Analytical Data
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Gene name
folD
- Application
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Alternative Names
folD；ads；Bifunctional Protein FolD
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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
P24186
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Expression Region
1-288aa
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AA Sequence
MAAKIIDGKTIAQQVRSEVAQKVQARIAAGLRAPGLAVVLVGSNPASQIYVASKRKACEEVGFVSRSYDLPETTSEAELLELIDTLNADNTIDGILVQLPLPAGIDNVKVLERIHPDKDVDGFHPYNVGRLCQRAPRLRPCTPRGIVTLLERYNIDTFGLNAVVIGASNIVGRPMSMELLLAGCTTTVTHRFTKNLRHHVENADLLIVAVGKPGFIPGDWIKEGAIVIDVGINRLENGKVVGDVVFEDAAKRASYITPVPGGVGPMTVATLIENTLQACVEYHDPQDE
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Molecular Weight
31.0 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
Related Products
Protein Description
The study of folD recombinant proteins is grounded in the importance of folate metabolism in various biological processes, particularly in microbial and human systems. FolD, or 5,10-methylenetetrahydrofolate dehydrogenase/cyclohydrolase, is a key enzyme involved in the folate biosynthetic pathway, catalyzing the conversion of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate, with significant implications for nucleotide synthesis and cellular function. Abnormalities in folate metabolism are linked to various health issues, including cardiovascular diseases and neural tube defects, highlighting the enzyme's potential as a therapeutic target. Recombinant DNA technology has facilitated the production of folD proteins, enabling detailed functional studies and structural analyses. By expressing folD in heterologous systems, researchers aim to elucidate its enzymatic mechanisms, stability, and substrate specificity. This research not only enhances our understanding of folate-related pathways but also contributes to biotechnological applications, such as the development of probiotics that can modulate folate levels in humans or the production of folate-rich food supplements. Overall, the exploration of folD recombinant proteins serves to bridge gaps in current biological knowledge and hold promise for innovations in health and nutrition.
