Cell Signaling Technology

Product Pathways - Apoptosis / Autophagy

Cleaved Caspase-6 (Asp162) Antibody #9761

Applications Reactivity MW (kDa) Source
W H M R 18 Rabbit

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

Specificity / Sensitivity

Cleaved Caspase-6 (Asp162) Antibody detects endogenous levels of the large subunit of caspase-6 resulting from cleavage at aspartic acid162. This antibody does not recognize other cleaved caspases.

Source / Purification

Polyclonal antibodies are produced by immunizing rabbits with a synthetic peptide (KLH coupled) derived from the carboxy-terminal sequence of p18, the large subunit of rat caspase-6. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of Jurkat cell extracts, untreated or etoposide-treated, and NIH/3T3 and C6 cell extracts, untreated or staurosporine-treated, using Cleaved Caspase-6 (Asp162) Antibody.

Background

Caspase-6 (Mch2) is one of the major executioner caspases functioning in cellular apoptotic processes (1,2). Upon apoptotic stimulation, initiator caspases such as caspase-9 are cleaved and activated (3). The activated upstream caspases further process downstream executioner caspases, such as caspase-3 and caspase-6, by cleaving them into large and small subunits, thereby initiating a caspase cascade leading to apoptosis (4,5). One of the major targets for caspase-6 is the membrane associated protein lamin A (6). The cleavage of this protein causes cell membrane malfunction, membrane blebbing and eventual cell death.

  1. Cohen, G.M. (1997) Biochem. J. 326, 1-16.
  2. Faleiro, L. et al. (1997) EMBO J. 16, 2271-2281.
  3. Li, P. et al. (1997) Cell 91, 479-489.
  4. Slee, E. A. et al. (1999) J. Cell. Biol. 144, 281-292.
  5. MacFarlane, M. et al. (1997) J. Cell. Biol. 137, 469-479.
  6. Orth, K. et al. (1996) J. Biol. Chem. 271, 16443-16446.

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