Analytical Data
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Gene name
DsbC
- Application
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Alternative Names
DsbC;xprA;Thiol:disulfide interchange Protein DsbC
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Species
Dickeya dadantii
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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
P39691
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Expression Region
22-238aa
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AA Sequence
DDAAIKQTL NRLGLQSAEV KDSPIGGMKT VLTENGVLYI TEDGKHLLQG PLYDVSGKTP VNVTNHILNE RLDALKDQMI VYKAPQEKHV ITVFTDITCG YCHKLHEQMK DYNALGITVR YLAYPRQGMN SQAAKDMQSI WCVADRNKAF DAAMKGDDVS PATCKTDIGA HYQLGVLFGV QGTPAIVLDD GTVVPGYQPP KEMMAMLDAH KASLKSGG
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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
DsbC is a periplasmic protein found in Gram-negative bacteria, playing a critical role in the formation of disulfide bonds in the folding of proteins during their transit through the periplasmic space. This protein is classified as a disulfide isomerase, facilitating the reshuffling of incorrect disulfide bonds to promote correct protein folding. The study of DsbC is significant for understanding bacterial physiology and pathogen-host interactions, as proper protein folding is essential for the functionality of many virulence factors. Research on DsbC has garnered attention in the context of biotechnology and vaccine development, leading to interest in its potential applications for producing correctly folded recombinant proteins. By harnessing the properties of DsbC, researchers aim to improve the yield and functionality of heterologous proteins expressed in bacterial systems. Moreover, insights into DsbC's mechanisms can also inform the design of novel therapeutic strategies targeting bacterial infections, particularly in combating antibiotic resistance. Understanding DsbC at a molecular level, including its structure and interaction with substrate proteins, is critical for optimizing its use in various applications while providing broader implications for protein engineering and microbial pathogenesis. As a result, studies involving DsbC not only advance fundamental microbiological knowledge but also hold promise for practical applications in medicine and industry.











