CATB (Cleaved-Asn126) rabbit pAb - 100 μL

Catalytic activity: 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. function: Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis. similarity: Belongs to the peptidase C1 family. subcellular location: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. subunit: Dimer of a heavy chain and a light chain cross-linked by a disulfide bond.