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Human Polyclonal PCMT1 Primary Antibody pour ICC, IF - ABIN4344090
Forsström, Axnäs, Stengele, Bühler, Albert, Richmond, Hu, Nilsson, Hudson, Rockberg, Uhlen: Proteome-wide epitope mapping of antibodies using ultra-dense peptide arrays. dans Molecular & cellular proteomics : MCP 2014
High expression of PCMT1 is associated with pancreatic cancer.
The new findings reported here extend the list of human PIMT variants that may contribute to neurological diseases in the young and the decline of CNS function in the aged.
decrease of PCMT1 significantly increased the proportion of D-Asp residues in PHB1 and had significant and fatal impacts on morphology and functions of the mitochondria, such as ATP production and the mitochondrial fusion-fission system
PIMT heterozygosity for R36C, G175R, R17H, or R17S would be detrimental to successful aging, whereas homozygosity (should it ever occur) would produce devastating neuropathology
Strong PIMT expression was a predictive marker of poor prognosis for surgically resected lung adenocarcinoma.
The data of this study indicated that DA-associated PIMT downregulation is an important event contributing to neuronal cell death
ERK2-mediated phosphorylation of transcriptional coactivator binding protein PIMT/NCoA6IP at Ser298 augments hepatic gluconeogenesis.
Overexpression of PCMT1 attentuates Mst1 kinase activation and its apoptotic effects in response to hypoxia-induced injury in cardiomyocytes.
Data indicate that human PROTEIN ISOASPARTYL METHYLTRANSFERASE (PIMT) can initiate isoAsp conversion to Asp, and is able to restore Arabidopsis PRH75's complex biochemical activity provided isoAsp formation has not led to conformational alterations.
Data show six differentially expressed proteins were identified as HSP70, PPIA and alpha-Enolase (up-regulated) S100-A9, PIMT and beta-5 tubulin (down-regulated), most of which had been shown to play a potential role in the pathogenesis of atherosclerosis.
The results implied that maternal polymorphisms in PCMT1 might be a potential genetic risk factor for isolated anencephaly in the Chinese population of Lvliang.
Study provides new insight into the molecular mechanisms by which PIMT suppresses the p53 activity through carboxyl methylation, and suggests a therapeutic target for cancers.
PIMT may act as a co-activator in ERalpha-mediated transcription of TFF1 through its recruitment to the promoter via interacting with ERalpha.
A tight cross-regulation exists between ERK and PIMT in regards to their activation and expression during the epithelial mesenchymal transition.
study demonstrates a novel role for PIMT as a negative regulator of Abeta peptide formation and a potential protective factor in the pathogenesis of Alzheimer disease
This protein has been found differentially expressed in thalami from patients with schizophrenia.
Protein L-Isoaspartyl Methyltransferase
crystal structure complexed with adenosyl homocysteine (AdoHcy) to 1.6-A resolution
Our results showed that the Ile120Val polymorphism of PCMT1 gene is a genetic modifier for the risk of spina bifida. Val/Val genotype was associated with a reduction in risk for spina bifida.
A potential role for PIMT in biological processes such as wound healing, cell migration, and tumor metastasis dissemination.
Loss of normal CKB structure and function contributes to the mechanisms by which isoaspartate accumulation leads to central nervous system dysfunction in the PIMT-Knockout mouse.
PIMT levels may significantly influence the course of age-related central nervous system dysfunction.
PIMT knockout mice have perturbations in glutamate metabolism in the brain and die prematurely of epileptic seizures.
synuclein is not a major target of PIMT in vivo
Altered levels of S-adenosylmethionine and S-adenosylhomocysteine in the brains of PCMT1 knockout mice
Recombinant adeno-PIMT improved the symptoms of PIMT-deficient mice in vivo, but only partially repaired IsoAsp in damaged proteins.
An accumulation of isoaspartyl residues in cells of mice lacking the isoaspartyl repair enzyme PCMT alters the effector function of T lymphocytes leading to autoantibody production.
Pcmt1-/- mice have altered regulation of the insulin pathway, possibly as a compensatory response to altered glucose uptake or metabolism or as an adaptive response to a general accumulation of isoaspartyl protein damage in the brain and other tissues.
Protein L-isoaspartyl methyltransferase (PIMT) catalyzes in vivo racemization of Asp-25 in mammalian histone H2B, suggesting that PIMT functions in the repair, rather than the metabolic turnover, of isoaspartyl proteins in vivo.
Pcmt1-/- mice have an increased number of granule cells in the granule cell layer and hilus of the dentate gyrus.
Synapsin I is a major endogenous substrate for Pcmt1 in the mouse brain.
PIMT-KO phenotype results from the cumulative effect of isoaspartate-related damage to a number of the neuron-rich proteins detected in this study
This gene encodes a member of the type II class of protein carboxyl methyltransferase enzymes. The encoded enzyme plays a role in protein repair by recognizing and converting D-aspartyl and L-isoaspartyl residues resulting from spontaneous deamidation back to the normal L-aspartyl form. The encoded protein may play a protective role in the pathogenesis of Alzheimer's disease, and single nucleotide polymorphisms in this gene have been associated with spina bifida and premature ovarian failure. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene.
L-isoaspartyl protein carboxyl methyltransferase
, protein L-isoaspartyl/D-aspartyl methyltransferase
, protein-L-isoaspartate(D-aspartate) O-methyltransferase
, protein-beta-aspartate methyltransferase
, protein carboxyl methyltransferase
, protein carboxyl-o-methyltransferase
, protein-L-isoaspartate (D-aspartate) O-methyltransferase 1
, Protein L-isoaspartyl/D-aspartyl methyltransferase
, Protein-beta-aspartate methyltransferase
, l-isoaspartyl protein carboxyl methyltransferase