PPP1R12A 抗体 (pSer668)
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Quick Overview for PPP1R12A 抗体 (pSer668) (ABIN8123156)
抗原
See all PPP1R12A 抗体适用
宿主
克隆类型
标记
应用范围
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抗原表位
- pSer668
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原理
- MYPT1 (Phospho Ser668) Antibody
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特异性
- This antibody detects endogenous levels of Human MYPT1 (phospho-Ser668)
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纯化方法
- The antibody was affinity-purified from rabbit serum by affinity-chromatography using specific immunogen.
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免疫原
- Synthesized phosho peptide around human MYPT1 (Ser668)
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亚型
- IgG
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应用备注
- WB 1:500-2000,IHC 1:50-300, ELISA 2000-20000
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限制
- 仅限研究用
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状态
- Liquid
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缓冲液
- Liquid in PBS containing 50 % glycerol, 0.5 % BSA and 0.02 % sodium azide.
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储存液
- Sodium azide
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注意事项
- This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
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储存条件
- -20 °C
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储存方法
- Store at -20°C/1 year
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有效期
- 12 months
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- PPP1R12A (Myosin Phosphatase, Target Subunit 1 (PPP1R12A))
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别名
- MYPT1
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背景
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Synonyms: Protein phosphatase 1 regulatory subunit 12A (Myosin phosphatase-targeting subunit 1) (Myosin phosphatase target subunit 1) (Protein phosphatase myosin-binding subunit)
Background: Myosin phosphatase target subunit 1, which is also called the myosin-binding subunit of myosin phosphatase, is one of the subunits of myosin phosphatase. Myosin phosphatase regulates the interaction of actin and myosin downstream of the guanosine triphosphatase Rho. The small guanosine triphosphatase Rho is implicated in myosin light chain (MLC) phosphorylation, which results in contraction of smooth muscle and interaction of actin and myosin in nonmuscle cells. The guanosine triphosphate (GTP)-bound, active form of RhoA (GTP.RhoA) specifically interacted with the myosin-binding subunit (MBS) of myosin phosphatase, which regulates the extent of phosphorylation of MLC. Rho-associated kinase (Rho-kinase), which is activated by GTP. RhoA, phosphorylated MBS and consequently inactivated myosin phosphatase. Overexpression of RhoA or activated RhoA in NIH 3T3 cells increased phosph
Gene Name: PPP1R12A MBS MYPT1
Protein Name: MYPT1 (Ser668)
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基因ID
- 4659
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UniProt
- O14974
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途径
- M Phase
抗原
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