Recombinant Human PD-L1/B7-H1 Fc Chimera Protein, CF


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Recombinant Human PD-L1/B7-H1 Fc Chimera Protein, CF Summary

Details of Functionality
Measured by its ability to inhibit anti-CD3 antibody induced IL-2 secretion in human T lymphocytes. The ED50 for this effect is 0.075-0.75 μg/mL.
Mouse myeloma cell line, NS0-derived human PD-L1/B7-H1 protein
Human PD-L1
Accession # Q9NZQ7
N-terminus C-terminus
Accession #
N-terminal Sequence
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.


Theoretical MW
52 kDa (monomer).
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
70-75 kDa, reducing conditions
Read Publications using
156-B7 in the following applications:

Packaging, Storage & Formulations

Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Lyophilized from a 0.2 μm filtered solution in PBS and NaCl.
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.


This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human PD-L1/B7-H1 Fc Chimera Protein, CF

  • Avelumab
  • B7-H
  • B7H1
  • B7-H1
  • B7H1PDCD1L1
  • CD274 antigenMGC142294
  • CD274 molecule
  • CD274
  • PDCD1L1
  • PDCD1LG1
  • PDCD1LG1MGC142296
  • PDL1
  • PD-L1
  • PD-L1B7 homolog 1
  • PDL1PDCD1 ligand 1
  • programmed cell death 1 ligand 1
  • Programmed death ligand 1


PD-L1, also known as B7-H1, is one of the ligands for PD-1 and plays a critical role in the regulation of T cell immunity (1-6). The PD-1:PD-L1 interaction initiates a negative signaling cascade in T cells leading to inhibition of T cell activation (2,5,7,8). PD-L1 provides a molecular stop signal to the adaptive immune system helping to distinguish between self and foreign antigens. PD-L1 also plays a role in the development of immune tolerance by promoting T cell anergy (1,5) and enhancing regulatory T cell development (8). In addition, PD-L1 favors the development of anti-inflammatory IL-10 and IL-22 producing dendritic cells (7,9) and inhibits the development of Th17 cells (8). Many cancers exhibit upregulated PD-L1 protein expression, and several cancers with high levels of PD-L1 have been associated with increased tumor aggressiveness and poor prognosis. Using new therapeutics that block the PD-L1:PD-1 interaction has proven successful in the clinic for many cancer types and has sparked great interest in the field of cancer immunotherapy.

The PD-L1 protein is an approximately 65 kDa transmembrane glycoprotein belonging to the B7 family of immune regulatory molecules (10). Mature human PD-L1 protein 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 (11). Within the ECD, human PD-L1 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 (12). PD-L1 is expressed on inflammatory-activated immune cells including macrophages, T cells, and B cells (10,13,14,16), keratinocytes (9,11), endothelial and intestinal epithelial cells (2,9), as well as a variety of carcinomas and melanoma (12,16).

  1. Tsushima, F. et al. (2007) Blood 110:180.
  2. Mazanet, M.M. and C.C.W. Hughes (2002) J. Immunol. 169:3581.
  3. Azuma, T. et al. (2008) Blood 111:3635.
  4. Butte, M.J. et al. (2008) Mol. Immunol. 45:3567.
  5. Park, J.-J. et al. (2010) Blood 116:1291.
  6. Ritprajak, P. et al. (2010) J. Immunol. 184:4918.
  7. Chen, L. et al. (2007) J. Immunol. 178:6634.
  8. Herold, M. et al. (2015) J. Immunol. 195:3584.
  9. Scandiuzzi, L. et al. (2014) Cell Rep. 6:625.
  10. Ceeraz, S. et al. (2013) Trends Immunol. 34:556.
  11. Dong, H. et al. (1999) Nat. Med. 5:1365.
  12. Frigola, X. et al. (2011) Clin. Cancer Res. 17:1915.
  13. Tamura, H. et al. (2001) Blood 97:1809.
  14. Kuang, D.-M. et al. (2014) J. Clin. Invest. 124:4657.
  15. Cao, Y. et al. (2010) Cancer Res. 71:1235.
  16. Dong, H. et al. (2002) Nat. Med. 8:793.

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Publications for PD-L1 (156-B7)(15)

We have publications tested in 3 confirmed species: Human, N/A, Yeast.

We have publications tested in 3 applications: Bioassay, ELISA (Standard), Flow Cytometry.

