Recombinant Human p53R2 Protein (His Tag)

Name: Recombinant Human p53R2 Protein (His Tag)
Brand: Beta LifeScience
SKU: BLPSN-3634
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Tag	His
Host Species	Human
Accession	Q7LG56
Synonym	MTDPS8A, MTDPS8B, P53R2
Background	Ribonucleoside reductase subunit M2B, also known as RRM2B or p53R2, is an enzyme belonging to the iron-dependent ribonucleotide reductase (RNR) enzyme family which is essential for DNA synthesis. Ribonucleotide reductase (RNR) is an enzyme that catalyzes the formation of deoxyribonucleotides from ribonucleotides and plays a critical role in regulating the total rate of DNA synthesis so that DNA to cell mass is maintained at a constant ratio during cell division and DNA repair. RRM2B is a phosphorylated protein. It is hypothesized that RRM2B activity can be regulated at the posttranslational level in response to DNA damage. RRM2B has previously been shown to be essential for the maintenance of mtDNA copy number and its candidacy for tumor suppression has been evaluated in several mutational analyses of different cancer types. However, the contribution of RRM2B to the DNA damage response has been questioned because its transcriptional induction upon DNA damage is not rapid enough for prompt DNA repair. Instead, ATM-mediated phosphorylation has been suggested to regulate the DNA repair activity of RRM2B posttranslationally. In addition, a defect in RRM2B can induce a mild muscle disease of adult onset through disturbance of mitochondrial homeostasis but that this defect does not appear to be oncogenic.
Description	A DNA sequence encoding the human RRM2B (Q7LG56-1) (Met 1-Phe 351) was expressed, with a His tag at the N-terminus.
Source	E.coli
Predicted N Terminal	Met
AA Sequence	Met 1-Phe 351
Molecular Weight	The recombinant human RRM2B consisting of 366 a.a. and has a calculated molecular mass of 42.6 kDa. It migrates as a 43 kDa band in SDS-PAGE under reducing conditions as predicted.
Purity	>92% as determined by SDS-PAGE
Endotoxin	Please contact us for more information.
Bioactivity	Please contact us for detailed information
Formulation	Lyophilized from sterile PBS, 30% glycerol, pH 8.5.
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function	Plays a pivotal role in cell survival by repairing damaged DNA in a p53/TP53-dependent manner. Supplies deoxyribonucleotides for DNA repair in cells arrested at G1 or G2. Contains an iron-tyrosyl free radical center required for catalysis. Forms an active ribonucleotide reductase (RNR) complex with RRM1 which is expressed both in resting and proliferating cells in response to DNA damage.
Subcellular Location	Cytoplasm. Nucleus. Note=Translocates from cytoplasm to nucleus in response to DNA damage.
Protein Families	Ribonucleoside diphosphate reductase small chain family
Database References	HGNC: 17296 OMIM: 604712 KEGG: hsa:50484 STRING: 9606.ENSP00000251810 UniGene: Hs.512592
Associated Diseases	Mitochondrial DNA depletion syndrome 8A (MTDPS8A); Mitochondrial DNA depletion syndrome 8B (MTDPS8B); Progressive external ophthalmoplegia with mitochondrial DNA deletions, autosomal dominant, 5 (PEOA5)
Tissue Specificity	Widely expressed at a high level in skeletal muscle and at a weak level in thymus. Expressed in epithelial dysplasias and squamous cell carcinoma.

