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Recombinant Cynomolgus/Rhesus Macaque CD27 Fc Protein, CF

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2 μg/lane of Recombinant Cynomolgus Monkey CD27 was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® blue staining, showing bands at kDa and kDa, respectively.

Product Details

Summary
Reactivity Pm-Cm, RMSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Cynomolgus/Rhesus Macaque CD27 Fc Protein, CF Summary

Details of Functionality
Measured by its ability to inhibit CD70-induced IL-8 secretion in HT1080 human fibrosarcoma cells transfected with human CD27. The ED50 for this effect is 0.25-1.5 μg/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived CD27/TNFRSF7 protein
Cynomolgus Monkey CD27
(Ala20-Arg191)
Accession # XP_005569963.1
IEGRMD Human IgG1
(Pro100-Lys330)
N-terminusC-terminus
Accession #
N-terminal Sequence
Thr21
Structure / Form
Disulfide-linked homodimer
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
  • Bioactivity
Theoretical MW
46 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
61-68 kDa, reducing conditions

Packaging, Storage & Formulations

Storage
  • 12 months from date of receipt, ≤ -20 °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.
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 Cynomolgus/Rhesus Macaque CD27 Fc Protein, CF

  • CD27 antigen
  • CD27 molecule
  • CD27
  • MGC20393
  • S152CD27L receptor
  • T cell activation antigen CD27
  • T cell activation antigen S152
  • T14
  • TNFRSF7
  • TNFRSF7T-cell activation antigen CD27
  • Tp55
  • Tumor necrosis factor receptor superfamily member 7
  • tumor necrosis factor receptor superfamily, member 7

Background

CD27, also known as TNFRSF7, is an approximately 55 kDa transmembrane protein in the TNF receptor superfamily. It functions as a co‑stimulatory molecule that supports lymphocyte activation and survival (1). Mature human CD27 consists of a 172 amino acid (aa) extracellular domain (ECD) with three TNFR cysteine‑rich repeats, a 21 aa transmembrane segment, and a 48 aa cytoplasmic domain (2). Within the ECD, cynomolgus CD27 shares 94%, 62% and 66% aa sequence identity with human, mouse, and rat CD27, respectively. CD27 is expressed as a disulfide‑linked homodimer that carries N‑linked and O‑linked glycosylation (3, 4). Proteolytic cleavage of CD27 results in the shedding of a 28‑32 kDa fragment of the ECD (4). CD27 is weakly expressed on naïve T cells and NK cells and is up‑regulated upon cell activation (4, 5). It is also up‑regulated on activated germinal center B cells, plasma cells, and a subset of memory B cells (6, 7). CD27 binds to the transmembrane glycoprotein CD27 Ligand/CD70 which is expressed on activated B cells, activated T cells, and dendritic cells (1, 8, 9). This interaction contributes to the activation and survival of CD4+ helper T cells (8‑11), CD8+ effector T cells (12, 13), memory T cells (10), and NK cells (5, 14). Ligation of CD27 on B cells promotes germinal center formation and the expansion and affinity maturation of memory B cell responses (6, 15).
  1. Nolte, M.A. et al. (2009) Immunol. Rev. 229:216.
  2. Camerini, D. et al. (1991) J. Immunol. 147:3165.
  3. van Lier, R.A. et al. (1987) J. Immunol. 139:1589.
  4. Loenen, W.A. et al. (1992) Eur. J. Immunol. 22:447.
  5. Takeda, K. et al. (2000) J. Immunol. 164:1741.
  6. Xiao, Y. et al. (2004) J. Immunol. 172:7432.
  7. Jung, J. et al. (2000) Eur. J. Immunol. 30:2437.
  8. Goodwin, R.G. et al. (1993) Cell 73:447.
  9. Bowman, M.R. et al. (1994) J. Immunol. 152:1756.
  10. Hendriks, J. et al. (2000) Nat. Immunol. 1:433.
  11. van Oosterwijk, M.F. et al. (2007) Int. Immunol. 19:713.
  12. Rowley, T.F. and A. Al Shamkhani (2004) J. Immunol. 172:6039.
  13. Hendriks, J. et al. (2003) J. Exp. Med. 198:1369.
  14. Kelly, J.M. et al. (2002) Nat. Immunol. 3:83.
  15. Raman, V.S. et al. (2003) J. Immunol. 171:5876.

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