Analytical Data
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Gene name
RRM2
- Application
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Alternative Names
MRM2;FJH1;FTSJ2;rRNA methyltransferase 2. mitochondrial
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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
P31350
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Expression Region
1-389aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MLSLRVPLAP ITDPQQLQLS PLKGLSLVDK ENTPPALSGT RVLASKTARR IFQEPTEPKT KAAAPGVEDEPLLRENPRRF VIFPIEYHDI WQMYKKAEAS FWTAEEVDLS KDIQHWESLK PEERYFISHV LAFFAASDGI VNENLVERFS QEVQITEARC FYGFQIAMEN IHSEMYSLLI DTYIKDPKER EFLFNAIETM PCVKKKADWA LRWIGDKEAT YGERVVAFAA VEGIFFSGSF ASIFWLKKRGLMPGLTFSNE LISRDEGLHC DFACLMFKHL VHKPSEERVR EIIINAVRIE QEFLTEALPV KLIGMNCTLM KQYIEFVADR LMLELGFSKV FRVENPFDFM ENISLEGKTN FFEKRVGEYQ RMGVMSSPTE NSFTLDADF
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Molecular Weight
47 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
RRM2, the regulatory subunit of ribonucleotide reductase (RNR), plays a critical role in nucleotide metabolism by catalyzing the conversion of ribonucleotides to deoxyribonucleotides, which are essential for DNA synthesis and repair. Abnormal expression levels of RRM2 have been implicated in various cancers, making it a target of interest for therapeutic interventions. Recent studies have focused on the characterization and production of recombinant RRM2 proteins to better understand its structure, function, and regulatory mechanisms. By utilizing techniques such as recombinant DNA technology and protein expression systems, researchers aim to produce high-purity RRM2 for biochemical assays and structural studies. Such investigations not only illuminate the role of RRM2 in cellular proliferation and tumorigenesis but also pave the way for the development of novel cancer treatments aimed at inhibiting its function. Additionally, elucidating the interactions between RRM2 and other cellular proteins can provide further insights into its regulatory pathways, underscoring the importance of RRM2 in maintaining cellular homeostasis and its potential as a biomarker in cancer diagnosis and prognosis.
