Recombinant Human Ribonucleoside-Diphosphate Reductase Subunit M2 B (RRM2B) Protein (GST)

Name: Recombinant Human Ribonucleoside-Diphosphate Reductase Subunit M2 B (RRM2B) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-08824P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Ribonucleoside-Diphosphate Reductase Subunit M2 B (RRM2B) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q7LG56
Target Symbol	RRM2B
Synonyms	DKFZp686M05248; MGC102856; MGC42116; MTDPS8A; MTDPS8B; p53 inducible ribonucleotide reductase small subunit 2 homolog; p53 inducible ribonucleotide reductase small subunit 2 like protein; P53 inducible ribonucleotide reductase small subunit 2 short form beta; p53 R2; p53-inducible ribonucleotide reductase small subunit 2-like protein; p53R2; Ribonucleoside diphosphate reductase M2 subunit B; Ribonucleoside-diphosphate reductase subunit M2 B; Ribonucleotide reductase M2 B (TP53 inducible); Ribonucleotide reductase M2 B; Ribonucleotide reductase small subunit like 2 p53 inducible; RIR2B_HUMAN; RRM 2B; RRM2B; TP53 inducible ribonucleotide reductase M2 B; TP53-inducible ribonucleotide reductase M2 B
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	MGDPERPEAAGLDQDERSSSDTNESEIKSNEEPLLRKSSRRFVIFPIQYPDIWKMYKQAQASFWTAEEVDLSKDLPHWNKLKADEKYFISHILAFFAASDGIVNENLVERFSQEVQVPEARCFYGFQILIENVHSEMYSLLIDTYIRDPKKREFLFNAIETMPYVKKKADWALRWIADRKSTFGERVVAFAAVEGVFFSGSFAAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFQYLVNKPSEERVREIIVDAVKIEQEFLTEALPVGLIGMNCILMKQYIEFVADRLLVELGFSKVFQAENPFDFMENISLEGKTNFFEKRVSEYQRFAVMAETTDNVFTLDADF
Expression Range	1-351aa
Protein Length	Full Length
Mol. Weight	67.7kDa
Research Area	Epigenetics And Nuclear Signaling
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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: 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

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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.

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