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Anti-FCAMR (CD351), clone TX61, Cat. No. MABF2329, is a mouse monoclonal antibody that detects FCAMR and is tested for use in Flow Cytometry, Immunoprecipitation, Immunohistochemistry, and Inhibitor/Function Analysis.
More>>Anti-FCAMR (CD351), clone TX61, Cat. No. MABF2329, is a mouse monoclonal antibody that detects FCAMR and is tested for use in Flow Cytometry, Immunoprecipitation, Immunohistochemistry, and Inhibitor/Function Analysis. Less<<
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Übersicht
Replacement Information
Description
Catalogue Number
MABF2329-100UL
Description
Anti-FCAMR (CD351) Antibody, clone TX61
Alternate Names
High affinity immunoglobulin alpha and immunoglobulin mu Fc receptor
Fc alpha/mu receptor
Fcα/μR
CD351
Background Information
High affinity immunoglobulin alpha and immunoglobulin mu Fc receptor (UniProt: Q2TB54; also known as Fc alpha/mu receptor, FcamR, CD351) is encoded by the Fcamr gene (Gene ID: 64435) in murine species. FcamR is a single-pass type I membrane protein that functions as a receptor for the Fc fragment of IgA and IgM. It binds with IgM with high affinity (Kd = 1.2 nM) and with IgA with reduced affinity (Kd = 10-18 nM). It is expressed in several tissues including thymus, spleen, liver, kidney, small and large intestine, testis and placenta. Its expression has also been shown in oligodendrocytes, B-cells, and macrophages. FcamR binds IgA and IgM with high affinity and mediates their endocytosis and may also function in the immune response to microbes mediated by IgA and IgM. FcamR is synthesized with a signal peptide (aa 1-35), which is subsequently cleaved off to generate the mature form that contains an extracellular domain (aa 36-455), a transmembrane domain (aa 456-476), and a cytoplasmic domain (aa 477-535). The amino acid region 504-523 is reported to be essential for its cell-surface expression and region 481-490 is required for heterodimer formation. The dimer is shown to be resistant to boiling ins SDS land to reduction by 2-mercaptoethanol. (Ref.: Takagaki, K., et al. (2013). Mol. Immunol. 56(1-2); 23-27; Yang, X., et al. (2013). Immunobiology. 218(5); 798-809).
References
Product Information
Format
Purified
Presentation
Purified mouse monoclonal antibody IgG1 in PBS without azide.
Applications
Application
Anti-FCAMR (CD351), clone TX61, Cat. No. MABF2329, is a mouse monoclonal antibody that detects FCAMR and is tested for use in Flow Cytometry, Immunoprecipitation, Immunohistochemistry, and Inhibitor/Function Analysis.
Key Applications
Flow Cytometry
Immunoprecipitation
Immunohistochemistry
Affects Function
Application Notes
Inhibits Activity/Function Analysis: A representative lot inhibited ligand binding to FCAMR (CD351). (Cho, Y., et. al. (2006). Biochem Biophys Res Commun. 345(1):474-8).
Flow Cytometry Analysis: A representative lot detected FCAMR (CD351) in Flow Cytometry applications (Anquetil, F., et. al. (2015). J Immunol. 194(8):3664-74; Takaqaki, K., et. al. (2013). Mol Immunol. 56(1-2):23-7; Honda, S., et. al. (2009). Proc Natl Acad Sci U S A. 106(27):11230-5).
Immunocytochemistry Analysis: A representative lot detected FCAMR (CD351) in Immunohistochemistry applications (Honda, S., et. al. (2009). Proc Natl Acad Sci U S A. 106(27):11230-5; Kurita, N., et. al. (2015). Mol Immunol. 63(2):367-72).
Immunoprecipitation Analysis: A representative lot immunoprecipitated FCAMR (CD351) in Immunoprecipitation applications (Takaqaki, K., et. al. (2013). Mol Immunol. 56(1-2):23-7).
