Analytical Data
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Gene name
folP
- Application
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Alternative Names
Dihydropteroate pyrophosphorylase
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Species
Staphylococcus haemolyticus
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q59919
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Expression Region
1-267aa
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Molecular Weight
33.6 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
FolP, or folate biosynthesis protein P, plays a crucial role in the biosynthesis of folate, an essential vitamin for various organisms, including bacteria and plants. Folate is vital for numerous cellular processes, including DNA synthesis and repair, making it a target for antibiotic development. The study of FolP has gained significant attention in recent years due to the increasing concern over antibiotic resistance and the necessity for new antimicrobial agents. Researchers have been focusing on the structural and functional characterization of FolP to understand its mechanism of action and identify potential inhibitors that could disrupt folate synthesis in pathogenic bacteria. By employing techniques such as X-ray crystallography and computational modeling, scientists aim to elucidate the protein's active sites and dynamics, which may pave the way for the design of novel antimicrobial drugs. Additionally, the role of folate in human health underscores the importance of these studies, as understanding FolP could lead to therapeutic applications in treating folate-related deficiencies and diseases. Overall, the investigation of FolP and its associated pathways represents a promising avenue for combatting infectious diseases and enhancing our understanding of metabolic processes in various organisms.
