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Recombinant Human Fc gamma RIIIB/CD16b Protein

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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.

Product Details

Summary
Product Discontinued
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Order Details


    • Catalog Number
      1597-FC
    • Availability
      Product Discontinued

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Recombinant Human Fc gamma RIIIB/CD16b Protein Summary

Details of Functionality
Measured by its ability to bind human IgG with an estimated Kd <150 nM.
Source
Mouse myeloma cell line, NS0-derived human Fc gamma RIIIB/CD16b protein
Thr20-Gln208, with a C-terminal 10-His tag
Accession #
N-terminal Sequence
Thr20
Protein/Peptide Type
Recombinant Proteins
Gene
FCGR3B
Purity
>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:

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 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.

  1. van de Winkel, J, and P. Capes (1993) Immunol. Today 14:215.
  2. Ravetch, J.V. and S. Bolland (2001) Annu. Rev. Immunol. 19:275.
  3. Takai, T. (2002) Nature Rev. Immunol. 2:580.
  4. Gauchat, G.J. et al. (1996) J. Immunol. 157:1184.

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1597-FC
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Applications: Binding Activity

Publications for Fc gamma RIIIB/CD16b (1597-FC)(7)

We have publications tested in 1 confirmed species: Human.

We have publications tested in 6 applications: Bioassay, ELISA (Capture), ELISA Capture, EMSA, Surface Plasmon Resonance, Surface Plasmon Resonance (SPR.


Filter By Application
Bioassay
(1)
ELISA (Capture)
(2)
ELISA Capture
(1)
EMSA
(1)
Surface Plasmon Resonance
(1)
Surface Plasmon Resonance (SPR
(1)
All Applications
Filter By Species
Human
(6)
All Species
Showing Publications 1 - 7 of 7.
Publications using 1597-FC Applications Species
Y Kitanaga, D Yamajuku, S Kubo, K Nakamura, M Maeda, M Seki, Y Kaneko, F Kinugasa, T Morokata, Y Kondo, H Yoshinari, S Nakayamada, T Sumida, Y Tanaka Discovery of a novel Igbeta and FcgammaRIIB cross-linking antibody, ASP2713, and its potential application in the treatment of systemic lupus erythematosus International immunopharmacology, 2021-11-12;101(0):108343. 2021-11-12 [PMID: 34781122] (ELISA Capture, Human) ELISA Capture Human
PA Blundell, D Lu, M Wilkinson, A Dell, S Haslam, RJ Pleass Insertion of N-Terminal Hinge Glycosylation Enhances Interactions of the Fc Region of Human IgG1 Monomers with Glycan-Dependent Receptors and Blocks Hemagglutination by the Influenza Virus J. Immunol., 2019-01-25;0(0):. 2019-01-25 [PMID: 30683699] (ELISA (Capture), Human) ELISA (Capture) Human
N Seo, A Polozova, M Zhang, Z Yates, S Cao, H Li, S Kuhns, G Maher, HJ McBride, J Liu Analytical and functional similarity of Amgen biosimilar ABP 215 to bevacizumab MAbs, 2018-04-20;0(0):1-58. 2018-04-20 [PMID: 29553864] (Surface Plasmon Resonance (SPR, Human) Surface Plasmon Resonance (SPR Human
Xie J, Yamniuk A, Borowski V, Kuhn R, Susulic V, Rex-Rabe S, Yang X, Zhou X, Zhang Y, Gillooly K, Brosius R, Ravishankar R, Waggie K, Mink K, Price L, Rehfuss R, Tamura J, An Y, Cheng L, Abramczyk B, Ignatovich O, Drew P, Grant S, Bryson J, Suchard S, Salter-Cid L, Nadler S, Suri A Engineering of a novel anti-CD40L domain antibody for treatment of autoimmune diseases. J Immunol, 2014-03-26;192(9):4083-92. 2014-03-26 [PMID: 24670803] (Bioassay, Human) Bioassay Human
Derer S, Glorius P, Schlaeth M, Lohse S, Klausz K, Muchhal U, Desjarlais J, Humpe A, Valerius T, Peipp M Increasing FcgammaRIIa affinity of an FcgammaRIII-optimized anti-EGFR antibody restores neutrophil-mediated cytotoxicity. MAbs, 2013-12-11;6(2):409-21. 2013-12-11 [PMID: 24492248] (Surface Plasmon Resonance) Surface Plasmon Resonance
Boltz A, Piater B, Toleikis L, Guenther R, Kolmar H, Hock B Bi-specific Aptamers Mediating Tumor Cell Lysis. J. Biol. Chem., 2011-04-29;286(24):21896-905. 2011-04-29 [PMID: 21531729] (EMSA, Human) EMSA Human
Bergin DA, Reeves EP, Meleady P, Henry M, McElvaney OJ, Carroll TP, Condron C, Chotirmall SH, Clynes M, O'Neill SJ, McElvaney NG Alpha-1 Antitrypsin regulates human neutrophil chemotaxis induced by soluble immune complexes and IL-8. J. Clin. Invest., 2010-11-08;120(12):4236-50. 2010-11-08 [PMID: 21060150] (ELISA (Capture), Human) ELISA (Capture) Human

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Bioinformatics

Gene Symbol FCGR3B
Uniprot