Analytical Data
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Gene name
burs
- Application
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Alternative Names
burs；burs-alpha；Bursicon
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Species
E.coli
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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
Q9VD83
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Expression Region
1-173aa
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AA Sequence
MLRHLLRHENNKVFVLILLYCVLVSILKLCTAQPDSSVAATDNDITHLGDDCQVTPVIHVLQYPGCVPKPIPSFACVGRCASYIQVSGSKIWQMERSCMCCQESGEREAAVSLFCPKVKPGERKFKKVLTKAPLECMCRPCTSIEESGIIPQEIAGYSDEGPLNNHFRRIALQ
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Molecular Weight
19.2 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
Burs reconstituted proteins are an area of research that focuses on the assembly and functionality of complex protein structures derived from naturally occurring proteins. The study of these proteins is significant due to their potential applications in biotechnology and medicine, particularly in drug delivery, enzyme catalysis, and the development of biomaterials. Burs proteins, which often exhibit unique folding patterns and stability, can be engineered to enhance their functional properties. Advances in molecular biology techniques, such as recombinant DNA technology and protein purification methods, have facilitated the exploration of these proteins at a molecular level. Researchers are particularly interested in understanding the interactions between different protein domains and the mechanisms that govern their assembly. This knowledge can lead to the design of novel proteins with tailored functions for specific applications. Moreover, studying the reconstitution of these proteins can provide insights into fundamental biological processes, such as protein-protein interactions and the role of chaperones in protein folding. Overall, the research on burs reconstituted proteins is poised to make significant contributions to various fields, including synthetic biology, pharmaceuticals, and materials science, enhancing our understanding of protein functionality and paving the way for innovative solutions to complex biological challenges.
