|Reactivity||Human, Mouse, Rat|
|Calculated MW||115281 Da|
|Other Names||Protein phosphatase 1 regulatory subunit 12A, Myosin phosphatase-targeting subunit 1, Myosin phosphatase target subunit 1, Protein phosphatase myosin-binding subunit, PPP1R12A, MBS, MYPT1|
|Target/Specificity||A synthetic peptide corresponding to residues in C-terminus of human MYPT1 or MYPT2 was used as 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||MYPT1/MYPT2 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Key regulator of protein phosphatase 1C (PPP1C). Mediates binding to myosin. As part of the PPP1C complex, involved in dephosphorylation of PLK1. Capable of inhibiting HIF1AN- dependent suppression of HIF1A activity.|
|Cellular Location||Cytoplasm. Note=Along actomyosin filaments and stress fibers|
|Tissue Location||Expressed in striated muscles, specifically in type 2a fibers (at protein level).|
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Provided below are standard protocols that you may find useful for product applications.
The major protein phosphatase-1 (PP1) is composed of 3 subunits with apparent molecular mass of 110-130, 37 & 20 kDa. The 110-130 kDa component acts as a regulatory subunit known as myosin binding (MBS) or myosin phosphatase targeting subunit (MYPT). The N-terminal portion of MYPT binds to both PP1c-delta and phosphorylated myosin, thereby increasing myosin phosphatase activity. Two isoforms of MYPT have been identified (MYPT1 & MYPT2) and share 61% sequence identity. While MYPT1 is widely distributed in human tissues, MYPT2 is mostly detected in brain and heart.
1. Alessi, D., MacDougall, L. K., Sola, M. M., Ikebe, M., and Cohen, P.(1992) Eur. J. Biochem. 210, 1023-1035
2. Fujioka, M.; Takahashi, N.; Odai, H.; Araki, S.; Ichikawa, K.;Feng, J.; Nakamura, M.; Kaibuchi, K.; Hartshorne, D. J.; Nakano, T.;Ito, M. Genomics 49: 59-68, 1998.
3. Hartshorne, D. J., Ito, M., and Erdodi, F. J. Muscle Res. Cell Motil. 19, 325-341, (1998)
4. Arimura T., Suematsu N., Zhou Y.-B., Nishimura J., Satoh S., Takeshita A., Kanaide H., Kimura A.; J. Biol. Chem. 276:6073-6082(2001).
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