor in autophagy, inhibiting Beclin 1-mediated autophagy by binding to Beclin 1. In addition, Beclin 1, Bcl-2 and Bcl-xL can cooperate with Atg5 or Ca2+ to regulate both autophagy and apoptosis. Bcl-xL is also implicated in anoxia induced cell death. The pathway is initiated by the loss of function of the prosurvival Bcl-2 family members Mcl-1 and Bcl-2 / Bcl-XL, resulting in Bax- or Bak-dependent release of cytochrome c and subsequent caspase-9-dependent cell death. Thus, Bcl-xL, the well-characterized apoptosis guards, appears to be important in cell death.
Death Receptor Signaling
B Cell Receptor Signaling Pathway
Vander Heiden MG, et al. (1997) Bcl-xL Regulates the Membrane Potential and Volume Homeostasis of Mitochondria. Cell. 91 (5): 627-37.
Muchmore SW, et al. (1996) X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death. Nature. 381: 335-341.
SharoffEH, et al. (2007) Bcl-2 family members regulate anoxia-induced cell death. Antioxid Redox Signal. 9 (9) :1405-9.
Zhou F, et al. (2011) Bcl-2 and Bcl-xL play important roles in the crosstalk between autophagy and apoptosis. FEBS J. 278 (3): 403-13.