Recombinant Human Fc gamma RIIIB/CD16b (aa18-200) Protein Summary
Details of Functionality |
Measured by its binding ability in a functional ELISA. When Recombinant Human Fc gamma RIIIB/CD16b is immobilized on
a His Tag Antibody (Catalog # MAB050R) coated plate, it binds Biotinylated Human IgG. The
concentration
of Biotinylated Human IgG that
produces 50% of the optimal binding response is 0.3-1.5
μg/mL. |
Source |
Human embryonic kidney cell, HEK293-derived human Fc gamma RIIIB/CD16b protein Met18-Ser200, with a C-Terminal 6-His tag |
Accession # |
|
N-terminal Sequence |
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 |
22 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 |
37-50 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 Human Fc gamma RIIIB/CD16b (aa18-200) Protein
Background
Receptors for the Fc region of IgG (Fc gamma R)
are members of the Ig superfamily. Based on the genetic organization and molecular
structure of receptors for the Fc region of IgG (Fc gamma R), three classes of
human Fc gamma Rs: RI (CD64), RII (CD32), and RIII (CD16), which generate
multiple isoforms, are recognized (1-3). These receptors function in the
activation or inhibition of immune responses. The activating-type receptor
either has, or associates non-covalently with an accessory subunit (FcR gamma or
zeta chain) that has an immunoreceptor tyrosine-based activation motif (ITAM)
in its cytoplasmic domain. In contrast, the inhibitory receptor (Fc gamma RIIB)
has a built-in immunoreceptor tyrosine-based inhibitory motif (ITIM) in its own
cytoplasmic domain. Fc gamma RI is a high-affinity receptor that binds
monomeric IgG. Both Fc gamma RII and RIII are low-affinity receptors that bind
IgG in the form of immune complexes. Two genes for human Fc gamma RIII, A and
B, encoding a transmembrane receptor and a glycosylphosphatidylinositol (GPI)
anchored protein, respectively, have been identified. Three allelic variants of
Fc gamma RIIIB, NA-1, NA-2, and SH, exist. A soluble form of Fc gamma RIIIB
corresponding to the extracellular region of the receptor is produced by
proteolytic cleavage and circulates in plasma and other body fluids. The
extracellular region of Fc gamma RIIIB share 62% and 59% sequence homology with
the mouse and rat variants, respectively. The extracellular domains of human Fc
gamma RIIIA and B share 97% amino acid sequence homology. Whereas Fc gamma RIIIA is expressed on most effector cells of the immune system including
macrophage, monocyte, NK cells, mast cells, eosinophils, dendritic cells
and Langerhans cells, Fc gamma RIIIB is selectively expressed in neutrophils
and eosinophils. Signaling through Fc gamma RIIIA results in oxidative burst,
cytokine release and phagocytosis by macrophages, antibody-dependent cellular
cytotoxicity by natural killer cells and degranulation of mast cells. By
contrast, Fc gamma RIIIB is a decoy receptor that binds IgG complexes without
triggering activation. Soluble Fc gamma RIIIB has a regulatory role in
inflammatory processes (4). It interacts with complement receptors CR3 and CR4
on monocytes to induce the production of pro-inflammatory cytokines.
- van de Winkel, J, and P. Capes (1993) Immunol. Today 14:215.
- Ravetch, J.V. and S. Bolland (2001) Annu. Rev. Immunol. 19:275.
- Takai, T. (2002) Nature Rev. Immunol. 2:580.
- Gauchat, G.J. et al. (1996) J. Immunol. 157:1184.
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