Description
Key facts
Purity:>90% SDS-PAGE,
Expression system:Escherichia coli,
Tags:His tag N-Terminus,
Applications:Mass Spec, SDS-PAGESee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:No,
Accession:Q9NX52,
Animal free:No,
Carrier free:No,
Species:Human,
Storage buffer:pH: 7.2 - 7.4Constituents: Tris buffer, 50% Glycerol (glycerin, glycerine)
Product details:
Previously labelled as RHBDL2
Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage conditions--20°C, Appropriate long-term storage conditions--20°C, Storage information-Avoid freeze / thaw cycle
Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
RRP2 also known as Rpa2 or Rrm2 acts as a subunit of the ribonucleoside-diphosphate reductase complex. This protein plays a mechanical role in converting ribonucleosides into deoxyribonucleosides which are necessary for DNA synthesis and repair. RRP2 has a mass of approximately 45 kDa and shows expression in proliferating cells where DNA synthesis is active such as in the skin gastrointestinal tract and various cancer cells.
Biological function summary
In its role within the ribonucleotide reductase complex RRP2 is important for maintaining the balance of deoxyribonucleotide triphosphates (dNTPs) within the cell. These dNTPs are essential for chromosomal DNA replication which links this protein's role to processes like cell cycle progression and cellular proliferation. The complex consists of two subunits of which RRP2 is one; it works in tight coordination to ensure the production of dNTPs.
Pathways
The activity of RRP2 integrates into the DNA replication and repair pathways essential pathways for cell cycle regulation and genomic stability. RRP2 associates with proteins such as RRM1 which forms the large subunit of the ribonucleotide reductase complex and directly interacts in the pathway. Together they contribute significantly to the DNA synthesis process.
Mutations or dysregulation of RRP2 have been linked to cancer due to its role in cellular proliferation. Increase in RRP2 expression often correlates with high proliferative activity observed in various tumors including colorectal and breast cancer. Furthermore aberrant activity of proteins like MCM2 which involve in DNA replication sometimes relate to elevated RRP2 function contributing to tumorigenesis.
