Analytical Data
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Gene name
FOXM1
- Application
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Alternative Names
Forkhead-related protein FKHL16 Hepatocyte nuclear factor 3 forkhead homolog 11
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q08050
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Expression Region
235-327aa
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Molecular Weight
31.2 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
FOXM1, a member of the Forkhead box family of transcription factors, plays a critical role in cell proliferation, differentiation, and tumorigenesis. Its expression is tightly regulated during the cell cycle, with heightened activity observed in the S and G2/M phases, correlating with its function in cell cycle progression and DNA repair mechanisms. Aberrant FOXM1 expression is implicated in various cancers, making it a potential biomarker and therapeutic target. Researchers have increasingly focused on the production and characterization of recombinant FOXM1 proteins to investigate their biological functions and regulatory mechanisms in cancer development. By utilizing advanced techniques such as molecular cloning and protein purification, studies aim to elucidate the structural and functional properties of FOXM1, including its interaction with other proteins and DNA. Understanding the specific roles of FOXM1 in oncogenesis could provide valuable insights into novel therapeutic strategies aimed at targeting this transcription factor in cancer treatment. Consequently, the study of FOXM1 recombinant proteins not only enhances our comprehension of its biological significance but also paves the way for the development of targeted therapies that could inhibit its oncogenic activity.
