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Merck
모든 사진(2)

주요 문서

M7060

Sigma-Aldrich

Monoclonal Anti-Moesin antibody produced in mouse

clone 38/87, purified immunoglobulin, buffered aqueous solution

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About This Item

MDL number:
UNSPSC 코드:
12352203
NACRES:
NA.41

생물학적 소스

mouse

Quality Level

결합

unconjugated

항체 형태

purified immunoglobulin

항체 생산 유형

primary antibodies

클론

38/87, monoclonal

형태

buffered aqueous solution

분자량

antigen 78-80 kDa

종 반응성

human, bovine, rat, mouse, pig

기술

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

동형

IgG1

UniProt 수납 번호

저장 온도

−20°C

타겟 번역 후 변형

unmodified

유전자 정보

human ... MSN(4478)
mouse ... Msn(17698)
rat ... Msn(81521)

특이성

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.

면역원

bovine uterus moesin.

애플리케이션

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.

생화학적/생리학적 작용

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.

물리적 형태

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

면책조항

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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Storage Class Code

10 - Combustible liquids


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문서 라이브러리 방문

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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