Analytical Data
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Gene name
eglS
- Application
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Alternative Names
eglS；bglC；gld；Endoglucanase
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Species
E.coli
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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
P10475
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Expression Region
30-499aa
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AA Sequence
AGTKTPVAKNGQLSIKGTQLVNRDGKAVQLKGISSHGLQWYGEYVNKDSLKWLRDDWGITVFRAAMYTADGGYIDNPSVKNKVKEAVEAAKELGIYVIIDWHILNDGNPNQNKEKAKEFFKEMSSLYGNTPNVIYEIANEPNGDVNWKRDIKPYAEEVISVIRKNDPDNIIIVGTGTWSQDVNDAADDQLKDANVMYALHFYAGTHGQFLRDKANYALSKGAPIFVTEWGTSDASGNGGVFLDQSREWLKYLDSKTISWVNWNLSDKQESSSALKPGASKTGGWRLSDLSASGTFVRENILGTKDSTKDIPETPSKDKPTQENGISVQYRAGDGSMNSNQIRPQLQIKNNGNTTVDLKDVTARYWYKAKNKGQNFDCDYAQIGCGNVTHKFVTLHKPKQGADTYLELGFKNGTLAPGASTGNIQLRLHNDDWSNYAQSGDYSFFKSNTFKTTKKITLYDQGKLIWGTEPN
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Molecular Weight
59.7 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
EglS, an extracellular glycoside hydrolase, has garnered significant interest in biochemical and industrial research due to its role in the breakdown of complex carbohydrates. This enzyme is primarily derived from bacteria and is known for its ability to hydrolyze glycosidic bonds, facilitating the conversion of polysaccharides into simpler sugars. The study of EglS recombinant protein is essential for several reasons. Firstly, its applications in biotechnology, particularly in biofuel production and food industry processes, make it a valuable candidate for enzymatic research. Secondly, understanding the structure-function relationship of EglS can provide insights into its catalytic mechanism, which is crucial for optimizing its activity and stability under industrial conditions. Recombinant DNA technology allows for the expression of EglS in host organisms, enabling the production of large quantities of the enzyme for detailed functional assays and characterization. Furthermore, the modification of EglS through techniques such as site-directed mutagenesis can enhance its properties, making it more efficient for specific applications. Overall, the research on EglS recombinant protein not only contributes to fundamental enzymology but also has practical implications in various fields, including renewable energy, waste management, and the development of novel food processing techniques.
