Analytical Data
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Gene name
RRM2
- Application
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Alternative Names
Ribonucleotide reductase small chainRibonucleotide reductase small subunit
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Species
Human
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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
P31350
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Expression Region
1-389aa
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Molecular Weight
60.9 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
RRM2, the regulatory subunit of ribonucleotide reductase, plays a crucial role in the synthesis of deoxyribonucleotides, which are essential for DNA replication and repair. Its function is vital for cellular proliferation and maintaining genomic stability, making it a significant focus in cancer research. Overexpression of RRM2 has been linked to increased tumorigenesis and resistance to chemotherapy, as cancer cells often require elevated levels of deoxynucleotides to support their rapid growth. Studies have shown that targeting RRM2 could enhance the effectiveness of existing cancer therapies by depriving tumor cells of the nucleotides necessary for DNA synthesis. Furthermore, understanding the regulatory mechanisms and structural characteristics of RRM2 can provide insights into its function and potential as a therapeutic target. The development of recombinant RRM2 proteins allows for detailed biochemical and biophysical analyses, facilitating the exploration of its interactions, enzymatic activity, and the effects of post-translational modifications. This research not only enhances our comprehension of ribonucleotide reduction pathways in cancer cells but also opens avenues for innovative therapeutic strategies aimed at manipulating nucleoside metabolism for cancer treatment. Overall, investigating RRM2's role in cancer biology is pivotal for advancing personalized medicine approaches and improving patient outcomes in oncology.
