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F3668

Sigma-Aldrich

Monoclonal Anti-CD16−FITC antibody produced in mouse

clone 3G8, purified immunoglobulin, buffered aqueous solution

Synonym(s):

Anti-CD16-II-Fluorescein isothiocyanate, Anti-CD16A-Fluorescein isothiocyanate, Anti-FCG3-Fluorescein isothiocyanate, Anti-FCGR3-Fluorescein isothiocyanate, Anti-FCGRIII-Fluorescein isothiocyanate, Anti-FCR-10-Fluorescein isothiocyanate, Anti-FCRIII-Fluorescein isothiocyanate, Anti-FCRIIIA-Fluorescein isothiocyanate, Anti-FcGRIIIA-Fluorescein isothiocyanate, Anti-IGFR3-Fluorescein isothiocyanate, Anti-IMD20-Fluorescein isothiocyanate

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.44

biological source

mouse

Quality Level

conjugate

FITC conjugate

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

3G8, monoclonal

form

buffered aqueous solution

species reactivity

human

storage condition

protect from light

technique(s)

flow cytometry: 10 μL using 1 × 106 cells

isotype

IgG1

UniProt accession no.

shipped in

wet ice

storage temp.

2-8°C

target post-translational modification

unmodified

Gene Information

Related Categories

General description

Human CD16 or FCγRIII is a 50-70kDa membrane glycoprotein expressed by neutrophils, eosinophils, cultured monocytes, natural killer (NK) cells, tissue macrophages subpopulation, and on a small subset of T cells that binds aggregated but not monomeric human IgG. It is also known as FcR3, the low affinity receptor for complexed IgG. It comprises of two truncated Ig-like cytoplasmic domains.
Monoclonal Anti-CD16 (mouse IgG1 isotype) is derived from the 3G8 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from an immunized CD2F1 mouse.

Specificity

Recognizes the human CD16 antigen expressed on natural killer (NK) cells, granulocytes and a macrophage subpopulation. The antibody reacts with both NA1 and NA2 neutrophils and NK lymphocytes. It strongly labels neutrophils in tissue frozen sections. Liver Kupffer cells are weakly stained. The epitope recognized by the antibody seems to reside near the IgG binding site of FCγ-RIII. The antibody functionally blocks binding of soluble immune complexes to granulocytes and inhibits E-IgG rosettes. It induces Ca2+ increase in neutrophils.

Immunogen

viable human polymorphonuclear cells.

Application

Monoclonal Anti-CD16-FITC antibody is suitable for receptor blocking in flow cytometry analysis.
Monoclonal Anti-CD16-FITC antibody produced in mouse has been used in direct immunofluorescent staining.

Biochem/physiol Actions

Cluster of differentiation 16 (CD16) induces Ca2+ increase in neutrophils. It strongly labels neutrophils in tissue frozen sections. Liver kupffer cells are weakly stained. The antibody functionally blocks binding of soluble immune complexes to granulocytes and inhibits E-IgG rosettes.
Human CD16 plays a pivotal role in immune responses by linking the humoral immune system with cellular effector functions. CD16 plays an important role in natural killer (NK)-cell function and in peripheral blood mononuclear cells (PBMCs). In the FcyRIII-expressing lymphocytes the NK cell activity is highly influenced through FcyRIII. CD16 exists as a transmembrane form in NK cells, macrophages and cultured monocytes with a 25 amino acid cytoplasmic tail which further connects with other receptors. The transmembrane form binds complexed IgG and mediates phagocytosis and antibody-dependent cellular cytotoxicity (ADCC).

Target description

CD16 antigen (also known as the low affinity receptor for complexed IgG, or Fcγ-RIII) expressed on natural killer (NK) cells, a macrophage sub-population and weakly on granulocytes. The human CD16 molecule exhibits two truncated Ig-like domains. In NK cells and macrophages, a trans-membrane form (50-80 kDa) with a 25 amino acid cytoplasmic tail is present. This form is non-covalently associated with other receptors (FcεRIγ or the TcRξ chain). The human CD16 molecule in granulocytes is a glycosyl-phosphatidyl-inositol (GPI)-linked form.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% bovine serum albumin and 15 mM sodium azide.

Preparation Note

Prepared by conjugation to fluorescein isothiocyanate isomer I (FITC). This green dye is efficiently excited at 495 nm and emits at 525 nm.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class Code

10 - Combustible liquids

WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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The structure and function of Fc receptors.
N Hogg
Immunology today, 9(7-8), 185-187 (1988-07-01)
Differential regulation of human neutrophil FcgammaRIIa (CD32) and FcgammaRIIIb (CD16)-induced Ca2+ transients
Edberg JC, et al.
The Journal of Biological Chemistry, 273(14), 8071-8079 (1998)
G A Peltz et al.
Proceedings of the National Academy of Sciences of the United States of America, 86(3), 1013-1017 (1989-02-01)
A cDNA clone encoding a human receptor for the Fc portion of IgG (Fc gamma R), Fc gamma RIII or CD16, was isolated from a human leukocyte library by a transient expression-immunoselection procedure. This cDNA (pGP5) encodes a 46-kDa phosphatidylinositol-linked
D Harrison et al.
Journal of immunology (Baltimore, Md. : 1950), 147(10), 3459-3465 (1991-11-15)
Two genes encode the CD16 low affinity IgG FcR. CD16-I (Fc gamma RIII-1) is expressed on PMN as a phosphatidylinositol-glycan anchored glycoprotein. CD16-II (Fc gamma RIII-2) is expressed on NK cells and macrophages as a transmembrane glycoprotein associated with CD3
J V Ravetch et al.
Annual review of immunology, 9, 457-492 (1991-01-01)
Recent advances in the structural analysis of the genes and proteins for immunoglobulin Fc domain receptors have provided a molecular characterization of this complex family. The wide cellular distribution of these receptors and their functional heterogeneity are reflected in the

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