Technical Data
BIRC3 (Baculoviral IAP Repeat-containing Protein 3, Apoptosis Inhibitor 2, API2, IAP-1, hIAP-1, hIAP1, RING Finger Protein 49, TNFR2-TRAF-signaling Complex Protein 1, C-IAP2, IAP Homolog C, Inhibitor of Apoptosis Protein 1, API2, IAP1, MIHC, RNF49)
cIAP2 is a member of the family of inhibitor of apoptosis proteins (IAP). IAPs suppress mitochondria-dependent and -independent apoptosis by binding to and inhibiting caspases through their BIR domains (reviewed in Liston et al, 2003; Wright and Duckett, 2005). Resistance towards apoptosis is a hallmark of cancer cells, and overexpression of IAPs can contribute to the development of cancer though inhibiting apoptosis. In addition to at least one BIR domain, some IAP members also have a RING-type finger motif at their carboxyl-terminal. The RING finger domain of several IAPs, including cIAP2, have E3 ubiquitin ligase activity and target the degradation of Smac/DIABLO through ubqiuitination. Smac/DIABLO is a death inducer and functions by inhibiting IAP-caspase interactions, thereby promoting apoptosis. Degradation of cell death inducers like Smac/DIABLO is thought to be a conserved mechanism by which IAPs enhance their anti-apoptotic activity, thereby promoting cell survival. The IAPs, including cIAP2, have widespread tissue protein expression, with expression levels and subcellular localization patterns differing depending on the cell lineage (see Vischioni et al. 2005 for a comprehensive study). cIAP2-MALT (API2-MALT1) fusion proteins have been implicated in the molecular pathology of mucosa associated lymphoid tissue (MALT) lymphoma (reviewed in Hosokawa, 2005). AP12-MALT fusion proteins are found in a subset of patients with MALT lymphoma. They are generated by chromosomal translocations whereby the N-terminal portion of AP12 (including the BIR domains) is linked to the C-terminal portion of MALT1 (containing at least an immunoglobulin-like domain and a caspase domain). Several variants of the API2-MALT1 fusion proteins can occur in MALT1 lymphoma patients depending on the chromosomal breakpoints. It is thought that AP12-MALT1 can enhance the activation of NK-kB signalling, which may be relevant to the pathology of MALT lymphomas.

Suitable for use in Western Blot, Immunohistochemistry and Immunoprecipitation. Other applications not tested.

Recommended Dilution:
Western Blot: 1:1000-1:2000
Immunohistochemistry (formalin fixed paraffin embedded): 1:1000-1:5000
Immunoprecipitation: 1:50-1:200
Immunohistochemistry: Frozen
Optimal dilutions to be determined by the researcher.

Positive Control:
Prostate, colon, spleen, many cancer cell lines, many brain tumors

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 at least 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
50ul-20CBlue IceHumanRabbit
Not determined.
Synthetic peptide corresponding to aa152-172 (QDFSALMRSSYHCAMNNENAR) of human cIAP2, GenBank no. 2205253B.
Supplied as a liquid, 0.05% sodium azide.
Recognizes human cIAP1. Should also recognize AP12-MALT1 fusion proteins assuming that they contain the cIAP2 peptide sequence (QDFSALMRSSYHCAMNNENAR) used for immunogen.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Wright CW and CS Duckett. 2005. Reawakening the cellular death program in neoplasia through the therapeutic blockade of IAP function. J Clin Investigation. 115:2673-2678. 2. Liston P, WG Fong and RG Korneluk. 2003. The inhibitors of apoptosis: there is more to life than Bcl2. Oncogene. 22:8568-8580. 3. Vischioni B, P van der Valk, SWS Ing, FAE Kruyt, JA Rodriguez, and G Giaccone. 2006. Expression and localization of inhibitor of apoptosis proteins in normal human tissues. Human Pathology. 37:78-86. 4. Hosokawa Y. 2005. Anti-apoptotic action of API2-MALT1 fusion protein involved in t(11;18)(q21;q21) MALT lymphoma. Apoptosis. 10:25-34.