Analytical Data
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Gene name
AGH
- Application
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Alternative Names
AGH；Androgenic gland hormone
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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
Q86SA8
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Expression Region
22-65aa
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AA Sequence
YQVEGMKSDVICADIRFTVHCICNELGRFPTARLTKPCPWPNRE
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Molecular Weight
20.4 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
The study of AGH (Alpha-glucosidase H) recombinant proteins is rooted in its critical role in various biological processes, particularly in carbohydrate metabolism. AGH is an enzyme responsible for the hydrolysis of glycosidic bonds in complex carbohydrates, which is essential for the proper functioning of digestive systems in many organisms. Research has indicated that irregularities in AGH activity can lead to metabolic disorders, including certain types of lysosomal storage diseases and diabetes. As such, producing AGH in a recombinant form offers significant advantages for therapeutic applications, including enzyme replacement therapies. Advances in biotechnology allow for the production of AGH in host organisms such as bacteria, yeast, or mammalian cells, facilitating large-scale synthesis and purification. Researchers are particularly interested in characterizing the functional properties of recombinant AGH, including its enzymatic activity, stability, and efficacy in metabolic pathways. The ongoing exploration of AGH recombinant proteins not only aims to better understand enzyme structure-function relationships but also seeks to develop innovative treatments for metabolic diseases, thus contributing to broader medical and pharmacological advancements. As the field progresses, understanding and manipulating AGH at the molecular level could yield significant therapeutic strategies in combating metabolic disorders and improving patient outcomes.
