Analytical Data
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Gene name
UAP1
- Application
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Alternative Names
UAP1；SPAG2；UDP-N-acetylhexosamine pyrophosphorylase
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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
Q16222
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Expression Region
1-522aa
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AA Sequence
MNINDLKLTLSKAGQEHLLRFWNELEEAQQVELYAELQAMNFEELNFFFQKAIEGFNQSSHQKNVDARMEPVPREVLGSATRDQDQLQAWESEGLFQISQNKVAVLLLAGGQGTRLGVAYPKGMYDVGLPSRKTLFQIQAERILKLQQVAEKYYGNKCIIPWYIMTSGRTMESTKEFFTKHKYFGLKKENVIFFQQGMLPAMSFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDMEQRGIWSIHVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQVVEYSEISLATAQKRSSDGRLLFNAGNIANHFFTVPFLRDVVNVYEPQLQHHVAQKKIPYVDTQGQLIKPDKPNGIKMEKFVFDIFQFAKKFVVYEVLREDEFSPLKNADSQNGKDNPTTARHALMSLHHCWVLNAGGHFIDENGSRLPAIPRSATNGKSETITADVNHNLKDANDVPIQCEISPLISYAGEGLESYVADKEFHAPLIIDENGVHELVKNGI
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Molecular Weight
60.8 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
UAP1, or UDP-N-acetylglucosamine pyrophosphorylase 1, is an enzyme involved in glycosylation processes critical for various biological functions, including cell signaling, adhesion, and immune responses. Understanding UAP1 is especially significant due to its role in the biosynthesis of glycosaminoglycans and glycoproteins, which are essential for maintaining cellular structure and function. Research has indicated that UAP1 may be linked to certain pathological conditions, including cancer and genetic disorders affecting glycosylation. Recombinant UAP1 protein, produced through molecular cloning and expression systems, provides a valuable tool for investigating the enzyme's biochemical properties and its interactions with substrates. This recombinant approach permits the study of UAP1 in a controlled environment, enabling detailed kinetic analyses, substrate specificity examinations, and the exploration of potential inhibitor compounds. Additionally, generating antibodies against UAP1 can help elucidate its physiological roles and regulatory mechanisms in vivo. Given the increasing recognition of glycosylation's importance in various fields, including therapeutic development and personalized medicine, UAP1 research stands at the intersection of biochemistry, molecular biology, and clinical application, making it a promising avenue for future investigations aimed at improving human health.
