Recombinant Human PILRA protein (GST tag N-Terminus)
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Recombinant Human PILRA protein (GST tag N-Terminus) is a Human Full Length protein, in the 1 to 226 aa range, expressed in Wheat germ, suitable for ELISA, WB.
대체 명칭 보기
Paired immunoglobulin-like type 2 receptor alpha, Cell surface receptor FDF03, Inhibitory receptor PILR-alpha, PILRA
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human PILRA protein (GST tag N-Terminus) (AB162304)
ab162304 on a 12.5% SDS-PAGE stained with Coomassie Blue.
Reactivity 정보
서열 정보
특성 및 보관 정보
제형
Purification 테크닉
배송 시 보관 조건
적절한 단기 보관 조건
적절한 장기 보관 조건
분주 정보
보관 정보
추가 정보
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
PILRA plays a significant role in the immune system regulation by inhibiting cellular activation processes. This regulation occurs through its participation in receptor-ligand interactions that modulate the immune response. It is not part of a complex but its pair PILRB acts as an activating receptor providing a balanced modulation of immune signaling. The balance between PILRA and PILRB affects how immune cells respond to various signals.
Pathways
PILRA is centrally involved in immune response pathways especially those controlling immune cell signaling. It interacts with proteins involved in immune system pathways such as LILRB1 which also mediates inhibitory signaling. PILRA functions in signaling pathways to regulate the activation and inhibition of immune responses maintaining immune system homeostasis.
일반 정보
기능
Paired receptors consist of highly related activating and inhibitory receptors and are widely involved in the regulation of the immune system. PILRA is thought to act as a cellular signaling inhibitory receptor by recruiting cytoplasmic phosphatases like PTPN6/SHP-1 and PTPN11/SHP-2 via their SH2 domains that block signal transduction through dephosphorylation of signaling molecules. Receptor for PIANP.. (Microbial infection) Acts as an entry co-receptor for herpes simplex virus 1.
Post-translational modifications
According to PubMed:10660620, N- and O-glycosylated. According to PubMed:10903717, only N-glycosylated.. Phosphorylated on tyrosine residues.
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