|Application ||WB, IHC|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||55630 Da|
|Other Names||Serine/threonine-protein kinase 4, Mammalian STE20-like protein kinase 1, MST-1, STE20-like kinase MST1, Serine/threonine-protein kinase Krs-2, Serine/threonine-protein kinase 4 37kDa subunit, MST1/N, Serine/threonine-protein kinase 4 18kDa subunit, MST1/C, STK4, KRS2, MST1|
|Target/Specificity||A synthetic peptide corresponding to residues near the N-terminus of human Mst1 was used as an immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Mst1 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. Key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. STK3/MST2 and STK4/MST1 are required to repress proliferation of mature hepatocytes, to prevent activation of facultative adult liver stem cells (oval cells), and to inhibit tumor formation (By similarity). Phosphorylates 'Ser-14' of histone H2B (H2BS14ph) during apoptosis. Phosphorylates FOXO3 upon oxidative stress, which results in its nuclear translocation and cell death initiation. Phosphorylates MOBKL1A, MOBKL1B and RASSF2. Phosphorylates TNNI3 (cardiac Tn-I) and alters its binding affinity to TNNC1 (cardiac Tn-C) and TNNT2 (cardiac Tn-T). Phosphorylates FOXO1 on 'Ser-212' and regulates its activation and stimulates transcription of PMAIP1 in a FOXO1-dependent manner. Phosphorylates SIRT1 and inhibits SIRT1-mediated p53/TP53 deacetylation, thereby promoting p53/TP53 dependent transcription and apoptosis upon DNA damage. Acts as an inhibitor of PKB/AKT1. Phosphorylates AR on 'Ser-650' and suppresses its activity by intersecting with PKB/AKT1 signaling and antagonizing formation of AR-chromatin complexes.|
|Cellular Location||Cytoplasm. Nucleus. Note=The caspase-cleaved form cycles between the nucleus and cytoplasm|
|Tissue Location||Expressed in prostate cancer and levels increase from the normal to the malignant state (at protein level). Ubiquitously expressed.|
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Provided below are standard protocols that you may find useful for product applications.
The human serine/threonine kinase, mammalian STE20-like kinase (MST), is considerably homologous to the budding yeast kinases, SPS1 and STE20, throughout their kinase domains. When stably expressed in HeLa cells, MST highly sensitizes the cells to death receptor-mediated apoptosis by accelerating caspase-3 activation. These findings suggest that MST1 and MST2 play a role in apoptosis both upstream and downstream of caspase activation (1). MST1 is cleaved and activated by caspases during apoptosis and is capable of inducing apoptotic morphological changes such as chromatin condensation upon over[removed]2). Mst1 can phosphorylate H2B at S14 in vitro and in vivo, and the onset of H2B S14 phosphorylation is dependent upon cleavage of Mst1 by caspase-3. These data reveal a histone modification that is uniquely associated with apoptotic chromatin in species ranging from frogs to humans and provide insights into a previously unrecognized physiological substrate for Mst1 kinase (3).
1. Lee KK, et al. J. Biol Chem. 276(22):19276-85, 2001.
2. Ura S, et al. Proc Natl Acad Sci USA 98(18):10148-53, 2001
3. Cheung WL, et al. Cell. 113(4):507-17, 2003.
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