Product Pathways - Apoptosis
Livin (D61D1) XP® Rabbit mAb #5471
|5471S||100 µl (10 western blots)||---||In Stock||---|
|5471P||40 µl (4 western blots)||---||In Stock||---|
|5471||carrier free and custom formulation / quantity||email request|
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|W||1:1000||Human||Endogenous||34, 36||Rabbit IgG|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, IP=Immunoprecipitation, IF-IC=Immunofluorescence (Immunocytochemistry)
Specificity / Sensitivity
Livin (D61D1) XP® Rabbit mAb detects endogenous levels of total livin protein.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ala195 of human livin protein.
Western blot analysis of extracts from various cell lines using Livin (D61D1) XP® Rabbit mAb.
The inhibitor of apoptosis protein (IAP) family consists of an evolutionarily conserved group of apoptosis inhibitors containing a conserved 70 amino acid BIR (baculovirus inhibitor repeat) domain (1,2). Human members of this family include c-IAP1, c-IAP2, XIAP, survivin, livin, and NAIP. Overexpression of IAP family members, particularly survivin and livin, in cancer cell lines and primary tumors suggests an important role for these proteins in cancer progression (3-5). In general, the IAP proteins function through direct interactions to inhibit the activity of several caspases, including caspase-3, caspase-7, and caspase-9 (5,6). In addition, binding of IAP family members to the mitochondrial protein Smac blocks their interaction with caspase-9, thereby allowing the processing and activation of the caspase (2).
Livin (BIRC7/ML-IAP) is a potent anti-apoptotic IAP family member containing a single BIR domain and RING finger motif that is highly expressed in human melanomas and absent in normal tissues (5,7). It is localized in the nucleus and diffusely in the cytoplasm (5). The livin gene encodes two splicing variants, a 298 amino acid isoform (α) and a 280 amino acid form (β), with different biological activity to various apoptotic stimuli (8). In addition to directly inhibiting caspase activity, livin can promote the degradation of the pro-apoptotic protein Smac through the ubiquitin-proteasome pathway (9). Its preferential expression in tumor cells, along with several studies showing that downregulation of livin can promote apoptosis, has led to studies analyzing the use of livin in cancer therapy (10).
- Deveraux, Q.L. and Reed, J.C. (1999) Genes Dev 13, 239-52.
- Deveraux, Q.L. et al. (1998) EMBO J 17, 2215-23.
- Altieri, D.C. et al. (1999) Lab Invest 79, 1327-33.
- Tamm, I. et al. (2000) Clin Cancer Res 6, 1796-803.
- Kasof, G.M. and Gomes, B.C. (2001) J Biol Chem 276, 3238-46.
- Deveraux, Q.L. et al. (1997) Nature 388, 300-4.
- Vucic, D. et al. (2000) Curr Biol 10, 1359-66.
- Ashhab, Y. et al. (2001) FEBS Lett 495, 56-60.
- Ma, L. et al. (2006) Cell Death Differ 13, 2079-88.
- Liu, B. et al. (2007) Cancer Lett 250, 168-76.
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For Research Use Only. Not For Use In Diagnostic Procedures.
XP® is a trademark of Cell Signaling Technology, Inc.
Cell Signaling Technology® is a trademark of Cell Signaling Technology, Inc.