Ugrás a tartalomra
Merck

F3668

Sigma-Aldrich

Monoclonal Anti-CD16−FITC antibody produced in mouse

clone 3G8, purified immunoglobulin, buffered aqueous solution

Szinonimák:

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

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

MDL-szám:
UNSPSC kód:
12352203
NACRES:
NA.44

biológiai forrás

mouse

Minőségi szint

konjugátum

FITC conjugate

antitest forma

purified immunoglobulin

antitest terméktípus

primary antibodies

klón

3G8, monoclonal

Forma

buffered aqueous solution

faj reaktivitás

human

tárolási körülmény

protect from light

technika/technikák

flow cytometry: 10 μL using 1 × 106 cells

izotípus

IgG1

UniProt elérési szám

kiszállítva

wet ice

tárolási hőmérséklet

2-8°C

célzott transzláció utáni módosítás

unmodified

Géninformáció

Related Categories

Általános leírás

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.

Egyediség

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.

Immunogén

viable human polymorphonuclear cells.

Alkalmazás

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.

Biokémiai/fiziológiai hatások

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).

Cél megnevezése

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.

Fizikai forma

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

Elkészítési megjegyzés

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

Jogi nyilatkozat

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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Tárolási osztály kódja

10 - Combustible liquids

WGK

nwg

Lobbanási pont (F)

Not applicable

Lobbanási pont (C)

Not applicable

Egyéni védőeszköz

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


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Analitikai tanúsítványok (COA)

Lot/Batch Number

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Dokumentumtár megtekintése

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)
The structure and function of Fc receptors.
N Hogg
Immunology today, 9(7-8), 185-187 (1988-07-01)
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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