Human PD1/PDCD1/CD279 (His Tag) recombinant protein
Programmed cell death 1, also known as PDCD1, is a type I transmembrane glycoprotein, and is an immunoreceptor belonging to the CD28/CTLA-4 family negatively regulates antigen receptor signaling by recruiting protein tyrosine phosphatase, SHP-2 upon interacting with either of two ligands, PD-L1 or PD-L2. PD1 inhibits the T-cell proliferation and production of related cytokines including IL-1, IL-4, IL-10 and IFN-γ by suppressing the activation and transduction of PI3K/AKT pathway. In addition, coligation of PD1 inhibits BCR-mediating signal by dephosphorylating key signal transducer. PD1 has been suggested to be involved in lymphocyte clonal selection and peripheral tolerance, and thus contributes to the prevention of autoimmune diseases. Furthermore, PD1 is shown to be a regulator of virus-specific CD8+ T cell survival in HIV infection. As a cell surface molecule, PDCD1 regulates the adaptive immune response. Engagement of PD-1 by its ligands PD-L1 or PD-L2 transduces a signal that inhibits T-cell proliferation, cytokine production, and cytolytic function.
Programmed cell death protein 1
Protein short names
SLEB2; LY101; PDCD1; CD279; HPD-1; PDC1; HPD-L; PD-1; PD1
A DNA sequence encoding the extracellular domain (Met 1-Gln 167) of human PD1 (NP_005009.2) was expressed with a C-terminal polyhistidine tag.
The recombinant mature human PD1 consists of 154 amino acids and has a calculated molecular mass of 17.4 kDa.
> 95 % as determined by SDS-PAGE
Measured by its binding ability in a functional ELISA. Immobilized human PD-1 at 10 μg/ml (100 μl/well) can bind recombinant human B7-H1 / PD-L1 / Fc chimera with a linear range of 0.02-0.4 μg/ml.
Human PD1 / PDCD1 Protein (His Tag) SDS-PAGE
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