Weight | 1 lbs |
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Dimensions | 9 × 5 × 2 in |
accession | NP_001301026 |
express system | HEK293 |
product tag | C-hFc |
purity | > 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC |
background | Programmed cell death protein 1, also known as PD-1 and CD279, is a protein found on the surface of cells that has a role in regulating the immune system's response to the cells of the human body by down-regulating the immune system and promoting self tolerance by suppressing T cell inflammatory activity. |
molecular weight | The protein has a predicted MW of 43.00 kDa. Due to glycosylation, the protein migrates to 55-70 kDa based on Tris-Bis PAGE result. |
available size | 100 µg, 500 µg |
endotoxin | Less than 1EU per μg by the LAL method. |
Canine PD-1/PDCD1 Protein 2317
$315.00 – $1,050.00
Summary
- Expression: HEK293
- Functional: Yes (ELISA)
- Amino Acid Range: Leu25-Val170
Canine PD-1/PDCD1 Protein 2317
protein |
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Size and concentration 100, 500µg and lyophilized |
Form Lyophilized |
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles. |
Storage buffer Shipped at ambient temperature. |
Purity > 95% as determined by Tris-Bis PAGE |
target relevance |
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Programmed cell death protein 1, also known as PD-1 and CD279 , is a protein found on the surface of cells that has a role in regulating the immune system's response to the cells of the human body by down-regulating the immune system and promoting self tolerance by suppressing T cell inflammatory activity. |
Protein names Programmed cell death protein 1 (Protein PD-1) (hPD-1) (CD antigen CD279) |
Mass 31647Da |
Function Inhibitory receptor on antigen activated T-cells that plays a critical role in induction and maintenance of immune tolerance to self (PubMed:21276005). Delivers inhibitory signals upon binding to ligands CD274/PDCD1L1 and CD273/PDCD1LG2 (PubMed:21276005). Following T-cell receptor (TCR) engagement, PDCD1 associates with CD3-TCR in the immunological synapse and directly inhibits T-cell activation (By similarity). 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 (By similarity). {ECO:0000250|UniProtKB:Q02242, ECO:0000269|PubMed:21276005}.; 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). {ECO:0000269|PubMed:22658127, ECO:0000269|PubMed:25034862, ECO:0000269|PubMed:25399552, ECO:0000303|PubMed:28951311}. |
Subellular location Cell membrane {ECO:0000269|PubMed:30487606}; Single-pass type I membrane protein. |
Structure Monomer (PubMed:26602187). Interacts with CD274/PDCD1L1 (PubMed:26602187). Interacts with CD273/PDCD1LG2 (By similarity). Interacts with FBXO38; leading to ubiquitination and degradation of PDCD1 by the proteasome (PubMed:30487606). {ECO:0000250|UniProtKB:Q02242, ECO:0000269|PubMed:26602187, ECO:0000269|PubMed:30487606}. |
Post-translational modification 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). {ECO:0000269|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. {ECO:0000250|UniProtKB:Q02242}.; 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). {ECO:0000269|PubMed:28165004}. |
Target Relevance information above includes information from UniProt accession: Q15116 |
The UniProt Consortium |
Data
Publications
Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.pmid | title | authors | citation |
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Protocols
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Documents
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