epitope corresponding to amino acids 191-240 mapping within an internal region of cathepsin K of human origin
Modification Notes
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 (1-6). The aspartyl protease class is composed of cathepsins D and E (7,8). Cathepsin G is in the serine protease class (9). Most cathepsins are lysosomal and each is involved in cellular metabolism, participating in various events such as peptide biosynthesis and protein degradation. Cathepsin K expression is highest in bone, cartilage and skeletal muscle. The strongest mRNA levels are revealed in osteoclasts (4).
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of cathepsin K of mouse, rat and human origin by WB, IP, IF and ELISA also reactive with additional species, including equine, canine, bovine, porcine and avian:
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 191-240 mapping within an internal region of cathepsin K of human origin
Tissue Specificity
epitope corresponding to amino acids 191-240 mapping within an internal region of cathepsin K of human origin
Western blot analysis of cathepsin K expression in MCF7 (A), H69AR (B) and C32 (C) whole cell lysates.
Application
Immunofluorescence staining of methanol-fixed HeLa cells showing cell surface localization.
Application Notes
recommended for detection of cathepsin K of mouse, rat and human origin by WB, IP, IF and ELISA also reactive with additional species, including equine, canine, bovine, porcine and avian:
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.