Analytical Data
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Gene name
gmhA
- Application
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Alternative Names
Sedoheptulose 7-phosphate isomerase
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Species
Escherichia coli
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P63224
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Expression Region
1-192aa
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Molecular Weight
36.8 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
The study of gmhA recombinant protein is rooted in the growing interest in understanding bacterial polysaccharide synthesis and its implications for human health. gmhA, a gene found in various Gram-negative bacteria, encodes an enzyme involved in the biosynthesis of lipopolysaccharides (LPS), crucial components of the outer membrane. LPS plays a significant role in the pathogenicity of bacteria, influencing immune responses and contributing to the virulence of infectious agents. Research on gmhA not only provides insights into bacterial structure and function but also has potential applications in vaccine development and drug design. The recombinant expression of gmhA allows for the production of large quantities of the protein, facilitating detailed studies on its biochemical properties and role in LPS biosynthesis. This approach can lead to the exploration of gmhA as a target for novel antimicrobial therapies, especially given the rising concern over antibiotic resistance. Additionally, characterizing gmhA and its enzymatic functions can aid in unraveling the complex mechanisms of bacterial resistance, ultimately contributing to the development of more effective strategies to combat bacterial infections. The continued investigation into gmhA recombinant protein highlights its significance as a model for understanding broader mechanisms of bacterial pathogenicity and offers pathways for innovative interventions in infectious disease management.
