Analytical Data
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Gene name
DHFR
- Application
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Alternative Names
DHFR;Dihydrofolate reductase
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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
P00374
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Expression Region
2-187aa
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AA Sequence
VGSLNCIVAVSQNMGIGKNGDLPWPPLRNEFRYFQRMTTTSSVEGKQNLVIMGKKTWFSIPEKNRPLKGRINLVLSRELKEPPQGAHFLSRSLDDALKLTEQPELANKVDMVWIVGGSSVYKEAMNHPGHLKLFVTRIMQDFESDTFFPEIDLEKYKLLPEYPGVLSDVQEEKGIKYKFEVYEKND
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Molecular Weight
37.3kDa
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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
Dihydrofolate reductase (DHFR) is a pivotal enzyme in the folate metabolism pathway, responsible for the reduction of dihydrofolate to tetrahydrofolate, a crucial cofactor in the synthesis of nucleotides and amino acids. Its significance is underscored by its role in cellular proliferation and survival, making it a key target in cancer therapy and antimicrobial drug development. Over the years, recombinant protein technology has enabled the production of DHFR with high purity and yield, facilitating detailed biochemical studies and structural analyses. Understanding the structure-function relationship of DHFR through crystallography and mutagenesis has provided insights into enzyme mechanisms and has led to the identification of novel inhibitors. Moreover, the recombinant DHFR protein has been utilized in various applications, including drug screening and the development of biosensors. Given the increasing prevalence of drug resistance, ongoing studies focus on engineering DHFR variants with improved properties or altered specificity to counteract resistance mechanisms. Overall, the research surrounding DHFR recombinant proteins not only enhances our understanding of fundamental biological processes but also holds significant therapeutic potential in combating diseases linked to folate metabolism dysregulation.
