GIG1, CLN2, LPIC, TPP-1

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

Baculovirus-Insect Cells

> 95 % as determined by SDS-PAGE

Lyophilized from sterile 20mM Tris, 500mM NaCl, pH 7.4, 10% gly

Samples are stable for up to twelve months from date of receipt at -70 degree C

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.

Background: Tripeptidyl-peptidase 1 (TPP1 / CLN2) is 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. TPP1 / CLN2 May act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases. Defects in TPP1 / CLN2 are the cause of neuronal ceroid lipofuscinosis type 2 (CLN2), a form of neuronal ceroid lipofuscinosis which is associated with the failure to degrade specific neuropeptides and a subunit of ATP synthase in the lysosome. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material, and clinically by seizures, dementia, visual loss, and/or cerebral atrophy.

Description: A DNA sequence encoding the pro form of human TPP1 (AAH14863.1) (Met 1-Pro 563) was fused with a polyhistidine tag at the C-terminus.

The secreted recombinant human TPP1 (pro form) comprises 554 amino acids and has a predicted molecular mass of 60.7 kDa. The apparent molecular mass of rhTPP1 is approximately 60 kDa in SDS-PAGE under reducing conditions.

34,464 Da

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]

TPP1: 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. Defects in TPP1 are the cause of neuronal ceroid lipofuscinosis type 2 (CLN2). A form of neuronal ceroid lipofuscinosis. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material, and clinically by seizures, dementia, visual loss, and/or cerebral atrophy. The lipopigment pattern seen most often in CLN2 consists of curvilinear profiles. Belongs to the peptidase S53 family. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: EC 3.4.14.9; Mitochondrial; Protease; Secreted; Secreted, signal peptide

Chromosomal Location of Human Ortholog: 11p15.4

Cellular Component: lysosomal lumen; lysosome

Molecular Function: endopeptidase activity; peptidase activity; peptide binding; protein binding; serine-type peptidase activity; tripeptidyl-peptidase activity

Biological Process: bone resorption; central nervous system development; epithelial cell differentiation; lipid metabolic process; lysosome organization and biogenesis; nervous system development; neuromuscular process controlling balance; peptide catabolic process; proteolysis

Disease: Ceroid Lipofuscinosis, Neuronal, 2

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