BclxS/L antibody, Blocking Peptides conjugate

Contents: BclxS/L (A18) Blocking Peptide
Catalog Number: 66-P701
Formulation: Each vial contains 100 μg of peptide in 0.5 ml PBS with 0.1% NaN₃ and 100 μg BSA.
Storage Conditions: Store at 4°C.
DO NOT FREEZE.

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66-P701-81

50 ug

Available Formats of This Product
Cat. No.	Format	Excite (nm)	Emit (nm)	Reported Applications
66-P701	Blocking Peptides for anti-mouse/human/rat BclxS/L polyclonal	N/A	N/A	WB

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Description

Bcl-xS/L is provided as an affinity purified rabbit polyclonal antibody, 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 Reported

For research use only, not for diagnostic or therapeutic use. This blocking peptide has been reported for use in competition studies.

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

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