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ELISA (Standard)
Flow Cytometry
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Showing Publications 1 - 10 of 15. Show All 15 Publications.
Publications using 156-B7 Applications Species
L Sun, CW Li, EM Chung, R Yang, YS Kim, AH Park, YJ Lai, Y Yang, YH Wang, J Liu, Y Qiu, KH Khoo, J Yao, JL Hsu, JH Cha, LC Chan, JM Hsu, HH Lee, SS Yoo, MC Hung Targeting glycosylated PD-1 induces potent anti-tumor immunity Cancer Res., 2020;0(0):. 2020 [PMID: 32156778] (Bioassay, Human) Bioassay Human
B Cembrola, V Ruzza, F Troise, ML Esposito, E Sasso, V Cafaro, M Passariell, F Visconte, M Raia, L Del Vecchi, AM D'Alise, R Cortese, E Scarselli, N Zambrano, C De Lorenzo, A Nicosia Rapid Affinity Maturation of Novel Anti-PD-L1 Antibodies by a Fast Drop of the Antigen Concentration and FACS Selection of Yeast Libraries Biomed Res Int, 2019;2019(0):6051870. 2019 [PMID: 31976323] (Yeast) Yeast
KJ Carpenter, AC Valfort, N Steinauer, A Chatterjee, S Abuirqeba, S Majidi, M Sengupta, RJ Di Paolo, LP Shornick, J Zhang, CA Flaveny LXR-inverse agonism stimulates immune-mediated tumor destruction by enhancing CD8 T-cell activity in triple negative breast cancer Sci Rep, 2019;9(1):19530. 2019 [PMID: 31863071] (Bioassay, Human) Bioassay Human
W Fu, C Lei, S Liu, Y Cui, C Wang, K Qian, T Li, Y Shen, X Fan, F Lin, M Ding, M Pan, X Ye, Y Yang, S Hu CAR exosomes derived from effector CAR-T cells have potent antitumour effects and low toxicity Nat Commun, 2019;10(1):4355. 2019 [PMID: 31554797]
JK Fierle, J Abram-Sali, M Brioschi, M deTiani, G Coukos, SM Dunn Integrating SpyCatcher/SpyTag covalent fusion technology into phage display workflows for rapid antibody discovery Sci Rep, 2019;9(1):12815. 2019 [PMID: 31492910] (Bioassay, Human) Bioassay Human
A Osa, T Uenami, S Koyama, K Fujimoto, D Okuzaki, T Takimoto, H Hirata, Y Yano, S Yokota, Y Kinehara, Y Naito, T Otsuka, M Kanazu, M Kuroyama, M Hamaguchi, T Koba, Y Futami, M Ishijima, Y Suga, Y Akazawa, H Machiyama, K Iwahori, H Takamatsu, I Nagatomo, Y Takeda, H Kida, EA Akbay, PS Hammerman, KK Wong, G Dranoff, M Mori, T Kijima, A Kumanogoh Clinical implications of monitoring nivolumab immunokinetics in non-small cell lung cancer patients JCI Insight, 2018;3(19):. 2018 [PMID: 30282824] (Flow Cytometry, Human) Flow Cytometry Human
UM Vogl, L Öhler, M Rasic, JM Frischer, M Modak, J Stöckl Evaluation of Prognostic Immune Signatures in Patients with Breast, Colorectal and Pancreatic Cancer Receiving Chemotherapy Anticancer Res., 2017;37(4):1947-1955. 2017 [PMID: 28373465] (ELISA (Standard)) ELISA (Standard)
E Burova, A Hermann, J Waite, T Potocky, V Lai, S Hong, M Liu, O Allbritton, A Woodruff, Q Wu, A D'Orvillie, E Garnova, A Rafique, W Poueymirou, J Martin, T Huang, D Skokos, J Kantrowitz, J Popke, M Mohrs, D MacDonald, E Ioffe, W Olson, I Lowy, A Murphy, G Thurston Characterization of the anti-PD-1 antibody REGN2810 and its antitumor activity in human PD-1 knock-in mice Mol. Cancer Ther, 2017;0(0):. 2017 [PMID: 28265006] (Bioassay, N/A) Bioassay N/A
Robert L Ferris Tumor-infiltrating Tim-3(+) T cells proliferate avidly except when PD-1 is co-expressed: Evidence for intracellular cross talk Oncoimmunology, 2016;5(10):e1200778. 2016 [PMID: 27853635] (Bioassay) Bioassay
B7-H1 antibodies lose antitumor activity due to activation of p38 MAPK that leads to apoptosis of tumor-reactive CD8(+) T cells Sci Rep, 2016;6(0):36722. 2016 [PMID: 27824138] (ELISA (Standard), Human) ELISA (Standard) Human
Show All 15 Publications.

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Gene Symbol CD274