BIRC5 Research Reagents

Baculoviral IAP repeat-containing protein 5 is a protein in humans that is encoded by BIRC5 gene. Multitasking protein that has dual roles in promoting cell proliferation and preventing apoptosis.

The following BIRC5 reagents supplied by CUSABIO are manufactured under a strict quality control system. Multiple applications have been validated and solid technical support is offered.

BIRC5 Antibodies

BIRC5 Antibodies for Homo sapiens (Human)

BIRC5 Antibodies for Mus musculus (Mouse)

BIRC5 Proteins

BIRC5 Proteins for Homo sapiens (Human)

BIRC5 Proteins for Mus musculus (Mouse)

BIRC5 Proteins for Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)

BIRC5 Proteins for Felis catus (Cat) (Felis silvestris catus)

BIRC5 Proteins for Bos taurus (Bovine)

BIRC5 Proteins for Canis lupus familiaris (Dog) (Canis familiaris)

BIRC5 Proteins for Rattus norvegicus (Rat)

BIRC5 Proteins for Sus scrofa (Pig)

BIRC5 Background

Baculoviral IAP repeat-containing protein 5 (BIRC5), also known as survivin, is a protein in humans that is encoded by the BIRC5 gene. Survivin contains a coiled-coil (CC) domain that interacts with chromosomal passenger proteins (including INCENP and borealin) and maintains the residency in the nucleus [1][2][3], and only one BIR domain that makes this protein unique compared to the other IAP family members [4][5]. The survivin protein is highly expressed in most human tumors and embryonic tissues but is barely detected in terminally differentiated cells [6][7]. Tamm I. et al. have shown that survivin inhibits both Bax and Fas-induced apoptotic pathways [8]. Survivin also plays a role in regulating cell mitosis [9]. The upregulation of survivin causes the functional loss of wild type p53. Tumors with high expression of survivin generally bear a poor prognosis and are associated with resistance to therapy. The expression of survivin is differential between cancer and normal tissues, making this protein a useful tool in cancer diagnosis and a promising therapeutic target [6][10]. A growing body of literature suggests the nuclear expression of survivin as a good prognostic marker. Disruption of the survivin induction pathway has increased apoptosis and inhibited tumor growth.

[1] Chantalat L, Skoufias DA, et al. Crystal structure of human survivin reveals a bow tie-shaped dimer with two unusual alpha-helical extensions [J]. Mol Cell, 2000,6: 183-189.
[2] Engelsma D, Rodriguez JA, et al. Homodimerization antagonizes nuclear export of survivin [J]. Traffic, 2007, 8: 1495-1502.
[3] Jeyaprakash AA, Klein UR, et al. Structure of a Survivin-Borealin-INCENP core complex reveals how chromosomal passengers travel together [J]. Cell,2007, 131: 271-285.
[4] Verdecia MA, Huang H, et al. Structure of the human anti-apoptotic protein surviving reveals a dimeric arrangement [J]. Nat. Struct. Biol. 2000, 7 (7): 602-8.
[5] Chantalat L, Skoufias DA, et al. Crystal structure of human survivin reveals a bow tie-shaped dimer with two unusual alpha-helical extensions [J]. Mol. Cell.2000, 6 (1): 183-9.
[6] Sah NK, Khan Z, et al. Structural, functional and therapeutic biology of survivin [J]. Cancer Lett.2006, 244 (2): 164-71.
[7] Ambrosini G, Adida C, et al. A novel anti-apoptosis gene, survivin, expressed in cancer and lymphoma [J]. Nat Med,1997, 3: 917-921.
[8] Tamm I, Wang Y, et al. IAP-family protein survivin inhibits caspase activity and apoptosis induced by Fas (CD95), Bax, caspases, and anticancer drugs [J]. Cancer Res.1998, 58 (23): 5315-20.
[9] Ruchaud S, Carmena M, et al. Chromosomal passengers: conducting cell division [J]. Nat Rev Mol Cell Biol, 2007, 8: 798-812.
[10] Pennati M, Folini M, et al. Targeting survivin in cancer therapy [J]. Expert Opin. Ther. Targets.2008, 12 (4): 463-76.

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