Cell Signaling Technology

Product Pathways - Apoptosis

Siva-1 Antibody #12532

Applications Reactivity Sensitivity MW (kDa) Source
W IP H Endogenous 19 Rabbit

Applications Key:  W=Western Blotting  IP=Immunoprecipitation
Reactivity Key:  H=Human
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

Siva-1 Antibody recognizes endogenous levels of total Siva-1 protein. This antibody does not cross-react with Siva-2. This antibody cross-reacts with a protein of unknown origin at ~70 kDa.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Pro71 of human Siva-1 protein. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from MOLT-4, HBP-ALL, and CCRF-CEM cells using Siva-1 Antibody.

Western Blotting

Western Blotting

Western blot analysis of extracts from 293T cells, mock transfected (-), transfected with a construct expressing Myc/DDK-tagged full-length human Siva-1 (hSiva-1-Myc/DDK; +), or transfected with a construct expressing Myc/DDK-tagged full-length human Siva-2 (hSiva-2-Myc/DDK; +), using Siva-1 Antibody or Myc-Tag (71D10) Rabbit mAb #2278.

Western Blotting

Western Blotting

Immunoprecipitation of Siva-1 from MOLT-4 cell extracts using Normal Rabbit IgG #2729 (lane 2) or Siva-1 Antibody (lane 3). Lane 1 is 10% input. Western blot analysis was performed using Siva-1 Antibody.


Background

First identified as a pro-apoptotic protein that binds the cytoplasmic tail of the TNF receptor superfamily member CD27 (1), Siva-1 also binds several other TNFR family members including glucocorticoid-induced tumor necrosis factor receptor (GITR) and OX40 (1-3), as well as anti-apoptotic Bcl-2 family members Bcl-xL and Bcl-2 (4,5). Siva-1 is composed of a central death domain homology region, a C-terminal box-B-like ring finger followed by a zinc finger-like domain, and a unique N-terminal amphipathic helical region (SAH) (1,4). Studies have demonstrated that Siva-1 has the ability to induce cell death via both the extrinsic and intrinsic apoptotic pathways (1-8). The SAH domain of Siva-1 is responsible for the inhibition of the pro-survival activities of Bcl-xL and Bcl-2, leading to caspase-mediated cell death (4,5,8). Siva-1 plays a role in T cell signaling and homeostasis by inhibiting NF-κB activity, also resulting in apoptotic cell death (7,9). An alternative splice variant of Siva-1, Siva-2, lacks part of the SAH and death domains and is less effective at inducing apoptosis (1,2,5,8). Studies in xenografts have shown that down-regulation of Siva-1 inhibits tumorigenesis in response to p53 activation (10). Down-regulation of Siva-1 may also play a role in tumor metastasis through its regulation of the epithelial-mesenchymal transition (EMT) and cell migration (11). Overexpression of Siva-1 is implicated in several pathological conditions including acute ischemic injury (12) and Coxsackievirus infection (13).

  1. Prasad, K.V. et al. (1997) Proc Natl Acad Sci U S A 94, 6346-51.
  2. Yoon, Y. et al. (1999) Oncogene 18, 7174-9.
  3. Spinicelli, S. et al. (2002) Cell Death Differ 9, 1382-4.
  4. Xue, L. et al. (2002) Proc Natl Acad Sci U S A 99, 6925-30.
  5. Chu, F. et al. (2004) Apoptosis 9, 83-95.
  6. Cao, C. et al. (2001) J Biol Chem 276, 11465-8.
  7. Gudi, R. et al. (2006) Oncogene 25, 3458-62.
  8. Py, B. et al. (2004) J Immunol 172, 4008-17.
  9. Hench, V.K. and Su, L. (2011) BMC Immunol 12, 54.
  10. Du, W. et al. (2009) Cell Death Differ 16, 1493-504.
  11. Li, N. et al. (2011) Proc Natl Acad Sci U S A 108, 12851-6.
  12. Padanilam, B.J. et al. (1998) Kidney Int 54, 1967-75.
  13. Henke, A. et al. (2000) J Virol 74, 4284-90.

Application References

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Companion Products

For Research Use Only. Not For Use In Diagnostic Procedures.

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