Recombinant Human TPP1/CLN2 Protein (His Tag)(Active) | PKSH030613

Recombinant Human TPP1/CLN2 Protein (His Tag)(Active) | PKSH030613 | Gentaur US, UK & Europe Disrtribition

Synonyms: Tripeptidyl-Peptidase 1; TPP-1; Cell Growth-Inhibiting Gene 1 Protein; Lysosomal Pepstatin-Insensitive Protease; LPIC; Tripeptidyl Aminopeptidase; TPP1; CLN2;GIG1;LPIC;SCAR7;TPP-1

Active Protein: Active protein

Activity: 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.

Protein Construction: 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.

Fusion Tag: C-His

Species: Human

Expressed Host: Baculovirus-Insect Cells

Shipping: This product is provided as lyophilized powder which is shipped with ice packs.

Purity: > 95 % as determined by reducing SDS-PAGE.

Endotoxin: < 1.0 EU per µg as determined by the LAL method.

Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

Molecular Mass: 60.7 kDa

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

Reconstitution: Please refer to the printed manual for detailed information.

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.

Research Area: N/A