Recombinant Human PD-L1/B7-H1 His-tag Avi-tag Protein, CF Summary
Additional Information |
Biotinylated |
Details of Functionality |
Measured by its binding ability in a functional ELISA. When Recombinant Human PD-1 Fc Chimera
(Catalog #
1086-PD)
is immobilized at 2 µg/mL (100
µL/well), Biotinylated Recombinant Human PD-L1 His-tag Avi-tag protein binds with an ED 50 of 2-12 μg/mL. |
Source |
Human embryonic kidney cell, HEK293-derived human PD-L1/B7-H1 protein Human B7-H1 (Phe19-Thr239) Accession # Q9NZQ7 | HHHHHH | Avi-tag
| N-terminus | | C-terminus | |
|
Accession # |
|
N-terminal Sequence |
Phe19 |
Structure / Form |
Biotinylated via Avi-tag |
Protein/Peptide Type |
Recombinant Proteins |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
28 kDa. 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. |
SDS-PAGE |
35-41 kDa, reducing conditions |
Packaging, Storage & Formulations
Storage |
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 °C under sterile conditions after reconstitution.
|
Buffer |
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 500 μg/mL in PBS. |
Notes
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 His-tag Avi-tag Protein, CF
Background
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), endothelial
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.
- Cao, Y. et al. (2010) Cancer Res. 71:1235.
- Scandiuzzi, L. et al. (2014) Cell Rep. 6:625.
- Dong, H. et al. (2002) Nat. Med. 8:793.
- Azuma, T. et al. (2008) Blood 111:3635.
- Butte, M.J. et al. (2008) Mol. Immunol. 45:3567.
- Park, J.-J. et al. (2010) Blood 116:1291.
- Ritprajak, P. et al. (2010) J. Immunol. 184:4918.
- Herold, M. et al. (2015) J. Immunol. 195:3584.
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