抗Mouse (Murine) PPP1R12A 抗体:
抗Human PPP1R12A 抗体:
抗Rat (Rattus) PPP1R12A 抗体:
Human Polyclonal PPP1R12A Primary Antibody for ELISA, IHC - ABIN6255746
Xiaojun, Yan, Hong, Xianghong, Shifeng, Dingjie, Xuemin, Lijuan, Bonan, Zhongqiu, Ruimin, Brann, Fang: Acetylated α-Tubulin Regulated by N-Acetyl-Seryl-Aspartyl-Lysyl-Proline(Ac-SDKP) Exerts the Anti-fibrotic Effect in Rat Lung Fibrosis Induced by Silica. in Scientific reports 2018
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Human Polyclonal PPP1R12A Primary Antibody for IHC, WB - ABIN6712094
Zhou, Zhang, Li, Guo, Wang, Wang: Fasudil hydrochloride hydrate, a Rho-kinase inhibitor, suppresses high glucose-induced proliferation and collagen synthesis in rat cardiac fibroblasts. in Clinical and experimental pharmacology & physiology 2011
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Human Polyclonal PPP1R12A Primary Antibody for ELISA, WB - ABIN537186
Lutter, Barger, Nair, Hackstadt: Chlamydia trachomatis inclusion membrane protein CT228 recruits elements of the myosin phosphatase pathway to regulate release mechanisms. in Cell reports 2013
Human Polyclonal PPP1R12A Primary Antibody for IHC (p), WB - ABIN3043902
Yan, Wang, Jiang, Chen, He, Mang, Shao, Xu: The role of Rho/Rho-kinase pathway and the neuroprotective effects of fasudil in chronic cerebral ischemia. in Neural regeneration research 2015
The findings define the PI3K/NUAK1/MYPT1/MLCP axis as a critical pathway to regulate actomyosin contractility in endothelial cells, supporting vascular patterning and expansion through the control of cell rearrangement.
Mypt1 E24 splice variants tune arterial reactivity and could be worthy targets for lowering vascular resistance in disease states.
revealed the presence of two MYPT1 isoforms, full length and variant 2 in human intestinal (Caco-2) epithelial cells and isolated intestinal epithelial cells from mice
phosphorylation of MYPT1 T694, but not T852, mediates force maintenance in bladder smooth muscle.
Constitutive phosphorylation of myosin phosphatase targeting subunit-1 in smooth muscle
Maturation of mesenteric artery smooth muscle involves TRA2beta mediated Mypt1 exon 24 splicing.
The role of MYPT1 in vascular smooth muscle was investigated in adult MYPT1 smooth muscle specific knock-out mice. MYPT1 deletion enhanced phosphorylation of myosin regulatory light chain and contractile force in isolated mesenteric arteries.
MYPT1 is not essential for smooth muscle function in mice but regulates the Ca(2+) sensitivity of force development and contributes to intestinal phasic contractile phenotype.
Tra2beta, by regulating the splicing of Mypt1 E23, sets the sensitivity of smooth muscle to cGMP-mediated relaxation.
Organ-specific mechanisms involving MYPT1, M-RIP, and CPI-17 are critical to regulating basal LC20 phosphorylation in gastrointestinal smooth muscles.
Findings define a new conserved pathway in which sexual development and pregnancy mediate smooth and striated muscle adaptations through SMTNL1 and MYPT1.
a reduction in the protein level of MYPT1 (LZ+) is involved in nitrate tolerance; this may result in part from a proteasome-dependent degradation of MYPT1 (LZ+)
Stable transfection of HEK 293 cells with GFP-MYPT1 was obtained. MYPT1 and its N-terminal mutants bound to retinoblastoma protein (Rb), raising the possibility that Rb is implicated in the effects caused by overexpression of MYPT1.
Ca(2+)-independent relaxation by urocortin can be attributed to cAMP-mediated increased activity of SMPP-1M which is partly attributable to decrease in inhibitory phosphorylation of MYPT1.
Therefore, our results show that preservation of GLUT4 expression prevents enhanced arterial reactivity in hypertension, possibly via effects on myosin phosphatase activity.
both eEF1A and MYPT1 have roles in EGCG signaling for cancer prevention through 67LR
MYPT1 and CARM1 are substrates of OGT and function to alter OGT substrate specificity in vitro
MYPT1 knockdown by siRNAs reproduced miR-145 effects suggesting miR-145 as a tumor suppressor through MYPT1 targeting.
PP2A dephosphorylates MYPT1(pThr696) and thereby stimulates MP activity inducing dephosphorylation of eNOS(pThr497) and the 20 kDa myosin II light chains.
