|
||||||||||||||||||
|
||||||||||||||||||
|
|||||||||||||||||||||||||||||||||||
Questions? Please consult our answers to frequently asked questions at http://www.ebioscience.com/faq. DescriptionThe polyclonal antibody reacts with mouse, human, and rat Bcl-xS/L; the antibody was raised against a peptide mapping to the amino terminus of Human Bcl-xS/L. Bcl-2 family of proteins is a key regulator of apoptosis that function to either inhibit or promote cell death. The over expression of members such as Bcl-2 and Bcl-xL inhibit the apoptotic process (1,2). The Bcl-2 family members are also characterized by dimerizing to further modulate apoptosis. Bag-1, for example, has been found to form a heterodimer with Bcl-2 resulting in the enhancement of the anti-apoptotic effect of Bcl-2 (3,4). Other anti-apoptotic Bcl-2 family members include A1, Bcl-xg, Bcl-xb, Mcl-1, BAR, BI-1 and Bcl-w (5). The pro-apoptotic family members include Bax, Bcl-xS, Bad, Bak, NBK, BID, Hrk, Bok, Bim, Noxa and Diva. Bax and Bak have been shown to play a critical role in cytochrome c release from mitochondria and thus initiate apoptosis (6). Bad plays a critical role in the Bax-mediated apoptosis pathway by dimerizing with Bcl-xL, causing the displacment of Bax. The displacement of Bax allows apoptosis to proceed (7). Bcl-xS, a shorter version of Bcl-xL (lacking amino acids 126-188), apparently utilizes a different pathway than Bax to induce cell death. Some research suggests that Bcl-xS uses a novel mechanism for regulating caspase or it may use an alternate cell death effector pathway (8,9). Applications ReportedFor research use only, not for diagnostic or therapeutic use. Purified anti-mo/hu/rat BclxS/L poly has been reported for use in immunoprecipitation, immunoblotting (WB), immunohistochemical staining of frozen tissue sections, and immunohistochemical staining of paraffin embedded tissue sections. Applications TestedPurified anti-mo/hu/rat BclxS/L poly has been tested by immunoblotting (WB). References
1.Huang Z. 2000. Bcl-2 family proteins as targets for anticancer drug design. Oncogene 19(56): 6627-6631 2.Reed JC. 1997. Double identity for proteins of the Bcl-2 family. Nature 387(6635): 773-776 3.Eversole-Cire P, Concepcion FA, Simon MI, Takayama S, Reed JC, Chen J. 2000. Synergistic effect of Bcl-2 and BAG-1 on the prevention of photoreceptor cell death. Invest Ophthalmol Vis Sci 41(7): 1953-1961 4.Coldwell MJ, deSchoolmeester ML, Fraser GA, Pickering BM, Packham G, Willis AE. 2001. The p36 isoform of BAG-1 is translated by internal ribosome entry following heat shock. Oncogene 20(30): 4095-4100 5.Bae j, Hsu SY, Leo CP, Zell K, Hsueh AJ. 2001. Underphosphorylated BAD interacts with diverse antiapoptotic Bcl-2 family proteins to regulate apoptosis. Apoptosis 6(5): 319-330 6.Wei MC, Zong WX, Cheng EH, Lindsten T, Panoutsakopoulou V, Ross AJ, Roth KA, MacGregor GR, Thompson CB, Korsmeyer SJ. 2001. Proapoptotic BAX and BAK: a requisite gateway to mitochondrial dysfunction and death. Science 292(5517): 624-626 7.Yang E, Zha J, Jockel J, Boise LH, Thompson CB, Korsmeyer SJ. 1995. Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death. Cell 80(2): 285-291 8.Fridman JS, Parsels J, Rehemtulla A, Maybaum J. 2001. Cytochrome c depletion upon expression of Bcl-XS. J Biol Chem 276(6): 4205-10 9.Lindenboim L, Yuan J, Stein R. 2000. Bcl-xS and Bax induce different apoptotic pathways in PC12 cells. Oncogene 19(14): 1783-1793 Related ProductsCat. 66-P701 Blocking Peptides for anti-mouse/human/rat BclxS/L polyclonal |
|||||||||||||||||||||||||||||||||||
![]() |
![]() |
|
Copyright © 2000-2008 eBioscience, Inc. Product For Research Use Only: Not for further distribution without written consent. |