Analytical Data
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Gene name
Tissue alpha-L-Fucosidase
- Application
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Alternative Names
A-FU; aFU; Alpha-L-Fucosidase; Alpha-L-fucoside fucohydrolase 1
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Species
Rat
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P17164
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Expression Region
Lys170~Leu420
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Molecular Weight
33kDa
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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
Tissue alpha-L-fucosidase is an important enzyme involved in glycoprotein degradation and is essential for various biological processes, including cellular communication and immune response. Deficiency in this enzyme is associated with genetic disorders, such as fucosidosis, which leads to the accumulation of fucosylated compounds and results in severe clinical manifestations. Research into the recombinant expression of tissue alpha-L-fucosidase is crucial for understanding its structure, function, and potential therapeutic applications. By producing this enzyme in a recombinant system, researchers aim to obtain sufficient quantities for enzymatic characterization, elucidate its catalytic mechanisms, and explore its role in disease pathology. Additionally, recombinant alpha-L-fucosidase could pave the way for developing enzyme replacement therapies for patients with fucosidosis and other related disorders. Advances in recombinant DNA technology have facilitated the expression of this enzyme in various host systems, enabling optimized production processes and functional studies. Thus, the exploration of recombinant tissue alpha-L-fucosidase not only contributes to the fundamental biochemistry of glycan metabolism but also holds promise for clinical advancements in treating disorders linked to fucose metabolism.
