Recombinant human PD1 protein (Biotin) (DDDDK tag C-Term + Avi tag C-Term + His tag C-Term)
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Recombinant human PD1 protein (Biotin) (DDDDK tag C-Term + Avi tag C-Term + His tag C-Term) is a Human Fragment protein, in the 25 to 167 aa range, expressed in HEK 293 cells, with >80%, suitable for SDS-PAGE, FuncS.
View Alternative Names
CD279, PD1, PDCD1, Programmed cell death protein 1, Protein PD-1, hPD-1
- FuncS
Unknown
Functional Studies - Recombinant human PD1 protein (Biotin) (DDDDK tag C-Term + Avi tag C-Term + His tag C-Term) (AB271670)
Binding activity of ab271670.
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant human PD1 protein (Biotin) (DDDDK tag C-Term + Avi tag C-Term + His tag C-Term) (AB271670)
SDS-PAGE analysis of ab271670.
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
Inhibitory receptor on antigen activated T-cells that plays a critical role in induction and maintenance of immune tolerance to self (PubMed : 21276005, PubMed : 31754127, PubMed : 32184441, PubMed : 37208329). Delivers inhibitory signals upon binding to ligands CD274/PDCD1L1 and CD273/PDCD1LG2 (PubMed : 21276005, PubMed : 26602187). Following T-cell receptor (TCR) engagement, PDCD1 associates with TCR-CD3 in the immunological synapse and directly inhibits T-cell activation (PubMed : 32184441). Suppresses T-cell activation through the recruitment of PTPN11/SHP-2 : following ligand-binding, PDCD1 is phosphorylated within the ITSM motif, leading to 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 (PubMed : 32184441).. The PDCD1-mediated inhibitory pathway is exploited by tumors to attenuate anti-tumor immunity and escape destruction by the immune system, thereby facilitating tumor survival (PubMed : 28951311). The interaction with CD274/PDCD1L1 inhibits cytotoxic T lymphocytes (CTLs) effector function (PubMed : 28951311). The blockage of the PDCD1-mediated pathway results in the reversal of the exhausted T-cell phenotype and the normalization of the anti-tumor response, providing a rationale for cancer immunotherapy (PubMed : 22658127, PubMed : 25034862, PubMed : 25399552).
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). Deubiquitinated and thus stabilized by USP5 (PubMed:37208329).. Tyrosine phosphorylated at Tyr-223 (within ITIM motif) and Tyr-248 (ITSM motif) upon ligand binding (PubMed:31754127, PubMed:32184441). Phosphorylation at Tyr-248 by FYN 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 (PubMed:32184441). Phosphorylation at Thr-234 promotes the recruitment of the deubiquitinase USP5 (PubMed:37208329).. 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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