Recombinant Human Fc gamma RIIIB/CD16b (Catalog # 1597-FC) binds human IgG with an estimated Kd
1 μg/lane of Recombinant Human Fc gamma RIIIB/CD16b was resolved with SDS-PAGE under reducing (R) conditions and visualized by silver staining, showing a band at 43-60 kDa.
>90%, 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
Binding Activity
Theoretical MW
22.7 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
40-60 kDa, reducing conditions
Publications
Read Publications using 1597-FC in the following applications:
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 with BSA as a carrier protein.
Purity
>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 containing at least 0.1% human or bovine serum albumin.
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 Protein
CD16
CD16b antigen
CD16b
Fc fragment of IgG, low affinity IIIb, receptor (CD16b)
Fc fragment of IgG, low affinity IIIb, receptor for (CD16)
Fc gamma RIIIB
FCG3
Fc-gamma receptor IIIb (CD 16)
Fc-gamma RIII
Fc-gamma RIIIb
Fc-gamma RIII-beta
FCGR3
FCGR3B
FcgRIIIB
FcR-10
fcRIII
FCRIIIB
IGFR3
IgG Fc receptor III-1
low affinity immunoglobulin gamma Fc region receptor III-B
Background
Receptors for the Fc region of IgG (Fc gamma R) are members of the Ig superfamily. Based on their genetic organization and molecular structure, 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 domains of 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.
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