Background
Survivin  is a member of the family of inhibitor of apoptosis proteins (IAP), and is involved in both the control of apoptosis and regulation of cell division.  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.  Structurally, survivin is composed of a single BIR domain and an extended COOH-terminal a-helical coiled-coil domain; survivin does not contain a RING-finger domain.    Survivin is highly expressed in embryonic and fetal organs, and is cell cycle regulated with a marked increase in the G₂M phase where it plays a role in facilitating cell division (reviewed in Li, 2005 and Zaffaroni et al, 2005).  Survivin is undetectable in most normal differentiated and non-proliferating tissues,  but is highly expressed in cancer.  Expression  has been described in the majority of human tumor types including lung, breast, colon, gastric, leukemias, neuroblastoma, brain tumors, pheochromocytoma, soft tissue sarcomas, melanomas and other skin tumors.  Additionally, survivin expression has been detected in a variety of preneoplastic or benign leisons, suggesting that re-expression of survivin may occur early during malignant transformation or following a disruption in the balance between cell division and apoptosis. Human survivin is a 142 amino acid protein which migrates at ~ 16.5 kDa on SDS-PAGE gels. Multiple surviving splice variants have been described and therefore the molecular weight may vary according to the isoform(s) expressed.  Described splice variants include: 1. Survivin-2B results insertion of an alternative exon. 2. Survivin-deltaEx3 results from the removal of exon 3. 3. Survivin-3B results from the addition of a novel exon 3B. 4. Survivin 2alpha consists of exon 1 and 2 and the acquisition of a new in-frame spot codon, predicting a truncated 74 amino acid protein.  Users are encouraged to refer to the NCBI AceView (http://www.ncbi.nlm.nih.gov/IEB/Research/Acembly/) and BLAST (http://www.ncbi.nlm.nih.gov/BLAST/) data bases for more information about survivin and splice variants.

Antigen
Full-length recombinant human survivin protein was used as immunogen.

Genebank Info (Protein)
NP_001081100

Related Products

Reference
1. Li F. 2005. Role of survivin and its splice variants in tumorigenesis. British J of Cancer. 92:212-216.
2. 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.
3. Liston P, WG Fong and RG Korneluk. 2003. The inhibitors of apoptosis: there is more to life than Bcl2. Oncogene. 22:8568-8580.
4. Zaffaroni N, M Pennati and MG Daidone. 2005. Survivin as a target for new anticancer interventions. J Cell Mol Med. 9:360-372.

Product Citations
1. Survivin and heat shock protein 25/27 colocalize with cleaved caspase-3 in surviving reactive astrocytes following excitotoxicity to the immature brain. Villapol S, L Acarin, M Faiz, B Castellano, B Gonzalez. Neuroscience 153: 108-119 (2008).  IHC (frozen): rat brain tissue, Figs. 1A-I, 2A-G.