Analytical Data
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Gene name
rbtD
- Application
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Alternative Names
rbtD; Ribitol 2-dehydrogenase; RDH; EC 1.1.1.56
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Species
Enterobacter aerogenes
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P00335
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Expression Region
1-249aa
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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
The study of the rbtD recombinant protein is grounded in its association with the virulence mechanisms of certain pathogenic bacteria, particularly within the context of bacterial infections. rbtD, a gene originally identified in the bacterium *Staphylococcus aureus*, encodes a protein that plays a crucial role in the synthesis of the polysaccharide capsule, which is a key factor in evading host immune responses. Research has shown that the expression of rbtD is upregulated during infection, highlighting its potential as a target for therapeutic intervention. Understanding the structure and function of the rbtD protein can provide valuable insights into the molecular pathways of pathogenesis and host-bacteria interactions. Moreover, rbtD's role in biofilm formation and persistence in hostile environments makes it an attractive subject for the development of novel antimicrobial strategies. Thus, the exploration of rbtD recombinant protein not only enhances our knowledge of bacterial virulence but also opens avenues for innovative treatments against persistent bacterial infections. Advances in recombinant DNA technology have made it feasible to produce rbtD protein in vitro, facilitating the study of its characteristics and interactions with host components. This research has significant implications for the development of vaccines and immune therapies aimed at reducing the impact of bacterial pathogens on public health.
