Analytical Data
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Gene name
zwf
- Application
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Alternative Names
zwf；Glucose-6-phosphate 1-dehydrogenase
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Species
E.coli
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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
P0AC53
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Expression Region
1-486aa
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AA Sequence
MAVTQTAQACDLVIFGAKGDLARRKLLPSLYQLEKAGQLNPDTRIIGVGRADWDKAAYTKVVREALETFMKETIDEGLWDTLSARLDFCNLDVNDTAAFSRLGAMLDQKNRITINYFAMPPSTFGAICKGLGEAKLNAKPARVVMEKPLGTSLATSQEINDQVGEYFEECQVYRIDHYLGKETVLNLLALRFANSLFVNNWDNRTIDHVEITVAEEVGIEGRWGYFDKAGQMRDMIQNHLLQILCMIAMSPPSDLSADSIRDEKVKVLKSLRRIDRSNVREKTVRGQYTAGFAQGKKVPGYLEEEGANKSSNTETFVAIRVDIDNWRWAGVPFYLRTGKRLPTKCSEVVVYFKTPELNLFKESWQDLPQNKLTIRLQPDEGVDIQVLNKVPGLDHKHNLQITKLDLSYSETFNQTHLADAYERLLLETMRGIQALFVRRDEVEEAWKWVDSITEAWAMDNDAPKPYQAGTWGPVASVAMITRDGRS
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Molecular Weight
82.0 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
Zwf, or glucose-6-phosphate dehydrogenase, is an essential enzyme in the pentose phosphate pathway, which is crucial for cellular metabolism and oxidative stress response. Its primary function is to catalyze the conversion of glucose-6-phosphate to 6-phosphoglucono-δ-lactone, generating NADPH, a key reducing agent required for biosynthetic reactions and detoxification processes. Research on Zwf and its protein structure is particularly relevant given its role in various metabolic disorders and its potential involvement in cancer progression, where altered metabolic pathways are often observed. Furthermore, mutations in the zwf gene can lead to conditions such as glucose-6-phosphate dehydrogenase deficiency, resulting in hemolytic anemia and other health issues. Understanding the structural and functional dynamics of the Zwf protein can provide insights into its regulatory mechanisms and interactions with other metabolic pathways. Advanced techniques, such as X-ray crystallography and nuclear magnetic resonance (NMR), are often employed to elucidate the protein's three-dimensional architecture, which is critical for designing targeted therapeutic strategies. Additionally, the application of recombinant DNA technology allows for the production of modified Zwf proteins, facilitating studies into how various mutations affect enzymatic activity and stability. Overall, ongoing research on Zwf recombinant proteins is pivotal not only for advancing our knowledge of fundamental metabolic processes but also for developing novel approaches to tackle metabolic diseases and improve therapeutic outcomes.
