Analytical Data
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Gene name
TPR
- Application
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Alternative Names
N(1),N(8)-bis(glutathionyl)spermidine reductase
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Species
Trypanosoma cruzi
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Source
Yeast
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P28593
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Expression Region
1-492aa
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Molecular Weight
55.9 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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
TPR (Tetratricopeptide Repeat) proteins are a diverse family of proteins characterized by the presence of repeating TPR motifs, typically consisting of around 34 amino acids. These motifs facilitate protein-protein interactions, playing critical roles in various cellular processes, including transcriptional regulation, protein folding, and the assembly of multiprotein complexes. Research has demonstrated that TPR-containing proteins are integral to processes such as cell cycle control, signal transduction, and stress responses. Due to their ability to mediate interactions with a wide range of partner proteins, TPR proteins are of significant interest in understanding the molecular mechanisms underlying various diseases, including cancer and neurodegenerative disorders. The study of TPR domain structures through techniques like X-ray crystallography and NMR has provided insights into their binding specificity and functional roles. Moreover, recombinant TPR proteins have become essential tools in biotechnology and drug development, offering potential for therapeutic interventions and the design of novel biomaterials. Ongoing research continues to uncover the complexities of TPR protein interactions, advancing our comprehension of their biological significance and therapeutic potential.
