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The protein encoded by PTPRN2 is a member of the protein tyrosine phosphatase (PTP) family. Additionally we are shipping Protein tyrosine Phosphatase, Receptor Type, N Polypeptide 2 Antibodies (60) and Protein tyrosine Phosphatase, Receptor Type, N Polypeptide 2 Kits (1) and many more products for this protein.
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Copy-number variations are enriched for PTPRN2 and other neurodevelopmental genes in children with developmental coordination disorder.
Haplotype-dependent allele-specific methylation of PTPRN2 gene is associated with neurological disorders.
Reduction in plasma membrane PI(4,5)P2 abundance by PTPRN2 and PLCbeta1 releases the PI(4,5)P2-binding protein cofilin from its inactive membrane-associated state into the cytoplasm where it mediates actin turnover dynamics.
Data indicate the X-ray structure of the mature ectodomain of mature ectodomain of phogrin/IA-2beta (PTPRN2) (ME phogrin) at pH 7.4 and 4.6.
ProPTPRN2 elicited these effects through direct interaction with TRAF2 (show TRAF2 Proteins).
While PTPRN2 shares sequence similarity with protein tyrosine phosphatases, this study in rat suggests that this protein instead functions as a membrane bound phosphatidylinositol phosphatase.
The findings in this patient raise the possibility that PTPRN2 may be active during early development of the human brainstem and that its overexpression may cause bilateral Duane retraction syndrome as occurs in patients with homozygous HOXA1 (show HOXA1 Proteins) mutations.
IA-2beta is involved in insulin (show INS Proteins) secretion, but despite its importance as a major autoantigen in human type 1 diabetes, it is not required for the development of diabetes in NOD mice.
In mice IA-2beta expressed exclusively in dense core secretory vesicles (DCV) and with fractions rich in synaptic vesicles (SV) of neuroendocrine cells of brain and impairment of conditioned learning.
The deletion of IA-2 (show PTPRN Proteins) and IA-2beta results in multiple pathophysiologic changes and represents a unique in vivo model for studying the effect of hormone and neurotransmitter reduction on known and still unrecognized targets.
Data show that miRNAs are involved in regulating the expression of the major type 1 diabetes (T1D) autoantigens IA-2 (show PTPRN Proteins), IA-2beta, and GAD65 (show GAD2 Proteins) enzyme.
Membrane-proximal ectodomain of phogrin was produced as a recombinant protein and characterized' results showed that it is a properly folded monomeric domain.
phogrin is recycled in Min6 beta-cells
analysis of a tyrosine-targeting motif for endocytosis and recycling of the dense-core vesicle membrane protein phogrin
experiments show that the dense core vesicle proteins IA-2 (show PTPRN Proteins) and IA-2beta, alone or in combination, are involved in insulin (show INS Proteins) secretion, but neither alone nor in combination are they required for the development of diabetes in NOD mice
IA-2beta, but not IA-2 (show PTPRN Proteins), is induced by ghrelin (show GHRL Proteins) and inhibits glucose-stimulated insulin (show INS Proteins) secretion
IA-2 (show PTPRN Proteins) and IA-2beta are dispensable for exocytosis of insulin (show INS Proteins) granules, but are probably more important for cargo loading and/or stability of dense core vesicles
Phogrin and IA-2 (show PTPRN Proteins) function as essential regulators of autocrine insulin (show INS Proteins) action in pancreatic beta-cells.
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 possesses an extracellular region, a single transmembrane region, and a single intracellular catalytic domain, and thus represents a receptor-type PTP. The catalytic domain of this PTP is most closely related to PTPRN/IA-2beta. This PTP and PTPRN are both found to be major autoantigens associated with insulin-dependent diabetes mellitus. Three alternatively spliced transcript variants of this gene, which encode distinct proteins, have been reported.
IAR/receptor-like protein-tyrosine phosphatase
, islet cell autoantigen-related protein
, protein tyrosine phosphatase receptor pi
, receptor-type tyrosine-protein phosphatase N2
, tyrosine phosphatase IA-2 beta
, IA-2 beta
, PTP IA-2beta
, protein tyrosine phosphatase-NP
, PTP NE-6
, protein tyrosine phosphatase receptor-type N polypeptide 2
, protein tyrosine phosphatase, receptor-type, N polypeptide 2