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MABF838

Sigma-Aldrich

Anti-FcgRII/III Anibody, clone Ab93

clone 93, from rat

Synonym(s):

Low affinity immunoglobulin gamma Fc region receptor III, IgG Fc receptor III, Fc-gamma RIII, FcRIII, CD16, FcgRII/III, Low affinity immunoglobulin gamma Fc region receptor II, Fc gamma receptor IIB, Fc-gamma RII, Fc-gamma-RIIB, FcRII, IgG Fc receptor II

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

Key Documents

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biological source

rat

Quality Level

100

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

93, monoclonal

species reactivity

mouse

technique(s)

activity assay: suitable
flow cytometry: suitable
immunocytochemistry: suitable

isotype

IgG2aκ

NCBI accession no.

NP_034317

UniProt accession no.

P08101
P08508

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

mouse ... Fcgr2b(14130), Fcgr3(14131)

Related Categories

General description

33.4 kDa (mature FcgRII) & 26.7 kDa (mature FcgRIII) calculated.
Murine low affinity IgG Fc region receptor FcγRII and FcγRIII (UniProt P08101 and P08508, respectively) are encoded by the Fcgr2 (also known as Fcgr2b, Ly-17) and Fcgr3 gene, respectively. Four different classes of IgG Fc receptors (FcγRs) have been reported: FcγRI/CD32b, FcγRII/CD16, FcγRIII/CD16.2, and FcγRIV/CD64. FcγRII, FcγRIII, and FcγRIV (UniProt P08101, P08508, and Q8R477, respectively) are low-affinity receptors for monomeric IgG, whereas FcγRI (UniProt P26151) is the only high-affinity FcγR. FcγRs play important roles in inflammatory cell activation, clearance, presentation of antigen, and maintenance of IgG homeostasis. In addition to binding immune complex (IC), FcγRs have been shown to bind to non-IgG ligands. For example, FcγRII is shown to bind oxLDL, while FcγRIII binding to an E. coli component negatively regulates the function of macrophage receptor with collagenous structure (MARCO). FcyRII activation is also reported to transduce a negative regulatory signal against CD38 cross-linking-induced proliferation of resting mature B cells.

Immunogen

Whole cells expressing mouse FcgRII/III.

Application

Flow Cytometry Analysis: A representative lot stained murine A20 B-cell lymphoma cells, but not the FcgammaRIl-deficient A20-IIA1.6 variant (Oliver, A.M., et al. (1999). Hybridoma 18(2):113-119).
Activity Assay Analysis: A representative lot prevented CD38-mediated proliferation of spleen-derived primary murine B-cells from wild-type, but not FcgammaRIl-deficient mice (Oliver, A.M., et al. (1999). Hybridoma 18(2):113-119).
Immunocytochemistry Analysis: A representative lot detected FcgRII association with cross-linkinked CD38 following anti-CD38 addition to cultured primary murine B-cells by fluorescent immunocytochemistry (Oliver, A.M., et al. (1999). Hybridoma 18(2):113-119).
This Anti-FcgRII/III Anibody, clone Ab93 is validated for use in Flow Cytometry, Immunocytochemistry, Activity Assay for the detection of FcgRII/II.

Biochem/physiol Actions

Recognizes both FcgammaRII and FcgammaRIII.

Physical form

Format: Purified
Purified rat monoclonal IgG2ak antibody in PBS without preservatives.

Analysis Note

Evaluated by Flow Cytometry in mouse splenocytes.

Flow Cytometry Analysis: 5.0 µg of this antibody detected FcgRII/III in mouse splenocytes.

Other Notes

Concentration: Please refer to lot specific datasheet.

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Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

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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Related Content

White Paper: Further considerations of antibody validation and usage.
Characterization of Estrogen Receptor α Phosphorylation Sites in Breast Cancer Tissue Using the SNAP i.d® 2.0 System

A major focus of breast cancer research is to understand the mechanisms responsible for disease progression and drug resistance. Toward that end, it has been found that approximately two thirds of all human breast carcinomas overexpress the Estrogen Receptor α (ERα) protein and it remains the primary pharmacological target for endocrine therapy1,2. The normal cellular function of ERα is as a transcription factor that mediates a wide variety of physiological processes, many of which are dependent upon phosphorylation of the receptor at specific amino acid residues3,4. Indeed, ERα is known to be phosphorylated at a multitude of different sites, yet how these all correlate to disease remains unclear5. Here, we interrogated multiple sites of ERα for phosphorylation status by screening an extensive panel of different breast cancer patient samples and other non-breast cancer tissue microarray (TMA) slide samples to determine their relevance to disease.

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