TPP1/CLN2, Recombinant Protein

Tripeptidyl-Peptidase 1; TPP-1; Cell Growth-Inhibiting Gene 1 Protein; Lysosomal Pepstatin-Insensitive Protease; LPIC; Tripeptidyl Aminopeptidase; Tripeptidyl-Peptidase I; TPP-I; TPP1; CLN2

For Research Use Only. Not for use in diagnostic procedures.

Human Cells

>95% as determined by reducing SDS-PAGE.

Supplied as a 0.2 mum filtered solution of 20mM TrisHCl, 150mM NaCl, 1mM GaCl2, 10% Glycerol, pH7.5.

Store at < -20 degree C, stable for 6 months. Please minimize freeze-thaw cycles.

Manufactured in an ISO 9001:2015 Certified Laboratory.

Small volumes of TPP1/CLN2 recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

Protein Construction: Recombinant Human TPP1 is produced by our mammalian expression system and the target gene encoding Ser20-Pro563 is expressed with a 6His tag at the C-terminus.

Background: Tripeptidyl-Peptidase 1 (TPP1) belongs to the peptidase S53 family. TPP1 is detected in all tissues examined with highest levels in heart and placenta and relatively similar levels in other tissues. TPP1 is lysosomal serine protease with tripeptidyl-peptidase I activity. TPP1 may act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases. TPP1 requires substrates with an unsubstituted N-terminus. TPP1 mutations have also been shown to cause neuronal ceroid lipofuscinosis type 2 (CLN2).

Molecular Mass: 60.35kDa
Actual Protein Molecular Mass: 74kDa

tripeptidyl peptidase 1

tripeptidyl-peptidase 1

Tripeptidyl-peptidase 1

CLN2; TPP-1; LPIC; TPP-I  [Similar Products]

This gene encodes a member of the sedolisin family of serine proteases. The protease functions in the lysosome to cleave N-terminal tripeptides from substrates, and has weaker endopeptidase activity. It is synthesized as a catalytically-inactive enzyme which is activated and auto-proteolyzed upon acidification. Mutations in this gene result in late-infantile neuronal ceroid lipofuscinosis, which is associated with the failure to degrade specific neuropeptides and a subunit of ATP synthase in the lysosome. [provided by RefSeq, Jul 2008]

Lysosomal serine protease with tripeptidyl-peptidase I activity. May act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases. Requires substrates with an unsubstituted N-terminus ().

All of MyBioSource's Products are for scientific laboratory research purposes and are not for diagnostic, therapeutics, prophylactic or in vivo use. Through your purchase, you expressly represent and warrant to MyBioSource that you will properly test and use any Products purchased from MyBioSource in accordance with industry standards. MyBioSource and its authorized distributors reserve the right to refuse to process any order where we reasonably believe that the intended use will fall outside of our acceptable guidelines.

While every efforts were made to ensure the accuracy of the information provided in this datasheet, MyBioSource will not be liable for any omissions or errors contained herein. MyBioSource reserves the right to make changes to this datasheet at any time without prior notice.

It is the responsibility of the customer to report product performance issues to MyBioSource within 30 days of receipt of the product. Please visit our Terms & Conditions page for more information.