Cell Signaling Technology

Product Pathways - Apoptosis

Aven Antibody #2300

Applications Reactivity Sensitivity MW (kDa) Source
W IF-IC F H M R Mk Endogenous 50 Rabbit

Applications Key:  W=Western Blotting  IF-IC=Immunofluorescence (Immunocytochemistry)  F=Flow Cytometry
Reactivity Key:  H=Human  M=Mouse  R=Rat  Mk=Monkey
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

Aven Antibody detects endogenous levels of total Aven protein.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues at the carboxy terminus of Aven. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from HeLa (human), L929 (mouse) and PC12 (rat) cell lines, using Aven Antibody.

Flow Cytometry

Flow Cytometry

Flow cytometric analysis of Hela cells, using Aven Antibody (blue) compared to a nonspecific negative control antibody (red).

IF-IC

IF-IC

Immunofluorescent analysis of HeLa cells showing cytoplasmic localization, using Aven Antibody.


Background

The Bcl-2 family regulates apoptosis in response to a wide range of stimuli through control of mitochondrial cytochrome c release and caspase activation (1-3). Cytosolic Apaf-1 forms a complex with caspase-9 in the presence of cytochrome c and dATP, ultimately leading to caspase-9 activation and subsequent activation of caspase-3. A large number of proteins have been found to interact with Bcl-2 and other family members that have been shown to help regulate apoptosis. Aven was identified in a yeast two-hybrid screen as a bcl-xL interacting protein (4). It also interacts with other anti-apoptotic family members, including Bcl-2, but fails to interact with pro-apopotic proteins Bax and Bak. Aven inhibits apoptosis and enhances anti-apopotic activity of Bcl-xL. It interferes with association with Apaf-1 and activation of caspase-9. Aven overexpression is associated with poor prognosis in acute lymphoblastic leukemia (5,6).

  1. Harris, M.H. and Thompson, C.B. (2000) Cell Death. Differ. 7, 1182-1191.
  2. Cory, S. et al. (2003) Oncogene 22, 8590-8607.
  3. Scorrano, L. and Korsmeyer, S.J. (2003) Biochem. Biophys. Res. Commun. 304, 437-444.
  4. Chau, B.N. et al. (2000) Mol. Cell 6, 31-40.
  5. Choi, J. et al. (2006) Leuk. Res. 30, 1019-1025.
  6. Paydas, S. et al. (2003) Ann. Oncol. 14, 1045-1050.

Application References

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Companion Products


For Research Use Only. Not For Use In Diagnostic Procedures.

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