Product Pathways - Cytoskeletal Signaling
Mst3 Antibody #3723
|W F||H M R Mk||Endogenous||50||Rabbit|
Reactivity Key: H=Human M=Mouse R=Rat Mk=Monkey
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Specificity / Sensitivity
Mst3 Antibody detects endogenous levels of total Mst3 protein.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues of human Mst3. Antibodies are purified by protein A and peptide affinity chromatography.
Western blot analysis of extracts from from variuos cell types using Mst3 Antibody.
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).
Mst3 phosphorylates and activates NDR protein kinases, which are involved in the regulation of cell cycle progression and cell morphology (7). Autophosphorylation of Mst3 at Thr178 is required for in vitro kinase activity, and alteration of this residue inhibits the ability of Mst3 to help regulate cell migration in vivo (8).
- Dan, I. et al. (2001) Trends Cell Biol. 11, 220-230.
- Creasy, C.L. et al. (1996) J. Biol. Chem. 271, 21049-21053.
- Lee, K. and Yonehara, S. (2002) J. Biol. Chem. 277, 12351-12358.
- Graves, J.D. et al. (2001) J. Biol. Chem. 276, 14909-14915.
- Lee, K. et al. (2001) J. Biol. Chem. 276, 19276-19285.
- Graves, J.D. et al. (1998) EMBO J. 17, 2224-2234.
- Stegert, M.R. et al. (2005) Mol. Cell. Biol. 25, 11019-11029.
- Lu, T.J. et al. (2006) J. Biol. Chem. 281, 38405-38417.
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For Research Use Only. Not For Use In Diagnostic Procedures.