This antibody recognizes an extracellular epitope on CD64, a 72 kDa single chain type I glycoprotein, that is expressed on monocytes / macrophages, dendritic cells, and activated granulocytes.

Applications

Flow Cytometry

Dilutions

Flow Cytometry: The reagent is designed for analysis of human blood cells using 4 µl reagent / 100 µl of whole blood or 10⁶ cells in a suspension. The content of a vial (0.4 ml) is sufficient for 100 tests.

Reactivity

Human, Non-Human Primates

Immunogen

Rheumatoid synovial fluid cells and fibronectin purified human monocytes.

Host

Mouse

Clonality

Monoclonal

Clone ID

10.1

Isotype

IgG1

Light Chains

kappa

Conjugate

FITC

Excitation: 490nm, Emission: 525nm

Purification

This antibody is conjugated with Fluorescein Isothiocyanate (FITC) under optimum conditions. The conjugate is purified by size-exclusion chromatography; removing unconjugated antibody and free fluorochrome.

Predicted MW

72 kDa

Product Form

Liquid

Formulation

Supplied in Phosphate Buffered Saline, pH 7.4, with 15 mM Sodium Azide.

Storage

Shipped at 4°C. Store in the dark at 2-8°C. Do not freeze!

Synonyms

CD 64, CD64 antigen, CD64A, CD64b, CD64c, Fc fragment of IgG high affinity Ia receptor, Fc fragment of IgG high affinity Ib receptor, Fc fragment of IgG high affinity Ic receptor, Fc fragment of IgG, high affinity Ia, receptor (CD64), Fc fragment of IgG, high affinity Ia, receptor for, Fc fragment of IgG, high affinity Ia, receptor for (CD64), Fc fragment of IgG, high affinity Ib, receptor (CD64), Fc fragment of IgG, high affinity Ib, receptor for, Fc fragment of IgG, high affinity Ic, receptor (CD64), Fc fragment of IgG, high affinity Ic, receptor (CD64), pseudogene, Fc fragment of IgG, high affinity Ic, receptor for, Fc gamma receptor, Fc gamma receptor I, Fc gamma receptor I A1, Fc gamma receptor I B2, Fc gamma RI, Fc gamma RIA, Fc gamma RIB, Fc of IgG high affinity Ia receptor, Fc-gamma RIC, FCG 1, FCG1, FcgammaRI, FcgammaRIa, FCGR 1, FCGR1, FCGR1A, FCGR1B, FCGR1C, FcRI, FcRIB, FCRIC, FLJ18345, HFcgammaRIB, High affinity immunoglobulin gamma Fc receptor I, High affinity immunoglobulin gamma Fc receptor IB, IGFR 1, IGFR1, IGFRB, IGFRC, IgG Fc receptor I, IgG Fc receptor IB, IgG Fc receptor IC, Immunoglobulin G Fc receptor I, Immunoglobulin G Fc receptor IB, Immunoglobulin G Fc receptor IC, MGC137713

Isotype Controls

Mouse IgG1 [MOPC-21] (FITC) (A86205)

Disclaimer

This product is for research use only. It is not intended for diagnostic or therapeutic use.

Scientific Validation Data (1)

Enlarge Image

Figure 1: Flow Cytometry - Anti-CD64 Antibody [10.1] (FITC) (A86157)

Surface staining of CD64 in human peripheral blood with Anti-CD64 Antibody (A86157).

Citations for this Clone (5)

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Intracellular cytokine profile of cord and adult blood monocytes.

References: Anti-CD64 Antibody [10.1] (FITC) (ab119828)

Abstract:

Cord blood (CB) transplantations are associated with low graft-versus-host disease (GVHD). The pathophysiology of GVHD involves interaction and activation of different cell types, as lymphocytes and monocytes, and results in a cascade of cytokine production. After antigen or mitogen stimulation, CB monocytes release lower levels of cytokines than adult blood (AB) monocytes. In this study, the detection of intracellular IL-1 beta and TNF-alpha produced by monocytes was evaluated in response to tuberculin PPD to investigate whether the reduced capacity of CB monocytes to secrete cytokines could be related to an impaired functional activity and to a particular phenotypic profile. Results showed that the percentage of CD64(+)monocytes producing intracellular IL-1 beta and TNF-alpha was significantly lower in CB and that the phenotypic profile of CB monocytes producing these cytokine (CD64(+)CD14(+)) was different to that of AB monocytes (CD64(+)CD14(+), CD64(+)CD33(+) and CD64(+) CD45RO(+)). These results suggest that the lower capacity of CB monocyte populations to produce IL-1 beta and TNF-alpha might be due to a functional immaturity of CB monocytes at the cellular level as reflected by the different phenotypic profile of CB monocytes.

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High affinity IgG binding by FcgammaRI (CD64) is modulated by two distinct IgSF domains and the transmembrane domain of the receptor.

