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The protein encoded by PTPRH is a member of the protein tyrosine phosphatase (PTP) family. Zusätzlich bieten wir Ihnen PTPRH Antikörper (29) und PTPRH Kits (11) und viele weitere Produktgruppen zu diesem Protein an.
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The results indicate that PTPRH is downregulated in colorectal tumors and its expression is epigenetically regulated via DNA methylation (zeige HELLS Proteine) and chromatin modifications.
PTPRH is overexpressed in non-small cell lung cancer, is regulated by DNA hypomethylation, and PTPRH DNA methylation (zeige HELLS Proteine) was an independent prognostic factor
SAP-1 (zeige ELK4 Proteine) induces apoptotic cell death by inhibition of cell survival signaling mediated by PI 3 (zeige PI3 Proteine)-kinase, Akt (zeige AKT1 Proteine), and ILK (zeige ILK Proteine) and activation of a caspase (zeige CASP3 Proteine)-dependent proapoptotic pathway.
SAP-1 (zeige ELK4 Proteine) expression is downregulated during the dedifferentiation of human hepatocellular carcinoma, which may play a causal role in disease progression
The results of this study suggest the partial contribution of SAP-1 (zeige ELK4 Proteine) to the regulated transport of hydrophilic macromolecules through paracellular tight junctions.
SAP-1 and CEACAM20 thus constitute a regulatory system through which the intestinal epithelium contributes to intestinal immunity.
These results thus suggest that SAP-1 (zeige ELK4 Proteine) is a microvillus-specific receptor-type protein tyrosine phosphatase (zeige ACP1 Proteine) that regulates intestinal tumorigenesis.
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 intracytoplasmic catalytic domain, and thus represents a receptor-type PTP. The extracellular region contains eight fibronectin type III-like repeats and multiple N-glycosylation sites. The gene was shown to be expressed primarily in brain and liver, and at a lower level in heart and stomach. It was also found to be expressed in several cancer cell lines, but not in the corresponding normal tissues. Alternative splicing results in multiple transcript variants.
, receptor-type tyrosine-protein phosphatase H
, stomach cancer-associated protein tyrosine phosphatase 1
, transmembrane-type protein-tyrosine phosphatase type H
, receptor type protein tyrosine phosphatase sap-1
, brain-enriched membrane-associated protein tyrosine BEM-2