Analytical Data
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Gene name
PNPO
- Application
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Alternative Names
PNPO;Pyridoxine-5'-phosphate oxidase
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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
Q9NVS9
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Expression Region
57-261aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMDPVKQFAAWFEEAVQCPDIGEANAMCLAT CTRDGKPSARMLLLKGFGKDGFRFFTNFESRKGKELDSNPFASLVFYWEP LNRQVRVEGPVKKLPEEEAECYFHSRPKSSQIGAVVSHQSSVIPDREYLR KKNEELEQLYQDQEVPKPKSWGGYVLYPQVMEFWQGQTNRLHDRIVFRRG LPTGDSPLGPMTHRGEEDWLYERLAP
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Molecular Weight
26 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
The study of recombinant proteins, particularly PNPO (pyridoxamine 5'-phosphate oxidase), has gained significant attention due to its critical role in vitamin B6 metabolism. PNPO catalyzes the conversion of pyridoxamine 5'-phosphate to pyridoxal 5'-phosphate, the active form of vitamin B6, which is essential for numerous biochemical processes, including amino acid metabolism and neurotransmitter synthesis. Deficiency in vitamin B6 has been linked to various health issues, including neurological disorders and impaired immune function. As a result, understanding the structure and function of PNPO is vital for elucidating the underlying mechanisms of these disorders. Advances in molecular biology techniques have facilitated the expression of recombinant PNPO in various host systems, enabling researchers to produce large quantities for functional studies and structural analysis. By investigating the enzyme's catalytic properties, substrate specificity, and interactions with cofactors, researchers aim to uncover potential therapeutic targets for conditions associated with vitamin B6 deficiency. Furthermore, the recombinant PNPO's application extends beyond basic research, as it holds promise in biotechnology and pharmaceutical industries for the development of vitamin supplementation and novel enzymatic assays. Overall, the research on PNPO recombinant proteins serves to deepen our understanding of vitamin B6's role in human health and disease, paving the way for innovative solutions to nutritional deficiencies.
