Cell Signaling Technology

Product Pathways - Apoptosis / Autophagy

Caspase-5 Antibody #4429

Applications Reactivity Sensitivity MW (kDa) Source
W H Endogenous 48, 20 Rabbit

Applications Key:  W=Western Blotting
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

Caspase-5 Antibody detects endogenous levels of total caspase-5 protein. This antibody detects the p20 subunit of active caspase-5.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Leu130 within the p20 subunit of human caspase-5 protein. Antibodies were purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from THP-1, HT-1080 and Ramos cells using Caspase-5 Antibody.

Western Blotting

Western Blotting

Western blot analysis of extracts from recombinant, active caspase-1, -4, and -5 using Caspase-5 Antibody.

Western Blotting

Western Blotting

Western blot analysis of extracts from THP-1 cells, differentiated with TPA (12-O-Tetradecanoylphorbol-13-Acetate) #4174 (80 nM, overnight) followed by LPS (1 μg/ml) for the indicated times, using Caspase-5 Antibody.


Background

Caspase-5 (Ich-3/ICErelIII/TY) is a member of the caspase family of cysteine proteases that play a key role in the execution of apoptosis and activation of inflammatory cytokines (1-3). Caspase-5 is widely expressed, with highest expression observed in placenta and lung (1). Interferon-γ and LPS regulate expression of caspase-5 (2,4). Members of the caspase-1 subfamily of caspases, which includes caspase-4, -5, and murine caspase-11 and -12, can induce apoptosis when over-expressed and mediate the proteolytic activation of inflammatory cytokines (5). Processing of IL-1β occurs through the activation of an inflammasome complex consisting of caspase-1, caspase-5, Pycard and NALP1 (6). Transcription factor Max, a component of the Myc/Mad/Max network, is cleaved by caspase-5 during Fas-induced apoptosis (7). Several alternative spliced variants of caspase-5 have been identified (8). Frameshift mutations of caspase-5 have been observed in leukemia, lymphoma (9), and colorectal cancers (10).

  1. Munday, N.A. et al. (1995) J Biol Chem 270, 15870-6.
  2. Wang, S. et al. (1996) J Biol Chem 271, 20580-7.
  3. Faucheu, C. et al. (1996) Eur J Biochem 236, 207-13.
  4. Lin, X.Y. et al. (2000) J Biol Chem 275, 39920-6.
  5. Martinon, F. and Tschopp, J. (2007) Cell Death Differ 14, 10-22.
  6. Martinon, F. et al. (2002) Mol Cell 10, 417-26.
  7. Krippner-Heidenreich, A. et al. (2001) Biochem J 358, 705-15.
  8. Eckhart, L. et al. (2006) Biochem Biophys Res Commun 348, 682-8.
  9. Takeuchi, S. et al. (2003) Leuk Res 27, 359-61.
  10. Trojan, J. et al. (2004) Int J Colorectal Dis 19, 538-44.

Application References

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Companion Products

This product is intended for research purposes only. The product is not intended to be used for therapeutic or diagnostic purposes in humans or animals.

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