Cayman PD-L1 Extracellular Domain (human, recombinant) - Biotinylated

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.^1,2,3,4 It is a 290-amino acid type I transmembrane protein encoded by CD274 in humans and is composed 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.^1,5 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.³ Binding of PD-L1 to its receptor, programmed cell death protein 1 (PD-1), suppresses T cell proliferation, migration, and cytokine production.^2,4 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.^6,7,8 Formulations containing PD-L1 blocking antibodies have been used in the treatment of a variety of cancers. Caymans PD-L1 Extracellular Domain (human, recombinant) - Biotinylated protein contains purified PD-L1 that has been biotinylated via the E. coli biotin ligase enzyme BirA, which was subsequently depleted by affinity chromatography. It consists of 253 amino acids including the purification tag, has a calculated molecular weight of 27.1 kDa, and a predicted N-terminus of Phe19 after signal peptide cleavage. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is 35 kDa due to post-translational modifications.

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