Description
Recombinant Mouse Legumain/LGMN Protein (His Tag)(Active) | PKSM040307 | Gentaur US, UK & Europe Disrtribition
Synonyms: Legumain;Lgmn;Asparaginyl endopeptidase;Protease cysteine 1;Prsc1;AEP
Active Protein: Active protein
Activity: A DNA sequence encoding the extracellular domain (Val 18-Tyr 435) of mouse LGMN (NP_035305.1) precursor was expressed with a C-terminal polyhistidine tag.
Protein Construction: A DNA sequence encoding the extracellular domain (Val 18-Tyr 435) of mouse LGMN (NP_035305.1) precursor was expressed with a C-terminal polyhistidine tag.
Fusion Tag: C-His
Species: Mouse
Expressed Host: HEK293 Cells
Shipping: This product is provided as lyophilized powder which is shipped with ice packs.
Purity: > 75 % as determined by reducing SDS-PAGE.
Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method.
Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.
Molecular Mass: 49.8 kDa
Formulation: Lyophilized from sterile 25mM Tris, 0.15M NaCl, 20% Glycerol, pH 7.5
Reconstitution: Please refer to the printed manual for detailed information.
Background: The Mammalian Legumain, also known as LGMN, also called asparaginyl endopeptidase (AEP), is a cysteine protease belonging to peptidase family C13 with a strict specificity for hydrolysis of asparaginyl bonds. Known previously only from plants and invertebrates, Legumain is discovered as a lysosomal endopeptidase in mammals. Mammalian Legumain is a cysteine endopeptidase, inhibited by iodoacetamide and maleimides, but unaffected by compound E64. The Mammalian Legumain is involved in the processing of bacterial peptides and endogenous proteins for MHC class II presentation in the lysosomal/endosomal systems. Legumain has been observed to be highly expressed in several types of solid tumors. It was demonstrated in membrane-associated vesicles concentrated at the invadopodia of tumor cells and on cell surfaces where it colocalized with integrins. Legumain was demonstrated to activate progelatinase A. Cells overexpressing Legumain possessed increased migratory and invasive activity in vitro and adopted an invasive and metastatic phenotype in vivo, inferring significance of Legumain in tumor invasion and metastasis. In addition, Legumain is expressed in both murine and human atherosclerotic lesions. The macrophage-specific expression of Legumain in vivo and ability of Legumain to induce chemotaxis of monocytes and endothelial cells in vitro suggest that Legumain may play a functional role in atherogenesis.
Research Area: N/A
