XIAP Antibody



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XIAP Antibody Summary

Recombinant BIR2 domain protein fragment of human XIAP was used as immunogen. The BIR2 domain used for immunogen corresponds to amino acids 163-230 of human XIAP (Deveraux et al, 1999).
The antibody recognizes epitopes in the BIR2 domain of XIAP. Therefore it can recognize full-length XIAP and XIAP cleavage fragments containing the BIR2 domain. However, XIAP cleavage fragments may be biologically unstable, and therefore cleavage fragments may be difficult to detect.
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Packaging, Storage & Formulations

Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.
0.02% Sodium Azide
This product is unpurified. The exact concentration of antibody is not quantifiable.

Reactivity Notes

Cross reacts with Gerbil, Human, Mouse and Rat.


XIAP [human X-linked IAP, hILP (human IAP-like protein), MIHA, BIRC4) 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 XIAP, have E3 ubiquitin ligase activity and target the degradation of Smac/DIABLO through ubqiuitination (Morizane et al, 2005). 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. XIAP is highly characterized with respect to its structure and biochemical mechanisms, and has received interest as a therapeutic target (reviewed in Schimmer, 2006). Since XIAP blocks a substantial portion of the apoptosis pathway and is associated with chemoresistance in cancer cells, inhibiting XIAP has been a focus for potential therapeutics. Approaches have included antisense oligonucleotides and small molecule inhibitors. Small molecules that that target the BIR2 and BIR3 domains of XIAP are considered particularly attractive. This is because the BIR domains inhibit caspase activity, and it is thought that removing the inhibition should increase the cell's ability to undergo apoptosis as well as decrease its potential for chemoresistance. Full-length human XIAP is a 497 amino acid protein and migrates at approx. 53 kDa on SDS-PAGE.


This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

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Blogs on XIAP.

Caspase 9 - an important apoptosis marker
Caspases are essential mediators of programmed cell death and are needed for both the induction of apoptosis as well as for aiding the degradation of cellular structures. Initiator caspases (such as Caspase-9) sense and respond to various signals i...  Read full blog post.

cIAP2 - balancing cell death and cell survival
The inhibitor of apoptosis proteins (IAPs) are important regulators of cell death and inflammation. The cellular inhibitor of apoptosis protein 2 (cIAP2) contains three Baculovirus IAP repeat (BIR) domains, a Ubiquitin associated (UBA) domain, and...  Read full blog post.

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Gene Symbol XIAP

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