How to Buy Cathepsin B

Cathepsin B is an enzymatic protein belonging to the peptidase (or protease) families. In
humans, it is coded by the CTSB gene. Reversible inhibitor of serine/cysteine proteases
and some trypsin-like serine proteases. Its action resembles leupeptin; however, its
plasmin inhibition is less and its cathepsin A inhibition is more than that observed with
leupeptin. Overexpression of cathepsin B has been associated with esophageal
adenocarcinoma and other tumors.

Chronic administration of antipain can reduce the frequency of chemically induced
transformation in BALB/c-/3T3 cells. Hydrolysis of proteins with broad specificity for
peptide bonds. Preferentially cleaves -Arg-Arg-|-Xaa bonds in small molecule substrates
(thus differing from cathepsin L). In addition to being an endopeptidase, shows peptidyl
-dipeptidase activity, liberating C-terminal dipeptides. Cathepsins play an important
role in the turnover of intracellular proteins and extracellular proteins via
endocytosis.
The protein encoded by this gene is a lysosomal cysteine protease composed of a dimer of
disulfide-linked heavy and light chains, both produced from a single protein precursor.
It is a member of the peptidase C1 family. Cathepsins are usually characterized as
members of the lysosomal cysteine protease (active site) family and the cathepsin family
name has been synonymous with lysosomal proteolytic enzymes. At least five transcript
variants encoding the same protein have been found for this gene. Thiol protease which is
believed to participate in intracellular degradation and turnover of proteins. Has also
been implicated in tumor invasion and metastasis.

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