Analytical Data
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Gene name
halysin
- Application
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Alternative Names
Platelet aggregation activation inhibitor
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Species
Gloydius blomhoffii
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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
P21858
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Expression Region
1-71aa
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Molecular Weight
9.5 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
Halysin is a proteolytic enzyme derived from the extremophilic bacterium *Halobacterium salinarum*, known for its potential in biotechnological applications due to its stability and activity in extreme conditions, including high salinity and temperature. Research on halysin has garnered interest because of its unique properties that may provide solutions in various fields, including food preservation, biomedical applications, and environmental biotechnology. The enzyme’s ability to cleave specific peptide bonds makes it a valuable tool for protein engineering and modification processes. Moreover, halysin's functionality in extreme environments could pave the way for innovations in industrial processes that require robust enzymes, especially in the production of biofuels or biopolymers. The recombinant production of halysin in suitable host organisms, such as *Escherichia coli*, allows for large-scale synthesis and detailed characterizations, facilitating the exploration of its properties and applications. Ongoing studies aim to optimize the expression and purification of halysin to enhance its catalytic efficiency and stability, thereby opening new avenues for its practical use in various industries. The exploration of halysin not only underscores the significance of extremophilic enzymes in biotechnology but also illuminates the potential of harnessing nature's diverse organisms to develop sustainable and efficient biotechnological solutions.
