TPP1 Protein, Mouse, Recombinant (His Tag)
Product Specifications
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.
Overview
A DNA sequence encoding the mouse TPP1 (NP_034036.1) (Met1-Pro562) was expressed with a polyhistidine tag at the C-terminus.
Synonyms
Cln2 Protein, Mouse; LPIC Protein, Mouse; TPP-1 Protein, Mouse; TPP-I Protein, Mouse
Gene Name
Tripeptidyl peptidase I
Expression System
Baculovirus-Insect Cells
Tag
C-His
Field of Research
Serine Proteases and Regulators
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
Purity
> 95 % as determined by SDS-PAGE.
Activity
At Leading Biology, the biological activity of a recombinant protein is routinely measured using a bioassay, e.g. chemotaxis or cell proliferation assay, enzyme assay, or a functional ELISA. When a recombinant protein is an enzyme, specific activity is derived from an enzymatic assay. Each enzyme is tested for potency by cleavage of a substrate. We are in the process of updating the biological activity data. If you have any questions regarding this update, please feel free to contact our technical support team.
Form
Lyophilized
Buffer
Lyophilized from sterile 20 mM Tris, 150 mM NaCl, pH 7.5, 10 % glycerol. Please contact us for any concerns or special requirements. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hard copy of CoA.
Function
Enzyme Proteins
Molecular Weight
The recombinant mouse TPP1 consists of 554 amino acids and predicts a molecular mass of 60.9 kDa.
Storage Conditions
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature. Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise. Stable for 1 year at -20°C or below from date of shipment. For maximum recovery of product, centrifuge the original vial after thawing and opening the cap. For long-term storage, aliquot and store at -20°C or below. Avoid repeated freeze-thaw cycles.
Symbol
TPP1
Species
Mouse
Protein ID
NP_034036.1
AA Sequence
Met1-Pro562
Protein ID Link
https://www.ncbi.nlm.nih.gov/protein/NP_034036.1
Frequently Asked Questions
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