Analytical Data
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Gene name
FUCA2
- Application
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Alternative Names
FUCA2;Plasma alpha-L-fucosidase
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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
Q9BTY2
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Expression Region
29-467aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSHSATRFDPTWESLDARQLPAWFDQAKF GIFIHWGVFSVPSFGSEWFWWYWQKEKIPKYVEFMKDNYPPSFKYEDFGP LFTAKFFNANQWADIFQASGAKYIVLTSKHHEGFTLWGSEYSWNWNAIDE GPKRDIVKELEVAIRNRTDLRFGLYYSLFEWFHPLFLEDESSSFHKRQFP VSKTLPELYELVNNYQPEVLWSDGDGGAPDQYWNSTGFLAWLYNESPVRG TVVTNDRWGAGSICKHGGFYTCSDRYNPGHLLPHKWENCMTIDKLSWGYR REAGISDYLTIEELVKQLVETVSCGGNLLMNIGPTLDGTISVVFEERLRQ MGSWLKVNGEAIYETHTWRSQNDTVTPDVWYTSKPKEKLVYAIFLKWPTS GQLFLGHPKAILGATEVKLLGHGQPLNWISLEQNGIMVELPQLTIHQMPC KWGWALALTNVI
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Molecular Weight
53 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
FUCA2, or fucosidase alpha-L-2, is an enzyme implicated in the metabolism of fucose, a carbohydrate that plays essential roles in various biological processes, including cell signaling, adhesion, and immune response. The interest in FUCA2 is particularly heightened due to its association with several pathological conditions, including cancer and genetic disorders like fucosidosis. The study of FUCA2 recombinant proteins has become increasingly relevant as researchers seek to understand the enzyme's structure-function relationship and its role in glycosylation pathways. This understanding could pave the way for novel therapeutic strategies targeting fucose-related pathways. Moreover, the development of FUCA2 recombinant proteins provides tools for studying enzyme kinetics, substrate specificity, and potential inhibitors, thereby contributing to the broader field of glycomics and its applications in medicine. Through techniques such as site-directed mutagenesis, protein engineering, and crystallization, researchers aim to elucidate the mechanisms by which FUCA2 exerts its biological effects. Overall, the exploration of FUCA2 and its recombinant counterparts holds promise for enhancing our knowledge of glycan biology and advancing therapeutic approaches for diseases linked to fucosylation anomalies.
