M7060
Monoclonal Anti-Moesin antibody produced in mouse
clone 38/87, purified immunoglobulin, buffered aqueous solution
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About This Item
Productos recomendados
origen biológico
mouse
conjugado
unconjugated
forma del anticuerpo
purified immunoglobulin
tipo de anticuerpo
primary antibodies
clon
38/87, monoclonal
Formulario
buffered aqueous solution
mol peso
antigen 78-80 kDa
reactividad de especies
human, bovine, rat, mouse, pig
técnicas
flow cytometry: suitable
immunocytochemistry: suitable
immunohistochemistry (formalin-fixed, paraffin-embedded sections): suitable
immunoprecipitation (IP): suitable
indirect ELISA: suitable
western blot: 0.5-1 μg/mL using whole extract of cultured human acute T cell leukemia Jurkat cells
isotipo
IgG1
Nº de acceso UniProt
temp. de almacenamiento
−20°C
modificación del objetivo postraduccional
unmodified
Información sobre el gen
human ... MSN(4478)
mouse ... Msn(17698)
rat ... Msn(81521)
Especificidad
Mouse monoclonal clone 38/87 anti-Moesin antibody recognizes the 78 kDa moesin and 80 kDa radixin molecules. It does not react with talin or ezrin. Reactivity has been reported with human, bovine, porcine, rat and mouse moesin.
Inmunógeno
bovine uterus moesin.
Aplicación
Mouse monoclonal clone 38/87 anti-Moesin antibody may be used for ELISA, immunoblotting (a closely spaced doublet of 78/80 kDa) immunoprecipitation, immunohistochemistry (reported for frozen sections and for formalin-fixed paraffin-embedded sections following boiling in 0.01M citrate buffer pH 6), immunocytochemistry (3.7% paraformaldehyde, 0.1% Triton X-100), flow cytometry (3-3.7% paraformaldehyde, 0.1-0.25% Triton X-100) and electron microscopy. The intensity of the fainter doublet‘s upper band seen in immunoblotting varies depending on the tissue. The antibody has been used to inhibit both the binding of proteoheparan sulfate to smooth muscle cells, and the infectivity of measles virus.
Acciones bioquímicas o fisiológicas
The ERM (ezrin-radixin-moesin) proteins, members of the talin-protein 4.1- merlin/schwannomin superfamily, are general cross-linkers between the plasma membrane and actin filaments. They provide such links through their N-terminal halves that associate with integral membrane proteins either directly or indirectly through adapter molecules, and through their C-terminal halves that associate with F-actin. ERM proteins are involved not only in cytoskeletal organization but also in signal transduction and apoptosis. Because their expression is regulated in a tissue-specific manner, each ERM protein has been proposed to have unique functions. There is approximately 80% homology between moesin, ezrin and radixin. These proteins are involved in a variety of cellular functions, such as cell adhesion, migration, and the organization of cell surface structures. However, moesin (in contrast to radixin and ezrin) is strongly expressed in endothelium of vessels, in T and B lymphocytes, in basal layers of squamous epithelium and glandular ducts, and in cells of carcinoma and mesothelioma. Moesin is expressed in variable amounts in cells of different phenotypes such as macrophages, lymphocytes, fibroblastic, endothelial, epithelial, and neuronal cell lines. It is overexpressed in some estrogen receptor (ER)-negative cell lines but absent from ER-positive ones, suggesting that it may play a role in the invasiveness and pattern of metastasis characteristic of ER-negative breast cancers.
Forma física
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
Cláusula de descargo de responsabilidad
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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Código de clase de almacenamiento
10 - Combustible liquids
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Mei Wang et al.
International journal of biological sciences, 18(3), 942-955 (2022-02-18)
Glioblastoma (GBM) is a highly vascularized malignant tumor that depends on new blood vessel formation. Small molecules targeting the angiogenic process may be an effective anti-GBM therapeutic strategy. We previously demonstrated that RhoJ promoted the progression and invasion of GBM.
L M Dunster et al.
The Journal of general virology, 76 ( Pt 8), 2085-2089 (1995-08-01)
Membrane cofactor protein (CD46) has been firmly established as the major high affinity receptor for measles virus (MV). In addition, another protein, moesin, has been shown to be linked with the susceptibility of human cells to MV infection. Murine cells
M R Amieva et al.
Experimental cell research, 219(1), 180-196 (1995-07-01)
Moesin, a member of the talin-4.1 superfamily, is a linking protein of the submembraneous cytoskeleton. It is expressed in variable amounts in cells of different phenotypes such as macrophages, lymphocytes, fibroblastic, endothelial, epithelial, and neuronal cell lines. In this report
A Ametzazurra et al.
Human reproduction (Oxford, England), 24(4), 954-965 (2008-12-20)
The development of non-invasive diagnostic methods for endometriosis requires sensitive and disease specific biomarkers. Here, we describe the use of aspirated endometrial fluid from women with and without endometriosis as a novel biological sample for biomarker discovery. Differential protein expression
F Nakamura et al.
Molecular biology of the cell, 10(8), 2669-2685 (1999-08-06)
Activation of human platelets with thrombin transiently increases phosphorylation at (558)threonine of moesin as determined with phosphorylation state-specific antibodies. This specific modification is completely inhibited by the kinase inhibitor staurosporine and maximally promoted by the phosphatase inhibitor calyculin A, making
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