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The protein encoded by PTPRS is a member of the protein tyrosine phosphatase (PTP) family. Additionally we are shipping PTPRS Antibodies (40) and PTPRS Kits (6) and many more products for this protein.
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Study identified several CpG sites and specifically several CpGs in the PTPRS and PER3 genes differentially methylated between obese and non-obese children, suggesting a role for DNA methylation (show HELLS Proteins) concerning development of childhood obesity.
interaction of receptor type of protein tyrosine phosphatase (show ACP1 Proteins) sigma (RPTPsigma) with a glycosaminoglycan library
Receptor protein tyrosine phosphatase (show PTPRT Proteins) sigma (RPTPsigma) regulates neuronal extension and acts as a presynaptic nexus for multiple protein and proteoglycan (show Vcan Proteins) interactions during synaptogenesis.
Data demonstrate that synoviocytes are regulated by an RPTPsigma-dependent proteoglycan (show Vcan Proteins) switch in vivo, which can be targeted for rheumatoid arthritis therapy.
represents an evolutionarily conserved pDC (show PNKD Proteins)-specific inhibitory receptor, and is required to prevent spontaneous IFN production and immune-mediated intestinal inflammation
crystallographic analyses of a shared HSPG-CSPG binding site reveal a conformational plasticity that can accommodat (show Vcan Proteins)e diverse glycosaminoglycans with comparable affinities; HS and analogs induced RPTPsigma ectodomain oligomerization which was inhibited by CS
Structural insights into the homology and differences between mouse protein tyrosine phosphatase (show ACP1 Proteins)-sigma and human protein tyrosine phosphatase (show ACP1 Proteins)-sigma.
Intragenic microdeletions of the EGFR (show EGFR Proteins) phosphatase PTPRS were found frequently (26%) in head and neck cancers, identifying this gene as a target of 19p13 loss.
Data show that PTPsigma localizes to PtdIns3P-positive membranes in cells, and this vesicular localization is enhanced during autophagy.
The receptor protein tyrosine phosphatase (show PTPRT Proteins) sigma (RPTPsigma) has now been identified as a receptor for inhibitory chondroitin sulfate proteoglycans.
These results demonstrate that NME2 associates with PTPsigma to elicit neurite outgrowth inhibition in response to chondroitin sulfate proteoglycans.
Receptor protein tyrosine phosphatase (show PTPRT Proteins) sigma (RPTPsigma) regulates neuronal extension and acts as a presynaptic nexus for multiple protein and proteoglycan (show Vcan Proteins) interactions during synaptogenesis
represents an evolutionarily conserved pDC (show PDC Proteins)-specific inhibitory receptor, and is required to prevent spontaneous IFN production and immune-mediated intestinal inflammation
PTPRS-deficient bone marrow cells display increased cobblestone area-forming cell capacity and augmented transendothelial migration capacity, which was abrogated by RAC (show AKT1 Proteins) inhibition.
the major binding sites for RPTPsigma in adult mouse brain are on neurons and are not proteoglycan (show Vcan Proteins) GAG chains, as RPTPsigma binding overlaps with the neuronal marker NeuN (show RBFOX3 Proteins) and was not altered by treatments which eliminate chondroitin or heparan sulfate.
Protein tyrosine phosphatase (show ACP1 Proteins) sigma targets apical junction complex proteins in the intestine and regulates epithelial permeability.
Ptprs and Ptprf (show PTPRF Proteins) deficiency affects mandibular cell proliferation.
The results of this study demonistrated that RPTPsigma limits synapse number and regulates synapse structure and function in the mature central nervous system.
The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP contains an extracellular region, a single transmembrane segment and two tandem intracytoplasmic catalytic domains, and thus represents a receptor-type PTP. The extracellular region of this protein is composed of multiple Ig-like and fibronectin type III-like domains. Studies of the similar gene in mice suggested that this PTP may be involved in cell-cell interaction, primary axonogenesis, and axon guidance during embryogenesis. This PTP has been also implicated in the molecular control of adult nerve repair. Four alternatively spliced transcript variants, which encode distinct proteins, have been reported.
, protein tyrosine phosphatase PTPsigma
, protein tyrosine phosphatase, receptor type, sigma
, receptor-type tyrosine-protein phosphatase S
, receptor-type tyrosine-protein phosphatase sigma
, Receptor-type tyrosine-protein phosphatase sigma
, tissue-specific protein tyrosine phosphatase
, leukocyte common antigen-related protein-tyrosine phosphatase 2
, leukocyte common antigen-related proten-tyrosine phosphatase 2
, protein tyrosine phosphatase, receptor type, D