Recombinant Cynomolgus Fc gamma RIII/CD16 Protein, CF Summary
Details of Functionality |
Measured by its binding ability in a functional ELISA. When Recombinant Cynomolgus Monkey Fc gamma RIII (CD16) was immobilize on a His Tag antibody coated plate, it binds biotinylated Human IgG. The concentration
of biotinylated Human IgG that
produces 50% of the optimal binding response is approximately 0.15-0.75
μg/mL. |
Source |
Human embryonic kidney cell, HEK293-derived cynomolgus monkey Fc gamma RIII (CD16) protein Gly17-Gln208, with a C-terminal 6-His tag |
Accession # |
|
N-terminal Sequence |
Gly17, Glu21 and Met18 |
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 |
23 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 |
36-44 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 to -70 °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 200 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 Fc gamma RIII/CD16 Protein, CF
Background
Fc gamma RIII/CD16 is a low/intermediate affinity receptor for polyvalent immune-complexed IgG. It is involved in phagocytosis, secretion of enzymes and inflammatory mediators, antibody-dependent cytotoxicity, and clearance of immune complexes (1-3). Mature cynomolgus Fc gamma RIII consists of a 192 aa ECD with two C2-type
Ig-like domains, a 21 aa transmembrane segment, and a 25 aa cytoplasmic domain (4). In humans, Fc gamma RIIIA/CD16a is expressed as a 50-70 kDa transmembrane activating receptor on NK cells, T cells, monocytes, and macrophages (2). It is closely related to the GPI-linked Fc gamma RIIIB which is expressed on human neutrophils and eosinophils (1, 3). These two proteins share 97% amino acid (aa) identity within their extracellular domains (ECD) (5). Within the ECD, mature cynomolgus Fc gamma RIII shares 92% and 90% aa sequence identity with human Fc gamma RIIIA and Fc gamma RIIIB, respectively. Fc gamma RIII surface expression requires interaction with an accessory chain, either the common gamma -chain or CD3 zeta (8, 9). Glycosylation patterns, electrophoretic mobility, and binding affinity appear to differ between NK cell and monocyte Fc gamma RIIIA (10). Shed forms of both Fc gamma RIIIA and Fc gamma RIIIB can be generated by proteolytic cleavage and retain binding activity (11-14). Shedding from monocytes and macrophages can be triggered by cell activation or phagocytosis (14). Soluble Fc gamma RIII circulates in normal plasma and is elevated in rheumatoid arthritis and in coronary artery diseases (12, 13). Cynomolgus Fc gamma RIII binds to cynomolgus IgG subclasses 1-4, to human IgG1 and 3, and more weakly to human IgG2 and 4 (15).
- Nagelkerke, S.Q. and T.W. Kuijpers (2015) Front. Immunol. 5:674.
- Nimmerjahn, F. and J.V. Ravetch (2006) Immunity 24:19.
- Ravetch, J.V. and B. Perussia (1989) J. Exp. Med. 170:481.
- Rogers, K.A. et al. (2008) J. Immunol. 177:3848.
- Scallon, B.J. et al. (1989) Proc. Natl. Acad. Sci. USA 86:5079.
- Wu, J. et al. (1997) J. Clin. Invest. 100:1059.
- Dall'Ozzo, S. et al. (2004) Cancer Res. 64:4664.
- Kim, M.-K. et al. (2003) Blood 101:4479.
- Lanier, L.L. et al. (1989) Nature 342:803.
- Edberg, J.C. and R.P. Kimberley (1997) J. Immunol. 159:3849.
- Li, P. et al. (2007) J. Biol. Chem. 282:6210.
- Masuda, M. et al. (2003) J. Rheumatol. 30:1911.
- Masuda, M. et al. (2006) Atherosclerosis 188:377.
- Webster, N.L. et al. (2006) J. Leukoc. Biol. 79:294.
- Warncke, M. et al. (2012) J. Immunol. 188:4405.
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