Human Protein Tyrosine Phosphatase Receptor Type S (PTPRS) CLIA Kit

Human Protein Tyrosine Phosphatase Receptor Type S (PTPRS) CLIA Kit es un kit CLIA tipo Sandwich para la detección de homogeizados de tejido, lisados celulares y otros fluidos biológicos.

Background

PTPRS is a receptor-type protein tyrosine phosphatase critical for neuronal development, axonal growth, and immune system function. Structurally, PTPRS consists of an extracellular domain containing multiple immunoglobulin (Ig)-like domains and fibronectin type III repeats, a single transmembrane segment, and two intracellular phosphatase domains, of which the first domain is catalytically active. PTPRS is primarily expressed in the nervous system and immune cells. It plays an essential role in the development and maintenance of synapses, particularly by modulating axon guidance through its interaction with ligands such as chondroitin sulfate proteoglycans (CSPGs) and contactin. PTPRS regulates signaling pathways by dephosphorylating key substrates like the tyrosine kinases and adhesion molecules, influencing cellular growth, differentiation, and repair. In the immune system, PTPRS is implicated in modulating immune responses, including T cell activation and signaling pathways involved in inflammation. Genetic polymorphisms and mutations in PTPRS have been linked to neurodevelopmental disorders, such as autism spectrum disorders (ASD) and schizophrenia, as well as immune dysfunctions. In cancer biology, PTPRS is increasingly recognized as a tumor suppressor, with its inactivation contributing to oncogenic signaling and tumor progression in cancers like colorectal and breast cancer. Its loss leads to increased activation of receptor tyrosine kinases (RTKs) and oncogenic signaling pathways, promoting uncontrolled cell proliferation. This highlights PTPRS as a potential therapeutic target in both neurological recovery and cancer treatment. Overall, PTPRS is a multifunctional phosphatase with pivotal roles in axonal repair, immune regulation, and tumor suppression, making it a critical protein in diverse biological processes.