Analytical Data
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Gene name
mgsA
- Application
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Alternative Names
mgsA；GRO；GRO1；GROA；Growth-regulated alpha Protein
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Species
Human
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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
P09341
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Expression Region
35-107aa
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AA Sequence
ASVATELRCQ CLQTLQGIHP KNIQSVNVKS PGPHCAQTEV IATLKNGRKA CLNPASPIVK KIIEKMLNSD KSN
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Molecular Weight
7.9 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
mgsA, or methylglyoxal synthase A, is an important enzyme in various microbial pathways, playing a crucial role in the metabolism of methylglyoxal, a toxic byproduct of glycolysis. Research into mgsA recombinant protein has gained interest due to its potential applications in biotechnology and medicine. Understanding the structure and function of mgsA can shed light on its role in metabolic regulation and stress response mechanisms in microorganisms. Moreover, since methylglyoxal has been implicated in various human diseases, including diabetes and neurodegenerative disorders, studying the recombinant form of mgsA could pave the way for novel therapeutic approaches and detoxification strategies. Recent advances in molecular cloning and protein expression techniques have enabled researchers to produce mgsA in vitro, allowing for in-depth biochemical characterization and the investigation of its enzymatic properties. By harnessing the potential of mgsA in synthetic biology, scientists aim to develop engineered strains with enhanced metabolic capabilities or to create biosensors for detecting methylglyoxal levels in various environments. Overall, the exploration of mgsA recombinant protein represents a promising frontier in the intersection of microbiology, biochemistry, and biomedical research, with the potential for significant implications in health and industry.
