Recombinant Human Cathepsin L

A cathepsin is a cysteine or aspartic protease, a type of protein that breaks apart other proteins, found in many types of cells including those in all animals. There are approximately a dozen members of this family, which are distinguished by their structure and which proteins they cleave. Most of the members become activated at the low pH found in lysosomes. Thus, the activity of this family lies almost entirely within those organelles. Cathepsins have a vital role in mammalian cellular turnover, e.g. bone resorption. They degrade polypeptides and are distinguished by their substrate specificites.

The biological activity of Human Cathepsin L was determined by its ability to cleave a fluorescent peptide substrate, N-carbobenzyloxy-Leu-Arg-7-amido-4-methylcoumarin (Z-L-R-AMC). The specific activity, measured with 10 μM Z-L-R-AMC and 1 ng enzyme in 100 μL of 50 mM MES, 5 mM dithiothreitol, pH 6.0, at room temperature, is > 15,000 pmoles/min/μg.

Histidine Tag

eaprsvdwre kgyvtpvknq gqcgscwafs atgalegqmf rktgrlisls eqnlvdcsgp qgnegcnggl mdyafqyvqd nggldseesy pyeateesck ynpkysvand tgfvdipkqe kalmkavatv gpisvaidag hesflfykeg iyfepdcsse dmdhgvlvvg ygfestesdn nkywlvknsw geewgmggyv kmakdrrnhc giasaasypt vhhhhhh

Glu113 & Ala114

Frozen

The predicted molecular weight of Recombinant Human Cathepsin L is Mr 36 kDa.

36

The cytokine is supplied frozen in 50 mM sodium acetate, 0.4 M NaCl, pH 5.0.

The frozen protein is stable for 6 months when kept a -20°C to -70°C in a manual defrost freezer. Avoid repeat freeze thaw cycles..

Dry Ice