Note: Actual optimal working dilutions must be determined by end user as specimens, and experimental conditions may vary with the end user
Biological Information
Immunogen
Ba/F3 cells transfected with murine FCAMR.
Epitope
extracellular domain
Clone
TX61
Concentration
0.5 mg/mL. Please refer to guidance on suggested starting dilutions and/or titers per application and sample type.
Host
Mouse
Specificity
Clone TX61 is a mouse monoclonal antibody that detects High affinity immunoglobulin alpha and immunoglobulin mu Fc receptor (FCAMR). It targets an epitope within the extracellular domain.
Evaluated by Flow Cytometry in BW5147 cells transfected with mouse FCAMR.
Flow Cytometry Analysis: 1 µg of this antibody detected FCAMR (CD351) in BW5147 cells transfected with mouse FCAMR.
Usage Statement
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.
Storage and Shipping Information
Storage Conditions
Stable for 1 year at -20°C from date of receipt. Handling Recommendations: Upon receipt and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance.
Increased serum IgA in Fcα/μR-deficient mice on the (129 x C57BL/6) F1 genetic background. Kurita N, Honda S, Shibuya A. Mol Immunol
63(2)
367-72
2015
Fcα/μR (CD351) is an Fc receptor for both IgA and IgM, which is abundantly expressed in the small intestine. However, the role of Fcα/μR in the intestinal tissue is largely unknown. Here, we found that Fcα/μR is highly expressed on follicular dendritic cells (FDCs) in Peyer's patches (PP) in the small intestine. Fcα/μR-deficient mice on the (129 x C57BL/6) F1 background showed increased serum, but not fecal, IgA level in response to gut-oriented antigens. IgA(+) B cells were increased in PP, but not in the lamina propria, of Fcα/μR-deficient mice, which was attenuated after reduction of commensal microbiota by oral treatment with antibiotics. Analyses of bone marrow chimeric mice, in which either FDCs or blood cells or both lack the expression of Fcα/μR, suggested that FDCs, but not blood cells, were responsible for the increased serum IgA concentration in Fcα/μR-deficient mice. Moreover, Fcα/μR-deficient mice showed enhanced germinal center formation against commensal microbiota in PP. Thus, serum IgA production against gut-oriented antigens is negatively regulated by Fcα/μR on FDCs in the F1 mice.
IgM and IgA rheumatoid factors purified from rheumatoid arthritis sera boost the Fc receptor- and complement-dependent effector functions of the disease-specific anti-citrullinated protein autoantibodies. Anquetil F, Clavel C, Offer G, Serre G, Sebbag M. J Immunol
194(8)
3664-74
2015
Rheumatoid factors (RF) and the disease-specific anti-citrullinated protein autoantibodies (ACPA) coexist in the joints of rheumatoid arthritis (RA) patients where they probably contribute to synovitis. We investigated the influence of IgM and IgA RF on the FcR- and complement-dependent effects of ACPA immune complexes (ACPA-IC). When stimulated by ACPA-IC formed in the presence of IgM RF or IgA RF fractions purified from RA serum pools, M-CSF-generated macrophages skewed their cytokine response toward inflammation, with increases in the TNF-α/IL-10 ratio and in IL-6 and IL-8 secretion, and decreases in the IL-1Ra/IL-1β ratio. In the IgM RF-mediated amplification of the inflammatory response of macrophages, the participation of an IgM receptor was excluded, notably by showing that they did not express any established receptor for IgM. Rather, this amplification depended on the IgM RF-mediated recruitment of more IgG into the ACPA-IC. However, the macrophages expressed FcαRI and blocking its interaction with IgA inhibited the IgA RF-mediated amplification of TNF-α secretion induced by ACPA-IC, showing its major implication in the effects of RF of the IgA class. LPS further amplified the TNF-α response of macrophages to RF-containing ACPA-IC. Lastly, the presence of IgM or IgA RF increased the capacity of ACPA-IC to activate the complement cascade. Therefore, specifically using autoantibodies from RA patients, the strong FcR-mediated or complement-dependent pathogenic potential of IC including both ACPA and IgM or IgA RF was established. Simultaneous FcR triggering by these RF-containing ACPA-IC and TLR4 ligation possibly makes a major contribution to RA synovitis.
