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TPP1 Protein, Human, Recombinant (His) is expressed in Baculovirus insect cells with His tag. The predicted molecular weight is 60.7 kDa and the accession number is AAH14863.1.
Pack Size | Price | Availability | Quantity |
---|---|---|---|
50 μg | $386 | In Stock | |
100 μg | $660 | 7-10 days | |
200 μg | $1,120 | 7-10 days | |
500 μg | $2,270 | 7-10 days |
Biological Activity | Measured by the cleavage of AlaAlaPheAMC. The specific activity is > 850 pmoles/min/μg. |
Description | TPP1 Protein, Human, Recombinant (His) is expressed in Baculovirus insect cells with His tag. The predicted molecular weight is 60.7 kDa and the accession number is AAH14863.1. |
Species | Human |
Expression System | Baculovirus Insect Cells |
Tag | C-His |
Accession Number | AAH14863.1 |
Synonyms | tripeptidyl peptidase I,TPP-1,SCAR7,LPIC,GIG1,CLN2 |
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. Predicted N terminal: Ser 20 |
Protein Purity | > 95 % as determined by SDS-PAGE |
Molecular Weight | 60.7 kDa (predicted); 60 kDa (reducing conditions) |
Endotoxin | < 1.0 EU/μg of the protein as determined by the LAL method. |
Formulation | Supplied as sterile 20 mM Tris, 500 mM NaCl, pH 7.4, 10% gly. |
Reconstitution | A Certificate of Analysis (CoA) containing reconstitution instructions is included with the products. Please refer to the CoA for detailed information. |
Stability & Storage | It is recommended to store the product under sterile conditions at -20°C to -80°C. Samples are stable for up to 12 months. Please avoid multiple freeze-thaw cycles and store products in aliquots. |
Shipping | Shipping 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. |
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