The cathepsin family of proteolytic enzymes contains several diverse classes of proteases. The cysteine protease class comprises cathepsins B, L, H, K, S and O. The aspartyl protease class is composed of cathepsins D and E. Cath-epsin G is in the serine protease class. Most cathepsins are lysosomal and each is involved in cellular metabolism, participating in various events such as peptide biosynthesis and protein degradation. Cathepsin E is a nonlysosomal, intracellular proteinase.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of cathepsin E of mouse, rat and human origin by WB, IP, IF and ELISA also reactive with additional species, including equine and canine
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 141-180 mapping within an internal region of cathepsin E of human origin
Tissue Specificity
epitope corresponding to amino acids 141-180 mapping within an internal region of cathepsin E of human origin
Western blot analysis of cathepsin E expression in non-transfected: (A) and human cathepsin E transfected: (B) 293T whole cell lysates.
Application Notes
recommended for detection of cathepsin E of mouse, rat and human origin by WB, IP, IF and ELISA also reactive with additional species, including equine and canine
Additional Information
Form
Liquid
Storage Instructions
For short-term storage, store at 4° C. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.