TPP1 Protein, Human, Recombinant (His)

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.

Pack Size	Availability	Price/USD
50 μg	In stock	$ 386.00
100 μg	5 days	$ 660.00
200 μg	5 days	$ 1,120.00
500 μg	5 days	$ 2,270.00

Pack Size

Availability

Price/USD

Quantity

50 μg

In stock

$ 386.00

100 μg

5 days

$ 660.00

200 μg

5 days

$ 1,120.00

500 μg

5 days

$ 2,270.00

Biological Information

Measured by the cleavage of AlaAlaPheAMC. The specific activity is > 850 pmoles/min/μg.

Description

Species	Human
Expression System	Baculovirus-Insect Cells
Tag	His
Accession Number	AAH14863.1
Synonyms	tripeptidyl peptidase I, CLN2, TPP-1, SCAR7, GIG1, LPIC
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.
Protein Purity	> 95 % as determined by SDS-PAGE
Molecular Weight	Approxiamtely 60.7 kDa

Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method.
Formulation	Supplied as sterile 20mM Tris, 500mM NaCl, pH 7.4, 10% glyPlease contact us for any concerns or special requirements. Please refer to the specific buffer information in the hard copy of CoA.
Reconstitution	A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
Stability & Storage	Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Shipping	Solution. It is shipped out with blue ice.
Research 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.