Analytical Data
-
Gene name
TPP1
- Application
-
Alternative Names
CLN2; GIG1; LPIC; Tripeptidyl aminopeptidase; Lysosomal pepstatin-insensitive protease; Ceroid-Lipofuscinosis,Neuronal 2,Late Infantile; Cell growth-inhibiting gene 1 protein
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
O14773
-
Expression Region
Met1~Pro320
-
Molecular Weight
38kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
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
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
TPP1, or Tripeptidyl Peptidase I, is a lysosomal enzyme that plays a critical role in protein degradation and the clearance of misfolded proteins. Dysfunctions in TPP1 have been linked to various neurodegenerative disorders, including Batten disease, a severe childhood-onset lysosomal storage disorder characterized by progressive neurodegeneration and cognitive decline. The study of TPP1 recombinant proteins has gained significant importance in understanding its enzymatic mechanisms, potential substrate interactions, and the pathophysiology associated with TPP1 deficiencies. Research has focused on elucidating the biochemical properties of TPP1, such as its substrate specificity, catalytic activity, and structural conformation through advanced techniques like X-ray crystallography and spectroscopy. Additionally, the development of recombinant TPP1 proteins serves therapeutic purposes, including enzyme replacement therapy for affected patients and the exploration of gene therapy approaches to restore TPP1 function in diseased tissues. Overall, the ongoing research into TPP1 recombinant proteins aims to provide insights into lysosomal biochemistry and develop innovative treatment modalities for associated disorders, contributing to a deeper understanding of lysosomal function and its implications in human health.
