Cell Signaling Technology

Product Pathways - Cytoskeletal Signaling

Mst4 Antibody #3822

Applications Reactivity Sensitivity MW (kDa) Source
W H M R Mk B Endogenous 52 Rabbit

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

Protocols

Specificity / Sensitivity

Mst4 Antibody detects endogenous levels of total Mst4 protein independent of phosphorylation. The antibody does not cross-react with Mst1-3.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to the amino-terminal residues of human Mst4. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from HeLa, NIH/3T3, C6 and COS cells, using Mst4 Antibody.

Background

Mst kinases, members of the STE20 family of kinases, are upstream activators of MAPK pathways that regulate processes such as apoptosis, morphogenesis and cytoskeletal rearrangements. The amino-terminal kinase domain of Mst is considerably homologous to the kinase domain of yeast STE20 kinase and other p21-activated kinases (1). The carboxy-terminal region of Mst1 and Mst2 contains dimerization and inhibitory domains (1-3). Dimerization and phosphorylation at the activation loop results in translocation of Mst1 from the cytosol to the nucleus (3). Growing evidence indicates that Mst1, Mst2 and Mst3 are activated by apoptotic signals as well as other stress conditions (4-6). Complete activation of Mst1 requires both phosphorylation and caspase-mediated cleavage (4). Sequence alignment of the activation loop of the GCK family indicates that Thr183 of Mst1 and Thr180 of Mst2 are the conserved residues and might be critical for the activity of the kinases. Activated Mst kinases may rely on p38 MAPK and JNK pathways to amplify apoptotic signals (5). Phosphorylation at Ser327 of Mst1, which is close to the caspase-3 recognition site, inhibits caspase-mediated cleavage (4).

  1. Dan, I. et al. (2001) Trends Cell Biol. 11, 220-230.
  2. Creasy, C.L. et al. (1996) J. Biol. Chem. 271, 21049-21053.
  3. Lee, K. and Yonehara, S. (2002) J. Biol. Chem. 277, 12351-12358.
  4. Graves, J.D. et al. (2001) J. Biol. Chem. 276, 14909-14915.
  5. Lee, K. et al. (2001) J. Biol. Chem. 276, 19276-19285.
  6. Graves, J.D. et al. (1998) EMBO J. 17, 2224-2234.

Application References

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Companion Products

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

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