Analytical Data
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Gene name
DsbG
- Application
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Alternative Names
DsbG；ybdP;Thiol:disulfide interchange Protein DsbG
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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
P77202
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Expression Region
18-248aa
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AA Sequence
EEL PAPVKAIEKQ GITIIKTFDA PGGMKGYLGK YQDMGVTIYL TPDGKHAISG YMYNEKGENL SNTLIEKEIY APAGREMWQR MEQSHWLLDG KKDAPVIVYV FADPFCPYCK QFWQQARPWV DSGKVQLRTL LVGVIKPESP ATAAAILASK DPAKTWQQYE ASGGKLKLNV PANVSTEQMK VLSDNEKLMD DLGANVTPAI YYMSKENTLQ QAVGLPDQKT LNIIMGNK
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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
DsbG is a periplasmic protein disulfide isomerase found in bacteria, playing a crucial role in the formation and rearrangement of disulfide bonds during protein folding processes. The study of DsbG is particularly significant in understanding bacterial pathogenicity, as many bacterial proteins require proper folding facilitated by disulfide bonds to exert their functions effectively. The relevance of DsbG extends to biotechnology and therapeutic applications, as engineering this protein may enhance the yields of correctly folded recombinant proteins in heterologous expression systems. Furthermore, DsbG shares structural and functional similarities with the well-studied protein disulfide isomerase (PDI) in eukaryotes, making it an interesting model for comparative studies in protein chemistry. Research on DsbG has also highlighted its unique structural features and active mechanisms, which could lead to novel insights into protein folding dynamics. Understanding the precise role and mechanisms of DsbG can contribute not only to the basic knowledge of microbial physiology but also to the development of strategies to combat bacterial infections and improve the industrial production of biopharmaceuticals. Overall, DsbG represents a vital component of the cellular machinery in bacteria and poses significant interest for both fundamental research and practical applications in biotechnology.