References: Anti-CD64 Antibody [10.1] (FITC) (ab93500)

Abstract:

The high affinity IgG receptor, FcgammaRI, is comprised of three immunoglobulin superfamily (IgSF) domains (EC1, EC2 and EC3), a single transmembrane spanning region, and a short cytoplasmic tail. We have shown a role for three separate domains of FcgammaRI in the high affinity binding of IgG. Affinity measurements of chimeric FcgammaRs in which EC1 and EC2 of FcgammaRI have been replaced with the homologous EC1 and/or EC2 domains of the low affinity IgG receptor, FcgammaRII indicate that both EC2 and EC3 are essential for high affinity binding of monomeric IgG. Identification of EC3 from FcgammaRI as the binding site for the monoclonal antibody 10.1, which blocks IgG binding, provides further evidence for the role of this domain in binding. In addition, we have found that the affinity of FcgammaRI is increased threefold when co-expressed with its accessory molecule, gamma-chain. Affinity measurements of further chimeras indicates that the transmembrane domain of FcgammaRI has a negative influence upon the affinity of the receptor. To account for these observations, we propose that receptor dimerization is required for maximal affinity of FcgammaRI. Dimerization may serve as the mechanism by which IgG binding triggers several FcgammaRI-mediated events.

View Publication

Enhancement of macrophage colony-stimulating factor-induced growth and differentiation of human monocytes by interleukin-10.

References: Anti-CD64 Antibody [10.1] (FITC) (ab119828)

Abstract:

Interleukin-10 (IL-10) has been reported to be a negative cytokine for monocytes/macrophages. In the present study, we showed that IL-10 is rather a positive cytokine and augments the growth and differentiation of human monocytes stimulated with macrophage colony-stimulating factor (M-CSF). Highly purified adherent human monocytes were cultured for 7 days with M-CSF in the presence or absence of IL-10. The number of recovered cells increased in the culture of monocytes with M-CSF + IL-10 compared to the culture with M-CSF alone. IL-10 alone was not enough to maintain the survival and differentiation of monocytes into macrophages. Morphological change cultured in M-CSF was also accelerated by addition of IL-10, and macrophages cultured in M-CSF + IL-10 were more elongated compared to macrophages cultured with M-CSF alone. Binding of 125I-M-CSF to monocytes incubated with M-CSF + IL-10 was about 1.7-fold higher than that to monocytes incubated with M-CSF alone. In accordance with the binding study, Northern blot analysis showed that the levels of the expression of c-fms, M-CSF receptor, mRNA in macrophages cultured in M-CSF + IL-10 were higher than that in macrophages cultured in M-CSF alone. Macrophages cultured in M-CSF + IL-10 expressed higher level of Fc gamma RI, II, III, and showed augmented Fc gamma receptor mediated phagocytosis. The former also produced higher level of H2O2 and O2-, when stimulated with zymosan, and of IL-6 when stimulated with lipopolysaccharide compared to the latter. These results taken together suggest that IL-10 augments the growth and differentiation of human monocytes cultured in M-CSF.

View Publication

The human mononuclear phagocyte high-affinity Fc receptor, FcRI, defined by a monoclonal antibody, 10.1.

References: Anti-CD64 Antibody [10.1] (FITC) (ab119828)

Abstract:

The properties of the mononuclear phagocyte (Mph) high-affinity Fc receptor, FcRI, were investigated using a novel monoclonal antibody (mAb) designated 10.1. This receptor was shown to be a protein of 71 kDa, presented chiefly on monocytes and the myeloid cell lines U937 and HL60. mAb 10.1 inhibited the binding to Mph of erythrocytes opsonized with rabbit IgG or human IgG3. It also blocked T cell proliferation induced by murine CD3 mAb of the IgG2a but not the IgG1 subclass. These results suggest that rabbit IgG, human IgG3 and murine IgG2a all bind to FcRI in a similar manner and that mAb 10.1 reacts with an epitope on FcRI near to the binding site for the Fc region of IgG. In addition, although it is well known that FcRI has a high affinity for both monomeric human IgG1 and IgG3, we show in this study that while erythrocytes opsonized with human IgG3 bind to Mph, equivalent cells opsonized with IgG1 surprisingly do not. These results define further the nature of the constraints on the interaction between Mph FcRI and particular IgGs.

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The Fc receptor, FcRI, and other activation molecules on human mononuclear phagocytes after treatment with interferon-gamma.

References: Anti-CD64 Antibody [10.1] (FITC) (ab119828)

Abstract:

Human monocytes and the myeloid cell lines U937 and HL60 have been tested with monoclonal antibodies (MoAbs) reactive with 22 different cell surface molecules before and after treatment with interferon-gamma (IFN-gamma). An increase in the expression of the high affinity Fc receptor, FcRI, and the receptor for interleukin 2, IL-2R, were the most consistent alterations which were observed. In addition, expression of the gp55 molecule recognized by CD14 MoAbs was decreased on monocytes. Of the MHC Class II molecules, there was little expression by the myeloid cell lines and no enhancement after IFN-gamma treatment. In contrast monocytes expressed all three MHC Class II subloci with DR much greater than DQ and DP. However there was much variation in IFN-gamma-mediated increase in expression of the individual subregions. In monocytes, the alteration in expression of FcRI, IL-2R, gp55 and MHC Class II molecules took place in a co-ordinate fashion and reached a plateau only after 48 h. In U937 cells, activation proceeded more rapidly and was at maximum levels between 12-16 h. This increase in FcRI appears to be a hallmark of IFN-gamma activation for mononuclear phagocytes (Mph) as the other alterations are either not found on all types of Mph (gp55, MHC Class II) or are induced by other cytokines on Mph and on other cells (IL-2R, MHC Class II). Conversely, other cytokines do not induce FcRI on Mph. These results also suggest that the cell membrane phenotypic changes induced in Mph by IFN-gamma may not be extensive and that FcRI must play a specific role in the IFN-gamma-activated Mph.

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