Analytical Data
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Gene name
TRY
- Application
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Alternative Names
TRY；PRSS4；TRY3；TRY4；Trypsin-3
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8GV05
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Expression Region
1-106aa
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AA Sequence
MDNTDRRRRR KQHKIALHDS EEVSSIEWEF INMTEQEEDL IFRMYRLVGD RWDLIAGRVP GRQPEEIERY WIMRNSEGFA DKRRQLHSSS HKHTKPHRPR FSIYPS
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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
The study of the TRY (Truncated Yolk Protein) recombinant protein has gained significant attention in the field of molecular biology and biochemistry due to its potential applications in various biotechnological and therapeutic contexts. TRY proteins, known for their role in lipid binding and transport, are crucial in cellular processes such as metabolism and membrane function. Their structural properties and functionality make them ideal candidates for research in protein engineering and drug development. Advances in recombinant DNA technology facilitate the production of TRY proteins in microbial or eukaryotic systems, enabling the exploration of their properties and interactions at a molecular level. Research on TRY encompasses understanding its biophysical characteristics, post-translational modifications, and the impact of specific amino acid changes on function and stability. Furthermore, the potential applications of TRY proteins in vaccine development, as well as in the enhancement of drug delivery systems, position them as valuable tools in the fight against diseases. Ongoing studies aim to harness the unique properties of TRY proteins, paving the way for innovative therapeutic solutions and improvements in biomanufacturing techniques. Ultimately, the investigation of TRY restructured proteins not only broadens our understanding of protein functionality but also holds promise for impactful advancements in medical and industrial biotechnology.
