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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 (35) and PTPRS Proteins (12) and many more products for this protein.
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Receptor protein tyrosine phosphatase (show PTPRT ELISA Kits) sigma (RPTPsigma) regulates neuronal extension and acts as a presynaptic nexus for multiple protein and proteoglycan (show Vcan ELISA Kits) interactions during synaptogenesis.
Data demonstrate that synoviocytes are regulated by an RPTPsigma-dependent proteoglycan (show Vcan ELISA Kits) switch in vivo, which can be targeted for rheumatoid arthritis therapy.
represents an evolutionarily conserved pDC (show PNKD ELISA Kits)-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 ELISA Kits)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 ELISA Kits)-sigma and human protein tyrosine phosphatase (show ACP1 ELISA Kits)-sigma.
Intragenic microdeletions of the EGFR (show EGFR ELISA Kits) 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 ELISA Kits) sigma (RPTPsigma) has now been identified as a receptor for inhibitory chondroitin sulfate proteoglycans.
Trans-synaptic adhesions between netrin-G ligand-3 (NGL-3 (show LRRC4B ELISA Kits)) and receptor tyrosine phosphatases LAR (show PTPRF ELISA Kits), protein-tyrosine phosphatase delta (show PTPRD ELISA Kits) (PTPdelta), and PTPsigma via specific domains regulate excitatory synapse formation.
interactions between RPTP-domain1s and RPTP-domain 2s are a common but specific mechanism that is likely to be regulated- domain2s and the wedge structures are crucial determinants of binding specificity, thus regulating cross-talk between RPTPs
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 ELISA Kits) sigma (RPTPsigma) regulates neuronal extension and acts as a presynaptic nexus for multiple protein and proteoglycan (show Vcan ELISA Kits) interactions during synaptogenesis
represents an evolutionarily conserved pDC (show PDC ELISA Kits)-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 ELISA Kits) inhibition.
the major binding sites for RPTPsigma in adult mouse brain are on neurons and are not proteoglycan (show Vcan ELISA Kits) GAG chains, as RPTPsigma binding overlaps with the neuronal marker NeuN (show RBFOX3 ELISA Kits) and was not altered by treatments which eliminate chondroitin or heparan sulfate.
Protein tyrosine phosphatase (show ACP1 ELISA Kits) sigma targets apical junction complex proteins in the intestine and regulates epithelial permeability.
Ptprs and Ptprf (show PTPRF ELISA Kits) 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