Cell Signaling Technology

Product Pathways - Apoptosis

Caspase-4 Antibody #4450

Applications Reactivity Sensitivity MW (kDa) Source
W H (Mk) Endogenous 45 Rabbit

Applications Key:  W=Western Blotting
Reactivity Key:  H=Human  Mk=Monkey
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-4 Antibody detects endogenous levels of total caspase-4 protein. Processing intermediate forms of caspase-4 are observed at 40 kDa and 32 kDa as previously reported (7). The antibody does not cross-react with other caspases.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ile125 within the p20 subunit of human caspase-4 protein. Antibodies were purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from KARPAS-299, THP-1 and IM-9 cells using Caspase-4 Antibody.

Western Blotting

Western Blotting

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

Background

Caspase-4 (TX/ICH-2/ICErelII) is a member of the caspase family of proteases that play a key role in the execution of apoptosis and activation of inflammatory cytokines (1-3). Expression of caspase-4 has been observed in most tissues except brain, with highest levels in placenta, lung, spleen, and peripheral blood lymphocytes (PBL). Caspase-4 was originally found to contribute to Fas-mediated apoptosis (4). Several caspases (including caspase-4, caspase-5, and mouse caspase-11 and -12) are most closely related to caspase-1 and are capable of inducing apoptosis when over-expressed but are better characterized in the proteolytic activation of inflammatory cytokines (5). Caspase-4 associates with TRAF6 and is involved in the LPS inducible production of inflammatory cytokines IL-8 and MIP1 in THP-1 cells (6). While caspase-4 and mouse caspase-12 localize to the endoplasmic reticulum (ER) and may be activated by drugs that induce ER-stress (7), at least one study suggests that caspase-4 and caspase-12 are not essential for the ER-stress induced apoptosis (8).

  1. Faucheu, C. et al. (1995) EMBO J 14, 1914-22.
  2. Kamens, J. et al. (1995) J Biol Chem 270, 15250-6.
  3. Munday, N.A. et al. (1995) J Biol Chem 270, 15870-6.
  4. Kamada, S. et al. (1997) Oncogene 15, 285-90.
  5. Martinon, F. and Tschopp, J. (2007) Cell Death Differ 14, 10-22.
  6. Lakshmanan, U. and Porter, A.G. (2007) J Immunol 179, 8480-90.
  7. Hitomi, J. et al. (2004) J Cell Biol 165, 347-56.
  8. Obeng, E.A. and Boise, L.H. (2005) J Biol Chem 280, 29578-87.

Application References

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Companion Products

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

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