Analytical Data
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Gene name
Anionic trypsin-2
- Application
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Alternative Names
TRY2; Trypsin 2; Serine Endopeptidases; Anionic trypsinogen
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P07478
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Expression Region
Ile24~Asp241
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Molecular Weight
27kDa
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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
Anionic trypsin-2 is a serine protease that plays a crucial role in various physiological processes, including digestion, blood coagulation, and inflammation. The study of this enzyme has garnered significant interest due to its unique biochemical properties and potential applications in biomedical research and therapeutic interventions. As a member of the trypsin family, anionic trypsin-2 exhibits a specific substrate preference for basic amino acids, making it vital for protein digestion in the small intestine. Moreover, its involvement in regulating peptide signaling pathways underscores its relevance in health and disease states, including cancer and autoimmune disorders. The recombinant production of anionic trypsin-2 allows researchers to obtain the enzyme in a controlled manner for detailed structural and functional studies. Understanding the enzyme's catalytic mechanisms and substrate interactions can reveal insights into protein processing and the development of enzyme inhibitors. Furthermore, the generation of modified forms of anionic trypsin-2 could lead to innovations in drug design and the advancement of therapeutic strategies, particularly for conditions associated with protease dysregulation. Overall, the research on anionic trypsin-2 contributes significantly to our understanding of protease biology and its implications in health and disease.
