Recombinant Human PD1 (mutated P130A) protein (Tagged) (Biotin)
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Recombinant Human PD1 (mutated P130A) protein (Tagged) (Biotin) is a Human Fragment protein, in the 25 to 167 aa range, expressed in HEK 293 cells, with >90%, suitable for SDS-PAGE.
View Alternative Names
CD279, PD1, PDCD1, Programmed cell death protein 1, Protein PD-1, hPD-1
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human PD1 (mutated P130A) protein (Tagged) (Biotin) (AB271662)
SDS-PAGE analysis of 2 μg ab271662.
This protein runs at a higher MW by SDS-PAGE due to glycosylation.
Reactivity data
Product details
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
PD1 serves as an inhibitory receptor acting as a checkpoint in the immune system. It becomes part of an immune-suppressive complex when it binds with its ligands PD-L1 or PD-L2 which are expressed on various cell types including some tumor cells. This interaction suppresses the proliferation of T cells and cytokine production contributing to immune homeostasis. By controlling T cell activity PD1 limits autoimmunity but can also reduce the immune system's capability to attack cancer cells.
Pathways
PD1 functions in the immune checkpoint pathway a critical regulatory circuit in immune regulation. The engagement of PD1 with its ligands initiates a cascade that inhibits the function and proliferation of T cells through downstream SHP-2 phosphatase activity. This pathway frequently involves other regulatory proteins like CTLA-4 and is an important mechanism by which the body modulates immune responses. Related pathways often intersect with those involving T cell receptor signaling and contribute to the overall modulation of immune activity.
Specifications
Form
Liquid
General info
Function
The protein expressed by the gene PDCD1 functions as an inhibitory receptor on antigen-activated T-cells, playing a critical role in the induction and maintenance of immune tolerance to self. It delivers inhibitory signals by binding to the ligands CD274/PDCD1L1 and CD273/PDCD1LG2. Tumors exploit the PDCD1-mediated inhibitory pathway to attenuate anti-tumor immunity, enabling tumor survival by evading immune system destruction. The interaction with CD274/PDCD1L1 inhibits the effector function of cytotoxic T lymphocytes (CTLs). Blocking the PDCD1-mediated pathway can reverse the exhausted T-cell phenotype and normalize the anti-tumor response, providing a rationale for cancer immunotherapy. This supplementary information is collated from multiple sources and compiled automatically.
Post-translational modifications
Ubiquitinated at Lys-233 by the SCF(FBXO38) complex, leading to its proteasomal degradation (PubMed:30487606). Ubiquitinated via 'Lys-48'-linked polyubiquitin chains (PubMed:30487606).. Tyrosine phosphorylated at Tyr-223 (within ITIM motif) and Tyr-248 (ITSM motif) upon ligand binding. Phosphorylation at Tyr-248 promotes the recruitment of the protein tyrosine phosphatase PTPN11/SHP-2 that mediates dephosphorylation of key TCR proximal signaling molecules, such as ZAP70, PRKCQ/PKCtheta and CD247/CD3zeta.. N-glycosylation at Asn-58 contains at least two N-acetylglucosamine units and one fucose (PubMed:28165004). N-glycosylation does not affect binding to nivolumab drug (PubMed:28165004).
Target data
Product promise
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