PD-L1 Extracellular Domain (human, recombinant)

B7-H1|CD274|PDCD1 Ligand 1|Programmed Cell Death 1 Ligand 1

Programmed cell death 1 ligand 1 (PD-L1), also known as B7-H1 or CD274, is a B7 family protein that is involved in regulation and attenuation of the adaptive immune response and peripheral T cell tolerance.{53691,52533,53686,53693} It is a 290-amino acid type I transmembrane protein encoded by the CD274 gene in humans and is comprised of a 239-amino acid extracellular domain consisting of a signal peptide, an IgV-like domain, and an IgC-like domain, a transmembrane domain, and a cytoplasmic tail.{53691,53692} PD-L1 is constitutively expressed in T and B cells, dendritic cells, macrophages, and regulatory T cells (Tregs), as well as a variety of nonhematopoietic cells and is upregulated by IFN-γ.{53686} Binding of PD-L1 to its receptor, programmed cell death protein 1 (PD-1), suppresses T cell proliferation, migration, and cytokine production.{52533,53693} PD-L1 is also aberrantly expressed in a variety of tumor cells, and expression of PD-L1 in tumor tissue is associated with poor prognosis in patients with renal cell carcinoma. {53690,53688,53694} Formulations containing PD-L1 blocking antibodies have been used in the treatment of a variety of cancers. Cayman's PD-L1 Extracellular Domain (human, recombinant) protein can be used for ELISA, binding assay, and cell-based assay applications. This protein is a disulfide-linked homodimer. The reduced monomer, comprised of PD-L1 (amino acids 19-239) fused to mouse IgG1 Fc at its C-terminus, consists of 455 amino acids, has a calculated molecular weight of 51.7 kDa, and a predicted N-terminus of Phe19 after signal peptide cleavage. As a result of glycosylation, the monomer migrates at approximately 66 kDa by SDS-PAGE under reducing conditions.

-80

-80

Lyophilized from 20 mM Tris, pH 8.5, with 150 mM sodium chloride and 10% glycerol

365

≥95% estimated by SDS-PAGE