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CTDSP1 encodes a member of the small C-terminal domain phosphatase (SCP) family of nuclear phosphatases. Additionally we are shipping CTDSP1 Proteins (7) and CTDSP1 Kits (4) and many more products for this protein.
Showing 10 out of 108 products:
Human Polyclonal CTDSP1 Primary Antibody for IHC (p), ELISA - ABIN545075
Yeo, Lin, Dahmus, Gill: A novel RNA polymerase II C-terminal domain phosphatase that preferentially dephosphorylates serine 5. in The Journal of biological chemistry 2003
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Dog (Canine) Polyclonal CTDSP1 Primary Antibody for ELISA - ABIN451599
Zhang, Kim, Genoud, Gao, Kelly, Pfaff, Gill, Dixon, Noel: Determinants for dephosphorylation of the RNA polymerase II C-terminal domain by Scp1. in Molecular cell 2006
Our results provide a novel mechanistic insight into the activation of Myc by 27-HC via transcriptional repression of PP2A, SCP1 and FBW7 to increase Myc protein stability in breast cancer cells.
SCP1 is the phosphatase that counterregulates the MAPK-mediated phosphorylation of Ser(68)-Twist1.
SCP1 regulates c-Myc stability and functions through dephosphorylating c-Myc Serine-62.
hSCP1 may be an beta-O-linked N-acetylglucosamine modified protein in vivo.
CTDSP1 activity stabilizes REST in stem cells and ERK-dependent phosphorylation combined with Pin1 activity promotes REST degradation in neural progenitors.
SCP1 phosphatase substrate specificity: CdcA3 could be an enzymatic substrate for SCP1.
Captured the phosphoryl-aspartate intermediate in the crystal structure of a Scp1D206A mutant soaked with para-nitrophenyl phosphate (pNPP), providing strong evidence for the proposed mechanism.
Polymorphisms vary significantly between races; Not associated with TB susceptibility in Caucasians.
SCP1 may play a role in the regulation of gene expression, possibly by controlling the transition from initiation/capping to processive transcript elongation
results show that REST/NRSF recruits SCPs to neuronal genes that contain RE-1 elements, leading to neuronal gene silencing in non-neuronal cells
SCP1 acts as a phosphatase for regulatory phosphorylations in the linker region of Smad1 and Smad2.
Consistently, the authors observed increased AKT phosphorylation and angiogenesis followed by enhanced tumorigenesis in Ctdsp1 (which encodes SCP1) gene - knockout mice. Importantly, they discovered that the membrane localization of SCP1 is crucial for impeding angiogenesis and tumor growth, and this localization depends on palmitoylation of a conserved cysteine motif within its NH2 terminus.
Golli-BG21 enhanced SCP1/GIP phosphatase activity, whereas PKCalpha-phosphorylated BG21 inhibited its activity, suggesting a potential role of BG21 as a molecular switch ("quick-brake mechanism") on SCP1/GIP.
Findings suggest that SCP1 may inhibit the osteoblastic differentiation induced by the BMP-Smad axis via Runx2 by suppressing downstream effector(s).
Expression and purification of the active variant of recombinant murine Golli-interacting protein (GIP) and its characterization
This gene encodes a member of the small C-terminal domain phosphatase (SCP) family of nuclear phosphatases. These proteins play a role in transcriptional regulation through specific dephosphorylation of phosphoserine 5 within tandem heptapeptide repeats of the C-terminal domain of RNA polymerase II. The encoded protein plays a role in neuronal gene silencing in non-neuronal cells, and may also inhibit osteoblast differentiation. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene.
carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 1
, CTD (carboxy-terminal domain, RNA polymerase II, polypeptide A) small phosphatase 1
, NLI-interacting factor 3
, nuclear LIM interactor-interacting factor 3
, small C-terminal domain phosphatase 1
, golli-interacting protein
, small CTD phosphatase 1