Fcα/μR (CD351) is an Fc receptor for both IgA and IgM and forms an atypical dimer that is resistant to reduction by 2-mercaptoethanol or boiling. We previously demonstrated that the cytoplasmic portion of Fcα/μR is required for dimer formation and for its efficient cell-surface expression. However, the biochemical nature of these phenomena has not been determined. By using a BW5147 mouse cell line expressing deletion mutants of the cytoplasmic region of Fcα/μR, we found that the region spanning amino acids 504-523 was required for efficient cell-surface expression, whereas the region spanning amino acids 481-490 was required for dimmer formation. Immunoblotting analyses of transfectants simultaneously expressing Flag-tagged Fcα/μR and hemagglutinin-tagged Fcα/μR suggested that Fcα/μR does not form homodimers. Instead, our data suggest that Fcα/μR forms heterodimers with an as-yet-unknown molecule with a molecular weight of 60-70 kDa.
Enhanced humoral immune responses against T-independent antigens in Fc alpha/muR-deficient mice. Honda S, Kurita N, Miyamoto A, Cho Y, Usui K, Takeshita K, Takahashi S, Yasui T, Kikutani H, Kinoshita T, Fujita T, Tahara-Hanaoka S, Shibuya K, Shibuya A. Proc Natl Acad Sci U S A
106(27)
11230-5
2009
IgM is an antibody class common to all vertebrates that plays a primary role in host defenses against infection. Binding of IgM with an antigen initiates the complement cascade, accelerating cellular and humoral immune responses. However, the functional role of the Fc receptor for IgM in such immune responses remains obscure. Here we show that mice deficient in Fc alpha/muR, an Fc receptor for IgM expressed on B cells and follicular dendritic cells (FDCs), have enhanced germinal center formation and affinity maturation and memory induction of IgG3(+) B cells after immunization with T-independent (TI) antigens. Moreover, Fc alpha/muR-deficient mice show prolonged antigen retention by marginal zone B (MZB) cells and FDCs. In vitro studies demonstrate that interaction of the IgM immune complex with Fc alpha/muR partly suppress TI antigen retention by MZB cells. We further show that downregulation of complement receptor (CR)1 and CR2 or complement deprivation by in vivo injection with anti-CR1/2 antibody or cobra venom factor attenuates antigen retention by MZB cells and germinal center formation after immunization with TI antigens in Fc alpha/muR(-/-) mice. Taken together, these results suggest that Fc alpha/muR negatively regulates TI antigen retention by MZB cells and FDCs, leading to suppression of humoral immune responses against T-independent antigens.
Molecular characteristics of IgA and IgM Fc binding to the Fcalpha/muR. Cho Y, Usui K, Honda S, Tahara-Hanaoka S, Shibuya K, Shibuya A. Biochem Biophys Res Commun
345(1)
474-8
2005
Fcalpha/mu receptor (Fcalpha/muR), a novel Fc receptor for IgA and IgM, is a type I transmembrane protein with an immunoglobulin (Ig)-like domain in the extracellular portion. Although IgA and IgM bind to Fcalpha/muR, the molecular and structural characteristics of the ligand-receptor interactions have been undetermined. Here, we developed twelve monoclonal antibodies (mAbs) against murine Fcalpha/muR by immunizing mice deficient in Fcalpha/muR gene. Eight mAbs totally or partially blocked IgA and IgM bindings to Fcalpha/muR. These blocking mAbs bound to a peptide derived from the Ig-like domain of murine Fcalpha/muR, which is conserved not only in human and rat Fcalpha/muR but also in polymeric Ig receptor (poly-IgR), another Fc receptor for IgA and IgM. These results suggest that IgA and IgM bind to an epitope in the conserved amino acids in the Ig-like domain of Fcalpha/muR as well as poly-IgR.