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Mouse Cathepsin E / CTSE Protein (His Tag)

A430072O03Rik,C920004C08Rik,CatE,CE

Catalog Number P50564-M08H
Organism Species Mouse
Host Human Cells
Synonyms A430072O03Rik,C920004C08Rik,CatE,CE
Molecular Weight The secreted recombinant mouse CTSE (pro form) consists of 390 amino acids and has a predicted molecular mass of 42.4 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rmCTSE is approximately 45-48 kDa due to glycosylation.
predicted N Gln 19
SDS-PAGE
Purity > 97 % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the extracellular domain of mouse CTSE (NP_031825.2) (Met 1-Pro 397) was expressed, with a polyhistidine tag at the C-terminus.
Bio-activity
Research Area Immunology |Inflammation / Inflammatory Mediator |Lysosomal Enzymes
Formulation Lyophilized from sterile PBS, pH 7.4
1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background Cathepsin E Protein (CTSE Protein) is a member of the peptidase C1 family that is a gastric aspartic protease that functions as a disulfide-linked homodimer. Cathepsin E Protein (CTSE Protein) is predominantly present in the cells of immune system and is frequently implicated in antigen processing via the MHC classⅡ pathway which however does not appear to be involved in the digestion of dietary protein. The protein has a specificity similar to that of pepsin and pepsin. Cathepsin E Protein (CTSE Protein) is found in highest concentration in the surface of epithelial mucus-producing cells of the stomach and also been found in more than half of the gastric cancers. It appears, therefore, to be an oncofetal antigen.
Reference
  • Zaidi N, et al. (2008) Emerging functional foles of cathepsin E. Biochem Biophys Res Commun. 377(2) : 327-30.
  • Zaidi N, et al. (2008) Cathepsin E: a mini review. Biochem Biophys Res Commun. 367(3) :517-22.
  • Azuma T, et al. (1989) Human gastric cathepsin E Predicted sequence, localization to chromosome 1, and sequence homology with other aspartic proteinases.The journal of biological chemistry. 264: 16748-53.