Gene Functions References

The expression of p53R2 was associated closely with the development and progression of lung sarcomatoid carcinoma. PMID: 29246119
p53R2 protein is overexpressed in early-stage cervical cancer and unravels some unconventional oncogenic functions of p53R2. PMID: 28841361
High RRM2B expression is associated with neoplasms. PMID: 27004405
Studied the expression of ribonucleotide reductase (RR) subunit p53R2 in nasopharyngeal carcinoma and its significance in the prognosis. PMID: 29237424
RRM1/RRM2B enzyme is capable of retaining activity in hypoxia and therefore is favored over RRM1/RRM2 in order to preserve ongoing replication and avoid the accumulation of DNA damage in hypoxic cells. PMID: 28416140
A newly discovered role of E2F1 in the regulation of p53R2 expression in DNA damage response. PMID: 25312903
analysis of caspase-dependent degradation of human R2 and p53R2 small subunits PMID: 25878246
in Turkish population p53R2 genotype distributions between head and neck squamous epithelial cell cancer patients and control groups were not statistically significantly different. PMID: 24861915
Data indicate that forkhead transcription factorsF OXO3 directly bound to and transcriptionally activated the promoter of ribonucleotide reductase subunit RRM2B, and induced the expression of RRM2B at RNA and protein levels. PMID: 24947616
we found no support of the hypothesis that aberrations of RRM1 or RRM2B, neither individually nor in combination, are associated with an altered clinical outcome following chemotherapy. PMID: 24215511
Ribonucleotide reductase M2B inhibits cell migration and spreading by early growth response protein 1-mediated phosphatase and tensin homolog/Akt1 pathway in hepatocellular carcinoma. PMID: 24214128
RRM2B expression may discriminate cervical cancer phenotype and radiochemotherapy outcome PMID: 23552804
RRM2B is highly induced in a p53-dependent manner during senescence and is expressed at higher levels in senescent precancerous human prostatic intraepithelial neoplasm lesions compared to adjacent normal prostate glands. PMID: 23139867
p53R2 could regulate matrix synthesis via Akt phosphorylation during chondrocyte mechanotransduction. Down-regulation of p53R2 may be a new therapeutic approach in OA therapy. PMID: 22954457
p53R2 is directly regulated by p53 and also by a MEK2 (ERK kinase 2/MAP kinase kinase 2)-dependent pathway. PMID: 22895183
Propose p53R2 as a therapeutic target to enhance the effectiveness of chemotherapy in patients with p53R2-positive melanoma. PMID: 22902076
These results confirm a role for p53R2 in both Clofarabine and decitabine mechanism of action PMID: 22884950
In nontransformed cells only during quiescence, protein p53R2 is required for maintenance of mitochondrial DNA and for optimal DNA repair after ultraviolet damage. PMID: 22847445
Evidence that disease pathogenesis may be caused by defective RNR assembly is given. PMID: 21378381
Increased expression of p53R2 may predict gemcitabine resistance, and upregulated RNR activity may influence gemcitabine resistance in cholangiocarcinoma cells. PMID: 21451941
p53R2 may suppress cancer cell proliferation; plays critical roles not only in DNA damage repair but also in proliferation of cancer cells PMID: 21216934
p53R2 expression seems more important than that of hRRM2 in prognosis of early-stage lung cancer. PMID: 21965764
this study provides functional evidence that mitochondria is one of p53R2-targeted organelles and suggests an unexpected function of p53R2, which is beyond known ribonucleotide reductase function on dNTP synthesis, in mitochondrial homeostatic control. PMID: 21640705
Adult-onset progressive external ophthalmoplegia due to RRM2B mutations is associated with a benign myopathic phenotype and characterized by muscle-restricted, mitochondrial DNA deletions. PMID: 21646632
oss of p53R2 affects ribonucleotide reduction only in resting cells and leads to a decrease of dNTP catabolism by substrate cycles that counterweigh the loss of anabolic activity PMID: 21297166
This study correlates the distinct catalytic mechanisms of the small subunits hp53R2 and hRRM2 with a hydrogen-bonding network. PMID: 20484015
p53R2-dependent DNA synthesis plays a pivotal role in cell survival by repairing damaged DNA PMID: 11719458
Expression of p53R2, newly p53 target in oral normal epithelium, epithelial dysplasia and squamous cell carcinoma. PMID: 12565178
Wild-type p53 regulates human ribonucleotide reductase by protein-protein interaction with p53R2 as well as hRRM2 subunits. PMID: 12615712
UV-induced activation of p53R2 transcription and binding of p53R2 to hRRM1 to form RR holoenzyme are impaired in the p53-mutant cell line PC3. PMID: 14583450
Four regulatory-region variants were found, of which three were single nucleotide polymorphisms (SNPs) (nt 1 789 C/G, nt 1 928 A/G, 1 933 T/C), and one was 20 bp insertion which replaced a ATTTT between nt 1831 and 1835. PMID: 16127747
we developed a p53R2-dependent luciferase reporter gene assay, and demonstrated dose-dependent luminescence caused by adriamycin in two human cell lines that express wild-type p53, MCF-7 and HepG2 PMID: 16236544
RRM2 and p53R2 subunits share the same binding site on RRM1 PMID: 16376858
Expressions of p53 and p53R2 proteins should be useful for determining the tumor properties, including prognosis, in patients with esophageal squamous cell carcinoma. PMID: 16778101
Catalytic properties are assessed. PMID: 16846634
ectopic expression of human papillomavirus 16 E6 impaired p53R2 induction after DNA damage in human fibroblasts PMID: 16872707
Mutation of RRM2B is associated with mitochondrial Diseases PMID: 17486094
p53R2 expression is reduced after X-ray irradiation following the transfection of p53R2 siRNAin esophageal squamous cell carcinoma. This could potentially improve efficacy of radiotheraepy. PMID: 17671702
a protective function of the p53R2 ribonucleotide reductase subunit in prevention or repair of NO-mediated genotoxic injury. PMID: 18474260
Sequencing the RRM2B gene revealed three missense mutations and two single nucleotide deletions in exons 6, 8, and 9, confirming that RRM2B mutations are important causes of MDS. PMID: 18504129
analysis of the effects of p53R2 silencing on DNA damage in LNCaP cells PMID: 18505925
p53R2 constitutes a potential target for anticancer drugs as well as a diagnostic marker in cancer. PMID: 18760875
The redox property, structure, and function of hRRM2 and p53R2, are studied. PMID: 19082948
This report describes two brothers, both deceased in infancy, with severe depletion of mitochondrial DNA (mtDNA) in muscle tissue. A novel missense mutation in the RRM2B gene, encoding the p53R2 subunit, was identified PMID: 19138848
A heterozygous truncating mutation in RRM2B causes autosomal-dominant progressive external ophthalmoplegia with multiple mtDNA deletions. PMID: 19664747
This study expands the clinical spectrum of impaired RIR2B function. PMID: 19667227
The X-ray crystal structure of human p53R2 is determined to 2.6 A, in which monomers A and B exhibit mono- and binuclear iron occupancy, respectively. Sequence-structure-function correlations that differentiate p53R2 and RRM2 are revealed. PMID: 19728742

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.