Technical Data
Aven (Apoptosis Caspase Activation Inhibitor, Cell Death Regulator Aven, PDCD12)
The Bcl-2 family regulates apoptosis in response to a wide range of stimuli through control of mitochondrial cytochrome c release and caspase activation. 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. 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.

Suitable for use in Immunofluorescence, Flow Cytometry, ELISA and Western Blot. Other applications not tested.

Recommended Dilutions:
Western Blot: 1:1000
Immunofluorescence (IF-IC): 1:50
Flow Cytometry: 1:200
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20C. Aliquots are stable for 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
PabIgGAffinity Purified
100ul-20CBlue IceRabbit
Not Determined
Synthetic peptide corresponding to residues at the carboxy terminus of Aven
Purified by Protein A affinity chromatography
Supplied as a liquid in 10mM sodium HEPES, pH 7.5, 150mM sodium chloride, 0.1mg/ml BSA, 50% glycerol.
Detects endogenous levels of total Aven protein. Species Crossreactivity: human, monkey, mouse and rat
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Harris, M.H. and Thompson, C.B. (2000) Cell Death. Differ. 7, 1182119. 2. Cory, S. et al. (2003) Oncogene 22, 85908607. 3. Scorrano, L. and Korsmeyer, S.J. (2003) Biochem. Biophys. Res. Commun. 304, 437444. 4. Chau, B.N. et al. (2000) Mol. Cell 6, 3140. 5. Choi, J. et al. (2006) Leuk. Res. 30, 10191025. 6. Paydas, S. et al. (2003) Ann. Oncol. 14, 10451050.