Cathepsin L

• Description:

  Cathepsin L is a lysosomal cysteine protease expressed in most eukaryotic cells. Cathepsin L is known to hydrolyze a number of proteins, including the proform of urokinasetype plasminogen activator, which is activated by Cathepsin L cleavage. Cathepsin L has also been shown to proteolytically inactivate α1 anti trypsin and secretory leucoprotease inhibitor, two major protease inhibitors of the respiratory tract. These observations, combined with the demonstration of increased Cathepsin L activity in the epithelial lining fluid of the lungs of emphysema patients, have led to the suggestion that the enzyme may be involved in the progression of this disease. Cathepsin L has also been identified as a major excreted protein of transformed fibroblasts, indicating the enzyme could be involved in malignant tumor growth. Human Cathepsin L activity is greatest under mildly acidic conditions, from pH 4.5 to 6.5. The stability of the enzyme decreases at higher pH values.

• Synonyms:

  CTSL1; MEP; CATL; CTSL

• NCBI Gene ID:

  1514

• UniProt:

  P07711

• Accession Number:

  NP_001903

• Accession Number mRNA:

  NM_001912

• Chromosomal Location:

  9Q21.33

• Reactivity:

  Anti-Human

• Cross Reactivity:

  Human

• Target Antigen:

  Recombinant human Cathepsin-L

• Clone:

  (#6M17)

• Applications:

  WB, IHC

• Purification Method:

  Protein G chromatography

• Assay Protocol:

  Centrifuge vial prior to opening. Reconstitute the antibody with 500 µl sterile PBS and the final concentration is 200 µg/ml.

• Form:

  Lyophilized

• Buffer:

  PBS

• Reconstitution:

  PBS

• Storage Conditions:

  Lyophilized samples are stable for 2 years from date of receipt when stored at -70°C. Reconstituted antibody can be aliquoted and stored frozen at < -20°C for at least six months without detectable loss of activity.

• Host or Source:

  Rat

• Isotype:

  IgG2