Technical Data
Cathepsin B
Cathepsin B is a normal lysosomal cysteine proteinase that is expressed in all cells. It is synthesized as an inactive 43kD pro-enzyme which, by removal of a 62 amino acid propeptide, is activated to the single-chain form of 31kD or the two-chain form (25 and 5kD subunits). Matured cathepsin B is normally localized in the lysosomes where it functions in protein turnover. Cathepsin B is also shown capable of degrading extracellular matrix proteins. Elevated levels of cathepsin B correlate with malignancy suggesting that this enzyme may be a useful prognostic marker for several types of human cancers.

Suitable for use in Western Blot, Flow Cytometry and Immunohistochemistry. Other applications have not been tested.

Recommended Dilutions:
Western Blot: 0.5-4ug/ml
Flow Cytometry: 1:50
Immunohistochemistry: 1:100
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20C. Aliquots are stable for 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
PabIgGAffinity Purified
100ug-20CBlue IceHumanRabbit
Synthetic peptide surrounding aa322 of human cathepsins B
Purified by affinity chromatography
Supplied as a liquid in PBS, pH 7.2, 0.01% thimerosal, 0.5% BSA, 30% glycerol
Recognizes both the pro- (37-43kD) and mature (25kD) forms of human cathepsin B. Species Crossreactivity: mouse, rat (weak).
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Barrett, A.J. and Kirschke, H., Methods Enzymol. 80: 535-561 (1981). 2. Chan, S.J., et al. PNAS 83: 7721-7725 (1986).