Analytical Data
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Gene name
resilin
- Application
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Alternative Names
/
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Species
Drosophila melanogaster
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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
Q9V7U0
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Expression Region
342-620aa
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Molecular Weight
34.9 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
Resilin is a remarkable elastomeric protein found in the cuticles of various arthropods and has drawn significant interest due to its superior elastic properties. It possesses an extraordinary ability to stretch and recoil, allowing organisms like insects and crustaceans to perform rapid and efficient movements, such as the flight of a fly or the jump of a flea. The primary research background on resilin revolves around its unique molecular structure, which consists of highly repetitive sequences rich in glycine and proline, enabling it to store elastic energy effectively. Scientists are keen on understanding the molecular mechanics of resilin to explore its potential applications in biomaterials, tissue engineering, and soft robotics. The ability to produce resilin as a recombinant protein in microbial systems presents promising opportunities for creating sustainable materials that mimic its properties. Furthermore, advancements in genetic engineering and recombinant DNA technology have made it feasible to synthesize resilin and its variants, allowing researchers to tailor its characteristics for specific applications. The efforts to harness resilin’s biological and mechanical advantages could revolutionize various fields, including medicine, where it may be used to fabricate flexible implants, or in sports, to develop high-performance gear. Overall, the study of resilin and its recombinant forms represents a fascinating intersection of biology, materials science, and engineering, with the potential to innovate various sectors in society.
