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SRP5208

Sigma-Aldrich

Moesin (410-end), GST tagged human

recombinant, expressed in E. coli, ≥70% (SDS-PAGE), buffered aqueous glycerol solution

Synonym(s):

MSN

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About This Item

UNSPSC Code:
12352202
NACRES:
NA.32

recombinant

expressed in E. coli

Assay

≥70% (SDS-PAGE)

form

buffered aqueous glycerol solution

mol wt

~50 kDa

NCBI accession no.

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... MSN(4478)

General description

Moesin (or membrane-organizing extension spike protein) belongs to ERM family that modulates epithelial integrity by regulating cell-signalling events that affect actin organization and polarity. The effects of Moesin on epithelial cells appear to result from inhibition of Rho signaling. ERM proteins serve a structural role in linkage of the cytoskeletion to the plasma membrane and the rescue of cells lacking Moesin by modulation of Rho signaling indicates that inhibition of Rho activity may be a more critical function of Moesin. The negative feedback loop produced by Rho′s activation of ERM may be an important mechanism that prevents the excessive migratory and invasive properties characteristic of metastatic cancer cells.

Physical form

Supplied in 50mM Tris-HCl, pH 7.5, 150mM NaCl, 10mM glutathione, 0.1mM EDTA, 0.25mM DTT, 0.1mM PMSF, 25% glycerol.

Preparation Note

after opening, aliquot into smaller quantities and store at -70 °C. Avoid repeating handling and multiple freeze/thaw cycles

Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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Olga Speck et al.
Nature, 421(6918), 83-87 (2003-01-04)
Two prominent characteristics of epithelial cells, apical-basal polarity and a highly ordered cytoskeleton, depend on the existence of precisely localized protein complexes associated with the apical plasma membrane, and on a separate machinery that regulates the spatial order of actin
W T Lankes et al.
Proceedings of the National Academy of Sciences of the United States of America, 88(19), 8297-8301 (1991-10-01)
Moesin (membrane-organizing extension spike protein, pronounced mó ez in) has previously been isolated from bovine uterus and characterized as a possible receptor protein for heparan sulfate. We now have cloned and sequenced its complete cDNA, which represents a single 4.2-kilobase

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