Analytical Data
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Gene name
FUCA1
- Application
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Alternative Names
FUCA1;Tissue 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
P04066
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Expression Region
32-466aa
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AA Sequence
QPPRRYTPD WPSLDSRPLP AWFDEAKFGV FIHWGVFSVP AWGSEWFWWH WQGEGRPQYQ RFMRDNYPPG FSYADFGPQF TARFFHPEEW ADLFQAAGAK YVVLTTKHHE GFTNWPSPVS WNWNSKDVGP HRDLVGELGT ALRKRNIRYG LYHSLLEWFH PLYLLDKKNG FKTQHFVSAK TMPELYDLVN SYKPDLIWSD GEWECPDTYW NSTNFLSWLY NDSPVKDEVV VNDRWGQNCS CHHGGYYNCE DKFKPQSLPD HKWEMCTSID KFSWGYRRDM ALSDVTEESE IISELVQTVS LGGNYLLNIG PTKDGLIVPI FQERLLAVGK WLSINGEAIY ASKPWRVQWE KNTTSVWYTS KGSAVYAIFL HWPENGVLNL ESPITTSTTK ITMLGIQGDL KWSTDPDKGL FISLPQLPPS AVPAEFAWTI KLTGVK
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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
FUCA1, or fucosidase alpha-L-1, is a critical enzyme involved in the metabolism of fucose, a monosaccharide that plays essential roles in various biological processes, including cell signaling, immune response, and glycoprotein synthesis. Deficiencies in FUCA1 have been linked to fucosidosis, a rare genetic disorder characterized by a range of neurological and physical symptoms due to the accumulation of fucosylated compounds. Research into the recombinant expression of FUCA1 protein has gained traction in recent years, driven by the need for better diagnostic tools and potential therapeutic approaches for fucosidosis. Scientists have focused on optimizing the expression systems, such as using bacterial, yeast, or mammalian cell platforms, to produce functional FUCA1 protein at scale. This enables detailed biochemical characterization, enzyme activity assays, and investigations into potential substrates. Furthermore, expression of FUCA1 in these systems allows for the exploration of the enzyme's role in fucosylation pathways and its implications for health and disease. By elucidating the structure-function relationship of FUCA1, researchers aim to identify small molecules or biological agents that can modulate its activity, thus opening avenues for innovative treatments. Overall, the study of recombinant FUCA1 protein serves not only to advance our understanding of fucosidosis but also contributes to broader implications in glycobiology and therapeutic development.
