Analytical Data
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Gene name
Trypsin-3
- Application
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Alternative Names
Trypsin-3；PRSS4；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
P09943
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Expression Region
1-172aa
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AA Sequence
VLLDGNGEVVQNGGTYYLLPQVWAQGGGVQLAKTGEETCPLTVVQSPNEL SDGKPIRIESRLRSAFIPDDDKVRIGFAYAPKCAPSPWWTVVEDEQEGLS VKLSEDESTQFDYPFKFEQVSDQLHSYKLLYCEGKHEKCASIGINRDQKG YRRLVVTEDYPLTVVLKKDESS
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Molecular Weight
21 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
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Protein Description
Trypsin is a serine protease that plays a vital role in digestive processes by cleaving peptide bonds in proteins, facilitating their breakdown into amino acids. The study of Trypsin-3, a specifically studied isoform of trypsin, has gained significance due to its unique substrate specificity and potential applications in various fields, including biomedicine and biotechnology. Researchers have focused on the recombinant expression of Trypsin-3 to explore its biochemical properties, structural characteristics, and functional capabilities. The recombinant protein production allows for enhanced yields, purity, and bioactivity, which are crucial for understanding its physiological roles and developing therapeutic applications. Investigating Trypsin-3's action in different biological contexts can provide insights into digestive disorders, protein digestion, and even cancer biology, where proteolytic enzymes are often dysregulated. Additionally, Trypsin-3 may prove beneficial in industrial processes, such as protein hydrolysis and food processing, due to its enzymatic efficiency. Overall, the research on Trypsin-3 recombinant protein not only contributes to the fundamental understanding of proteolytic enzymes but also paves the way for innovative applications across various scientific disciplines.
