epitope mapping near the C-terminus of CLN2 of rat origin
recommended for detection of CLN2 of mouse, rat and human origin by WB, IP, IF and ELISA; also reactive with additional species, including equine, canine, bovine and porcine
CLN2 Background Information CLN2, also known as Tripeptidyl peptidase I (TTP-I), a member of the family of serine-carboxyl proteinases (S53), plays a crucial role in lysosomal protein degradation, and a deficiency in this enzyme leads to fatal neurodegenerative disease. CLN2 is a lysosomal aminopeptidase that sequentially removes tripeptides from small polypeptides and also shows a minor endoprotease activity. In lysosomes, CLN2 proenzyme is converted into a mature enzyme with the assistance of another protease and is able to autoactivate in acidic pH in vitro via an unimolecular mechanism.
CLN2 (G-16)
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CLN2 (G-16): sc-34866. Western blot analysis of CLN2 expression in mouse heart tissue extract.
CLN2 (G-16): sc-34866. Western blot analysis of CLN2 expression in mouse heart tissue extract.
CLN2 (G-16): sc-34866. Immunofluorescence staining of methanol-fixed HeLa cells showing nuclear localization.
