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Phospho-MYPT1 (Thr696) Antibody

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品牌：CST/賽信通

貨號(hào)：5163T

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商品名稱	規(guī)格	代理級(jí)別	價(jià)格	運(yùn)費(fèi)	供應(yīng)商	購(gòu)買
CST 5163T Phospho-MYPT1(Thr696) Antibody 交貨周期:部分現(xiàn)貨，期貨3-4周左右，優(yōu)質(zhì)售后	20μl	經(jīng)銷	登錄可見(jiàn)	-	上海優(yōu)寧維生物科技股份有限公司	- + 立即購(gòu)買庫(kù)存：999

產(chǎn)品詳情

文獻(xiàn)引用

文獻(xiàn)圖片

實(shí)驗(yàn)數(shù)據(jù)

應(yīng)用：W
Protein phosphatase 1 (PP1) is a ubiquitous eukaryotic protein serine/threonine phosphatase involved in the regulation of various cell functions. Substrate specificity is determined by the binding of a regulatory subunit to the PP1 catalytic subunit (PP1c). It is estimated that over fifty different regulatory subunits exist (1).The myosin phosphatase holoenzyme is composed of three subunits: PP1c, a targeting/regulatory subunit (MYPT/myosin-binding subunit of myosin phosphatase), and a 20 kDa subunit of unknown function (M20). MYPT binding to PP1cdelta alters the conformation of the catalytic cleft and increases enzyme activity and specificity (2). Two MYPT isoforms that are 61% identical have been described. MYPT1 is widely expressed, while MYPT2 expression appears to be exclusive to heart and brain (3). Related family members include MBS85, MYPT3, and TIMAP (4).Myosin phosphatase regulates the interaction of actin and myosin in response to signaling through the small GTPase Rho. Rho activity inhibits myosin phosphatase via Rho-associated kinase (ROCK). Phosphorylation of MYPT1 at Thr696 and Thr853 results in phosphatase inhibition and cytoskeletal reorganization (5,6).

Supporting Data

REACTIVITY	H M R Mk
SENSITIVITY	Endogenous
MW (kDa)	140
SOURCE	Rabbit

Application Key:

W-Western
IP-Immunoprecipitation
IHC-Immunohistochemistry
ChIP-Chromatin Immunoprecipitation
IF-Immunofluorescence
F-Flow Cytometry
E-P-ELISA-Peptide

Species Cross-Reactivity Key:

H-Human
M-Mouse
R-Rat
Hm-Hamster
Mk-Monkey
Vir-Virus
Mi-Mink
C-Chicken
Dm-D. melanogaster
X-Xenopus
Z-Zebrafish
B-Bovine
Dg-Dog
Pg-Pig
Sc-S. cerevisiae
Ce-C. elegans
Hr-Horse
All-All Species Expected

Product Usage Information

Application	Dilution
Western Blotting	1:1000

Storage

Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 μg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.

Specificity / Sensitivity

Phospho-MYPT1 (Thr696) Antibody detects endogenous levels of MYPT1 only when phosphorylated at Thr696. The antibody may cross-react with the phospho-MYPT2 (Thr 646) due to high sequence homology.

Species Reactivity:

Human, Mouse, Rat, Monkey

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surroundiing Thr696 of human MYPT1. Antibodies are purified using protein A and peptide affinity chromatography.

Background

Protein phosphatase 1 (PP1) is a ubiquitous eukaryotic protein serine/threonine phosphatase involved in the regulation of various cell functions. Substrate specificity is determined by the binding of a regulatory subunit to the PP1 catalytic subunit (PP1c). It is estimated that over fifty different regulatory subunits exist (1).

The myosin phosphatase holoenzyme is composed of three subunits: PP1c, a targeting/regulatory subunit (MYPT/myosin-binding subunit of myosin phosphatase), and a 20 kDa subunit of unknown function (M20). MYPT binding to PP1cδ alters the conformation of the catalytic cleft and increases enzyme activity and specificity (2). Two MYPT isoforms that are 61% identical have been described. MYPT1 is widely expressed, while MYPT2 expression appears to be exclusive to heart and brain (3). Related family members include MBS85, MYPT3, and TIMAP (4).

Myosin phosphatase regulates the interaction of actin and myosin in response to signaling through the small GTPase Rho. Rho activity inhibits myosin phosphatase via Rho-associated kinase (ROCK). Phosphorylation of MYPT1 at Thr696 and Thr853 results in phosphatase inhibition and cytoskeletal reorganization (5,6).

Cohen, P.T. (2002) J Cell Sci 115, 241-56.
Terrak, M. et al. (2004) Nature 429, 780-4.
Fujioka, M. et al. (1998) Genomics 49, 59-68.
Ito, M. et al. (2004) Mol Cell Biochem 259, 197-209.
Birukova, A.A. et al. (2004) Microvasc Res 67, 64-77.
Birukova, A.A. et al. (2004) J Cell Physiol 201, 55-70.