Analytical Data
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Gene name
MTHFD2
- Application
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Alternative Names
NAD-dependent methylenetetrahydrofolate dehydrogenase Methenyltetrahydrofolate cyclohydrolase
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Species
Bovine
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q0P5C2
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Expression Region
36-350aa
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Molecular Weight
49.9 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
MTHFD2 (Methylenetetrahydrofolate dehydrogenase 2) is a pivotal enzyme involved in one-carbon metabolism, particularly in the de novo synthesis of purines and amino acids. This enzyme catalyzes the conversion of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate, playing a crucial role in the folate cycle. MTHFD2 has garnered significant attention in cancer research because it is often overexpressed in various cancer types, facilitating rapid cell proliferation and tumor growth by providing essential metabolites. Its unique expression pattern in cancer cells as compared to normal tissues presents a potential target for therapeutic intervention. Studies have shown that inhibiting MTHFD2 could disrupt nucleotide synthesis and diminish the growth of cancer cells. Additionally, MTHFD2 has been linked to mitochondrial metabolism, further highlighting its role in cellular energy production and overall cell homeostasis. The exploration of recombinant MTHFD2 protein is crucial for understanding its enzymatic properties, interaction with potential inhibitors, and its function within cellular metabolic pathways. Consequently, characterizing recombinant MTHFD2 can pave the way for the development of novel anti-cancer strategies and enhance our understanding of its implications in metabolic disorders.
