Analytical Data
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Gene name
maiA
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简介
The maiA protein is a key enzyme involved in catalyzing the cis-trans isomerization of the C2-C3 double bond in maleic acid, leading to the formation of fumaric acid. By facilitating this chemical transformation, maiA plays a crucial role in regulating the isomeric configuration of the C2-C3 double bond in maleic acid, ultimately converting it into fumaric acid. maiA Protein, Serratia marcescens is the recombinant maiA protein, expressed by E. coli , with tag free.
- Application
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Alternative Names
maiA; Maleate isomerase; Maleate cis-trans isomerase
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Species
Others
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Source
E. coli
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9KWI0
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Expression Region
M1-Y250
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Protein Length
Full Length
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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
MaiA is a crucial protein involved in the biosynthesis of the antibiotic moenomycin, which is produced by certain strains of *Micromonospora*. The research on MaiA has gained significant attention due to its role in catalyzing the rearrangement of the antibiotic's molecular structure, a process that is essential for its biological activity. Moenomycin is particularly important as it exhibits potent activity against a wide range of Gram-positive bacteria, including drug-resistant strains, thus holding potential as a therapeutic agent. Understanding the structure and function of the MaiA protein can provide insights into its enzymatic mechanisms, facilitating the development of novel antibiotics through metabolic engineering or synthetic biology approaches. Researchers aim to elucidate the protein's structure-function relationships by employing techniques such as X-ray crystallography and site-directed mutagenesis, which will contribute to a deeper understanding of its catalytic properties. Additionally, the study of MaiA is pertinent in the context of the increasing global concern over antibiotic resistance, making it a key target for the design of new antimicrobials. Overall, the exploration of MaiA and its role in moenomycin biosynthesis not only enhances our comprehension of antibiotic production but also paves the way for innovative strategies to combat bacterial infections in the era of diminishing antibiotic effectiveness.
