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The protein encoded by PTPRD is a member of the protein tyrosine phosphatase (PTP) family. Additionally we are shipping PTPRD Antibodies (30) and many more products for this protein.
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PTPRD was identified as a novel locus potentially associated with blood pressure response to atenolol and resistant hypertension in multiple ethnic groups.
PTPRD mutation, but not methylation or copy number loss, may serve as a predictive biomarker of sensitivity to STAT3 (show STAT3 Proteins) inhibitors in HNSCC.
Study shows for the first time that DNMT1 (show DNMT1 Proteins) caused PTPRD DNA hypermethylation and induced insulin (show INS Proteins) signaling silencing in T2D patients.
PTPRD is homozygously deleted and epigenetically downregulated in hepatocellular carcinomas (HCCs (show HCCS Proteins)).
This study demonstrated that the copy number variations of PTPRD relate to opioid dependence.
Silencing PTPRD expression by siRNA treatment significantly enhanced cell proliferation compared with mock siRNA treatment.
we report desmoplakin, a desmosomal protein that is implicated in cell-cell adhesion, as a novel PTPRD substrate.
Ptprd is a tumor suppressor that can promote tumorigenesis in concert with Cdkn2a loss.
The absence of MIM (show MTSS1 Proteins) led to PTPdelta-mediated activation of SRC (show SRC Proteins).
Periodic leg movements during sleep are associated with polymorphisms in BTBD9 (show BTBD9 Proteins), TOX3 (show TOX3 Proteins)/BC034767, MEIS1 (show MEIS1 Proteins), MAP2K5 (show MAP2K5 Proteins)/SKOR1, and PTPRD
Chondroitin Sulfate Proteoglycans Negatively Modulate Spinal Cord Neural Precursor Cells by Signaling Through LAR (show PTPRF Proteins) and RPTPsigma (show PTPRS Proteins) and Modulation of the Rho/ROCK Pathway.
We reveal that PTPRD is a bona fide tumor suppressor, pinpoint PTPRD loss as a cause of aberrant STAT3 activation in gliomas, and establish PTPRD loss, in the setting of CDKN2A/p16(INK4A) deletion, as a driver of glioma progression.
RPTP-sigma (show PTPRS Proteins) and RPTP-delta complement each other functionally during mammalian development, and reveal an essential contribution of RPTP-sigma (show PTPRS Proteins) and RPTP-delta to appropriate motoneuron axon targeting during mammalian axonogenesis.
Receptor protein tyrosine phosphatase (show PTPRT Proteins)-delta cooperates with hedgehog (show SHH Proteins)-responsive gene MIM (show MTSS1 Proteins) to induce cytoskeletal remodeling.
PTPRD may be one of a select group of tumor suppressor genes that are inactivated in a wide range of common tumor types.
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 three Ig-like and eight fibronectin type III-like domains. Studies of the similar genes in chicken and fly suggest the role of this PTP is in promoting neurite growth, and regulating neurons axon guidance. Multiple alternatively spliced transcript variants of this gene have been reported. A related pseudogene has been identified on chromosome 5.
, protein tyrosine phosphatase, receptor type, delta polypeptide
, protein-tyrosine phosphatase delta
, receptor-type tyrosine-protein phosphatase delta