Analytical Data
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Gene name
Esterase D/FGH
- Application
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Alternative Names
rHuS-formylglutathione hydrolase/FGH, His; S-Formylglutathione Hydrolase; FGH; Esterase D; Methylumbelliferyl-Acetate Deacetylase; ESD
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Species
Human
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Source
E. coli
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Tag
C-6*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
AAH01169.1
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Expression Region
M1-A282
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AA Sequence
MALKQISSNKCFGGLQKVFEHDSVELNCKMKFAVYLPPKAETGKCPALYWLSGLTCTEQNFISKSGYHQSASEHGLVVIAPDTSPRGCNIKGEDESWDFGTGAGFYVDATEDPWKTNYRMYSYVTEELPQLINANFPVDPQRMSIFGHSMGGHGALICALKNPGKYKSVSAFAPICNPVLCPWGKKAFSGYLGTDQSKWKAYDATHLVKSYPGSQLDILIDQGKDDQFLLDGQLLPDNFIAACTEKKIPVVFRLQEDYDHSYYFIATFITDHIRHHAKYLNA
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Protein Length
Full Length
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Molecular Weight
33.0 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
Esterase D, also known as FGH (fatty acid glycosyl hydrolase), is an enzyme that plays a significant role in the hydrolysis of ester bonds in various substrates, including lipids and carbohydrates. Its importance extends to multiple biological processes, including lipid metabolism and the detoxification of xenobiotics. Research into the recombinant expression of Esterase D/FGH has gained traction due to its potential applications in industrial biotechnology and medicine. By utilizing recombinant DNA technology, researchers are able to produce this enzyme in heterologous systems, enhancing its yield and purity for subsequent studies. Understanding the structure and function of Esterase D/FGH can lead to insights into its catalytic mechanisms and substrate specificity, which are critical for designing effective biocatalysts for industrial applications. Furthermore, mutations and modifications can be introduced to improve the enzyme's stability and activity under various conditions. The study of this enzyme not only contributes to fundamental enzymology but also opens avenues for biotechnological innovations, including the development of biosensors and environmentally friendly chemical processes. Overall, the exploration of Esterase D/FGH as a recombinant protein stands at the intersection of basic research and practical application, potentially leading to advancements in both scientific understanding and technological development.