These results indicate shear stress induced vascular smooth muscle cell contraction was mediated by cell surface glycocalyx via a ROCK-MLC phosphatase (MLCP) pathway, providing evidence of the glycocalyx mechanotransduction in myogenic response.
he phosphorylation of the MP inhibitory MYPT1(T850) and the regulatory PRMT5(T80) residues as well as the symmetric dimethylation of H2A/4 were elevated in human hepatocellular carcinoma and in other types of cancers.
Results indicated that MYPT1 was down-regulated in GC tissues and cells, and is related to clinical stages and overall survival of GC. Functional research demonstrated that overexpression of MYPT1 can inhibit cell proliferation, cell cycle progression, and migration and invasion of GC cells.
Thus, Cyclin A/Cdk1 phosphorylation primes MYPT1 for Plk1 binding. These data demonstrate cross-regulation between Cyclin A/Cdk1-dependent and Plk1-dependent phosphorylation of substrates during mitosis to ensure efficient correction of kinetochore microtubule attachment errors necessary for high mitotic fidelity.
NO-induced cGMP signaling modulated RhoA/ROCK signaling in platelets, leading to the disinhibition of MLCP to control the phosphorylation of MLC and remodeling of platelet actin cytoskeleton.
The authors call the mutual sequestration mechanism through which pCPI-17 and myosin light-chain phosphatase interact inhibition by unfair competition: myosin light-chain phosphatase protects pCPI-17 from other phosphatases, while pCPI-17 blocks other substrates from the active site of myosin light-chain phosphatase.
Myosin light chain phosphatase (MLCP) is a master regulator of smooth muscle responsiveness to stimuli. (review)
BLT2 ligation facilitates F-actin assembly with the upregulated phosphorylation of MYPT1.
Lipolysis-stimulated lipoprotein receptors (LSRs) localized to bicellular junctions in association with myosin regulatory light chain 2 (MRLC2) at low cell densities and to tricellular contacts when myosin phosphatase target subunit 1 (MYPT1) localized to the bicellular regions.
miR-30d and/or its target gene MYPT1 may serve as novel prognostic markers of PCa. miR-30d promotes tumor angiogenesis of PCa through MYPT1/c-JUN/VEGFA pathway.
Study revealed the presence of two MYPT1 isoforms, full length and variant 2 in human intestinal (Caco-2) epithelial cells and isolated intestinal epithelial cells from mice.
These results indicate that PPP1R12A indeed plays a role in skeletal muscle insulin signaling
the relative expression of LZ+/LZ- MYPT1 isoforms, in part, defines the vascular response to NO and NO based vasodilators, and therefore, plays a role in the regulation of vascular tone in both health and disease
Expression of NUAK1 is controlled by cyclin-dependent kinase, PLK1, and the SCFbetaTrCP (Skp, Cullin and F-boxbetaTrCP) E3 ubiquitin ligase complex.
distinct roles of two inhibitory phosphorylation sites of MYPT1
in apoptotic cells, the myosin-binding domain of myosin phosphatase targeting subunit 1 is cleaved by caspase-3, and the cleaved MYPT1 is strongly phosphorylated at Thr-696 and Thr-853, phosphorylation of which is known to inhibit myosin II binding
results suggested that during atherosclerosis progression oxidative stress mediates the downregulation of MYPT1, which may inhibit smooth muscle cell migration and contribute to the aberrant contractility
Calcineurin may modulate the phosphorylation level of MLC20 by influencing the phosphorylation state of MYPT1 to regulate endothelial barrier function.
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 phosphorylation of MBS and MLC. Thus, Rho appears to inhibit myosin phosphatase through the action of Rho-kinase. Several transcript variants encoding different isoforms have been found for this gene.
myosin phosphatase target subunit 1
, myosin phosphatase, target subunit 1
, myosin phosphatase-targeting subunit 1
, protein phosphatase 1 regulatory subunit 12A
, myosin binding subunit
, protein phosphatase 1, regulatory (inhibitor) subunit 12A
, protein phosphatase myosin-binding subunit
, protein phosphatase subunit 1M
, serine/threonine protein phosphatase PP1 smooth muscle regulatory subunit M110
, smooth muscle myosin phosphatase myosin-binding subunit
, 130 kDa myosin-binding subunit of smooth muscle myosin phophatase
, 130 kDa myosin-binding subunit of smooth muscle myosin phosphatase
, 133kDa myosin-binding subunit of smooth muscle myosin phosphatase (M133)
, PP1M subunit M110