>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
<0.10 EU per 1 μg of the protein by the LAL method.
Measured by its binding ability in a functional ELISA. When Recombinant Human PD-L1/B7-H1
is immobilized at 0.025 µg/mL
(100 µL/well), the concentration of
Recombinant Human PD‑1 Fc Chimera (Catalog # 1086-PD) that produces 50% of the optimal binding response is approximately 0.05-0.3 μg/mL.
Human embryonic kidney cell, HEK293-derived human PD-L1/B7-H1 protein Phe19-Thr239, with a C-terminal 6-His tag
WhenRecombinant Human PD-L1/B7-H1 is immobilized at 0.025 µg/mL,it binds to Recombinant Human PD‑1 Fc Chimera (Catalog # 1086-PD) with an ED50 of 0.05-0.3 μg/mL.
B7-H1, also known as PD-L1 and CD274, is an approximately 65 kDa transmembrane glycoprotein in the B7 family of immune regulatory molecules (1). Mature human B7-H1 consists of a 220 amino acid (aa) extracellular domain (ECD) with two immunoglobulin-like domains, a 21 aa transmembrane segment, and a 31 aa cytoplasmic domain (2). Within the ECD, human B7-H1 shares 73% and 74% aa sequence identity with mouse and rat B7-H1, respectively. Alternative splicing generates additional isoforms that either lack the first Ig-like domain or are truncated within the second Ig-like domain (3). B7-H1 is expressed on inflammatory-activated immune cells including macrophages, T cells, and B cells (4-7), keratinocytes (8, 9), enothelial and intestinal epithelial cells (8, 10), as well as a variety of carcinomas and melanoma (11, 12). B7-H1 binds to T cell B7-1/CD80 and PD-1 (7, 8, 12-15). It suppresses T cell activation and proliferation (5, 8, 14, 16) and induces the apoptosis of activated T cells (11). It plays a role in the development of immune tolerance by promoting T cell anergy (7, 14) and enhancing regulatory T cell development (16). B7-H1 favors the development of anti-inflammatory IL-10 and IL-22 producing dendritic cells (5, 10) and inhibits the development of Th17 cells (16). In cancer, B7-H1 provides resistance to T cell mediated lysis, enhances EMT, and enhances the tumorigenic function of Th22 cells (6, 9, 12, 15).
Ceeraz, S. et al. (2013) Trends Immunol. 34:556.
Dong, H. et al. (1999) Nat. Med. 5:1365.
Frigola, X. et al. (2011) Clin. Cancer Res. 17:1915.
Tamura, H. et al. (2001) Blood 97:1809.
Chen, L. et al. (2007) J. Immunol. 178:6634.
Kuang, D.-M. et al. (2014) J. Clin. Invest. 124:4657.
Tsushima, F. et al. (2007) Blood 110:180.
Mazanet, M.M. and C.C.W. Hughes (2002) J. Immunol. 169:3581.
R&D Systems personnel manually curate a database that contains references using R&D Systems products.
The data collected includes not only links to publications in PubMed,
but also provides information about sample types, species, and experimental conditions.
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