anti- PTPRS antibody

Este producto es parte de PTPR - protein tyrosine phosphatase receptor type
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935106861
info@markelab.com
name
anti- PTPRS antibody
category
Primary Antibodies
provider
FineTest
reference
FNab06948
tested applications
ELISA, WB, IHC, IP, FC

Description

Type II a receptor protein tyrosine phosphatases (rPTPσ) are cell surface receptors important for nervous system development, function, and repair.The expression of rPTPσ has previously been reported in b-cells and other target organs for INS although the probes chosen did not permit to distinguish between the splice variants.Proteolytic processing near the transmembrane domain generates an extracellular N-terminal E-domain of 130 kDa and a C-terminal P-domain of approximately 85 kDa of rPTPσ,and the short splice variants rPTPσ 3 and 4 contain an E-domain of 95 kDa (PMID: 16552719). rPTPσ expression was observed in tissue lysates of the adult mouse sensory-motor cortex and thoracic spinal cord (T8-T10) as a 75-80kDa immunoreactive band (PMID: 19780196).

Documents del producto

Instrucciones
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Data sheet

Product specifications

Category
Primary Antibodies
Immunogen Target
protein tyrosine phosphatase, receptor type, S
Host
Rabbit
Reactivity
human,mouse,rat
Recommended Dilution
WB: 1:200-1:2000; IP: 1:200-1:1000; IHC: 1:20-1:200
Clonality
polyclonal
Conjugation
Unconjugated
Isotype
IgG
Observed MW
75-100 kDa
Purity
≥95% as determined by SDS-PAGE
Purification
Immunogen affinity purified
Size 1
100µg
Form
liquid
Tested Applications
ELISA, WB, IHC, IP, FC
Storage
PBS with 0.02% sodium azide and 50% glycerol pH 7.3,-20℃ for 12 months(Avoid repeated freeze / thaw cycles.)
UniProt ID
Q13332
Gene ID
5802
Alias
R-PTP-S,PTPSIGMA,R-PTP-sigma,Receptor-type tyrosine-protein phosphatase sigma,Receptor-type tyrosine-protein phosphatase S
Background
Antibody anti-PTPRS
Status
RUO
Note
This product is for research use only.

Descripción

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.

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Type II a receptor protein tyrosine phosphatases (rPTPσ) are cell surface receptors important for nervous system development, function, and repair.The expression of rPTPσ has previously been reported in b-cells and other target organs for INS although the probes chosen did not permit to distinguish between the splice variants.Proteolytic processing near the transmembrane domain generates an extracellular N-terminal E-domain of 130 kDa and a C-terminal P-domain of approximately 85 kDa of rPTPσ,and the short splice variants rPTPσ 3 and 4 contain an E-domain of 95 kDa (PMID: 16552719). rPTPσ expression was observed in tissue lysates of the adult mouse sensory-motor cortex and thoracic spinal cord (T8-T10) as a 75-80kDa immunoreactive band (PMID: 19780196).

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