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Human MSN / Moesin Protein (aa 1-346, His Tag)

HEL70

Catalog Number P13659-H07E
Organism Species Human
Host E. coli
Synonyms HEL70
Molecular Weight The recombinant human MSN consists of 361 amino acids and has a calculated molecular mass of 42.8 kDa. It migrates as an approximately 45 kDa band in SDS-PAGE under reducing conditions.
predicted N Met
SDS-PAGE
Purity > 80 % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the human MSN (P26038) (Met 1-Glu 346) was expressed, with a polyhistidine tag at the N-terminus.
Bio-activity
Research Area Signaling |Signal Transduction |Cytoskeleton / ECM |Cytoskeletal Proteins |Microfilaments |Talin / Moesin |
Formulation Lyophilized from sterile 20mM Tris, 0.5M NaCl, pH 8.0
1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background Moesin is a member of the ERM family which includes ezrin and radixin. ERM proteins, highly related members of the larger protein 4.1 superfamily, can exist in an active or inactive conformation. It seems that ERM proteins function as cross-linkers between plasma membranes and actin-based cytoskeletons. The sole Drosophila ERM protein, moesin, functions to promote cortical actin assembly and apical-basal polarity. As a result, cells lacking moesin lose epithelial characteristics and adopt invasive migratory behaviour. It is localized to filopodia and other membranous protrusions that are important for cell-cell recognition and signaling and for cell movement. Moesin contains 1 FERM domain and is expressed in all tissues and cultured cells studied. Moesin has been shown to interact with CD43, Neutrophil cytosolic factor 1, VCAM-1, Neutrophil cytosolic factor 4, ICAM3 and EZR.
Reference
  • Lankes WT, et al. (1991) Moesin: a member of the protein 4.1-talin-ezrin family of proteins. Proc Natl Acad Sci. 88(19):8297-301.
  • Serrador, J M, et al. (1998) CD43 interacts with moesin and ezrin and regulates its redistribution to the uropods of T lymphocytes at the cell-cell contacts. Blood. 91(12):4632-44.
  • Barreiro Olga, et al. (2002) Dynamic interaction of VCAM-1 and ICAM-1 with moesin and ezrin in a novel endothelial docking structure for adherent leukocytes. J Cell Biol. 157(7):1233-45.