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Western blot analysis of MYPT1 on a rat cerebrum lysate. Lane 1: 1:500, lane 2: 1:1000, lane 3: 1:2000 dilution of the mouse anti-MYPT1 antibody.
BD Transduction Laboratories™ Purified Mouse Anti-MYPT1
Regulatory Statusの凡例
Any use of products other than the permitted use without the express written authorization of Becton, Dickinson and Company is strictly prohibited.
Preparation and Storage
推奨アッセイ手順
Western blot: Please refer to http://www.bdbiosciences.com/pharmingen/protocols/Western_Blotting.shtml
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
- Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
- Source of all serum proteins is from USDA inspected abattoirs located in the United States.
Protein phosphatase-1 (PP1) is a major serine/threonine phosphatase that is involved in various cellular processes in eukaryotic cells. The PP1 catalytic subunit may be directed to particular subcellular locations by targeting subunits, which can modify the substrate specificity of the enzyme. The PP1 enzyme associated with the myofibrils of striated and smooth muscle forms a complex with Myosin Phosphatase Targeting subunit 1 (MYPT1). MYPT1 contains seven ankyrin repeats in the N-terminal region, and a leucine zipper (LZ) motif in the C-terminus. Alternative splicing of the MYPT1 mRNA leads to expression of a truncated MYPT1 that lacks the leucine zipper region. The expression of MYPT1 splice variants correlate with a smooth muscle phenotype. In the tonic contracting chicken aorta, only the full length MYPT1 is expressed, while in the phasic contracting chicken gizzard, only the truncated MYPT1 is expressed. The leucine zipper motif may be required for association with cGMP-dependent protein kinase I. Thus, MYPT1 may direct not only PP1 enzymatic activity toward myosin, but also may regulate the cGMP responsiveness of PP1 through expression of alternative splice variants.
Development References (3)
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Chen YH, Chen MX, Alessi DR. Molecular cloning of cDNA encoding the 110 kDa and 21 kDa regulatory subunits of smooth muscle protein phosphatase 1M. FEBS Lett. 1994; 356(1):51-55. (Biology). View Reference
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Khatri JJ, Joyce KM, Brozovich FV, Fisher SA. Role of myosin phosphatase isoforms in cGMP-mediated smooth muscle relaxation. J Biol Chem. 2001; 276(40):27250-27257. (Biology). View Reference
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Kimura K, Ito M, Amano M. Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho-kinase). Science. 1996; 273(5272):245-248. (Biology). View Reference
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Comparisons, where applicable, are made against older BD Technology, manual methods or are general performance claims. Comparisons are not made against non-BD technologies, unless otherwise noted.
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