Analytical Data
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Gene name
Silicatein
- Application
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Alternative Names
; Silicatein; EC 3.4.22.-
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Species
Petrosia ficiformis
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q6YD92
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Expression Region
123-339aa
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Molecular Weight
30.5 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
Silicatein is a biomolecule originally discovered in the siliceous sponges, known for its unique ability to catalyze the polymerization of silicic acid into silica. This intriguing property has sparked significant interest in the field of biomaterials and nanotechnology, as silicatein could potentially serve as a template for biomimetic silica synthesis. Given its role in natural silica formation, researchers have focused on understanding the structure-function relationships of silicatein, including its enzymatic mechanisms and the environmental conditions that enhance its activity. Advances in genetic engineering have allowed for the recombinant production of silicatein, providing a more accessible means to study this protein and its functionalities in vitro. By utilizing recombinant silicatein, scientists aim to explore its applications in diverse fields such as drug delivery, tissue engineering, and the development of novel biomaterials. The potential for silicatein to influence the design of silica-based materials opens up exciting avenues for innovative uses in medicine and industry, making it a focal point of research in the intersection of biology, chemistry, and materials science.
