Recombinant Human RRM2 Protein (C-6His)

Name: Recombinant Human RRM2 Protein (C-6His)
Brand: Beta LifeScience
SKU: BL-0627NP
Availability: InStock

BL-0627NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: All products, High-quality recombinant proteins, Other 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

Description	Recombinant Human Ribonucleotide Reductase Small Chain is produced by our Mammalian expression system and the target gene encoding Met1-Phe389 is expressed with a 6His tag at the C-terminus.
Accession	P31350
Synonym	Ribonucleoside-Diphosphate Reductase Subunit M2; Ribonucleotide Reductase Small Chain; Ribonucleotide Reductase Small Subunit; RRM2; RR2
Gene Background	Ribonucleoside-Diphosphate Reductase Subunit M2 (RRM2) belongs to the ribonucleoside diphosphate reductase small chain family. The reductase of RRM2 catalyzes the formation of deoxyribonucleotides from ribonucleotides. Synthesis of the encoded protein (M2) is regulated in a cell-cycle dependent fashion. RRM2 supplies the precursors essential for DNA synthesis. RRM2 catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. Phosphorylation on Ser-20 relieves the inhibitory effect on Wnt signaling.
Molecular Mass	45.9 KDa
Apmol Mass	47 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of 20mM Tris-HCl, 150mM NaCl, 5% Trehalose, pH 8.0.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution	Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping	The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. Inhibits Wnt signaling.
Subcellular Location	Cytoplasm. Nucleus.
Protein Families	Ribonucleoside diphosphate reductase small chain family
Database References	HGNC: 10452 OMIM: 180390 KEGG: hsa:6241 STRING: 9606.ENSP00000353770 UniGene: PMID: 29767233 overexpression of RRM2 is associated with the genesis and progression of neuroblastoma, and may be a potential chemotherapeutic target PMID: 29749541 Data suggest that targeting of breast cancer 1, early onset protein (BRCA1)-ribonucleotide reductase regulatory subunit M2 (RRM2) axis may represent a paradigm for therapeutic intervention in glioblastoma (GBM). PMID: 27845331 These results demonstrate that gambogic acid sensitizes pancreatic cancer cells to gemcitabine in vitro and in vivo by inhibiting the activation of the ERK/E2F1/RRM2 signaling pathway. PMID: 28797284 OX2 and RRM2 are suggested to be prominent markers for breast cancer metastasis. PMID: 28782484 SLFN11 contributes to the sensitivity of Ewing sarcoma cells to inhibition of ribonucleotide reductase M2 PMID: 27557498 Results indicate CREB1 as a critical transcription factor of RRM2 which promotes tumor aggressiveness, and imply a significant correlation between CREB1 and RRM2 in CRC specimens. PMID: 27801665 These findings suggest that the identified APLP2, RRM2, and PRC1 signature could be useful for distinguishing between benign (follicular adenoma) and malignant (follicular carcionma and follicular variant of papillary carcinoma) tumors of the thyroid follicular epithelium. PMID: 27796194 Data show that inhibition of sphingosine kinase-2 by ABC294640 is synergistically cytotoxic with gemcitabine toward three pancreatic cancer cell lines, resulting in decreased expression of both ribonucleotide reductase regulatory subunit M2 (RRM2) and c-MYC protein (Myc) in all three cell lines. PMID: 27517489 Here we designed UC-rich and CU-rich 10-nt sequences for engagement of both RRM2 and RRM3 and demonstrated that the TIA-1 RRM23 construct preferentially binds the UC-rich RNA ligand. Together our data support a specific mode of TIA-1 RRM23 interaction with target oligonucleotides consistent with the role of TIA-1 in binding RNA to regulate gene expression PMID: 28184449 These data suggest that VASH2 reduces the chemosensitivity to gemcitabine in pancreatic cancer cells via JUN-dependent transactivation of RRM2. PMID: 28327155 HPV31 regulates RRM2 levels through expression of E7 and activation of the ATR-Chk1-E2F1 DNA damage response, which is essential to combat replication stress upon entry into S-phase. PMID: 27764728 To the best of our knowledge, this is the first study that investigated the relationship of RRM1 and RRM2 gene polymorphisms and Coronary artery disease (CAD). PMID: 27566080 The SCYL1- BP1 affects the cell cycle through increasing steady state levels of Cyclin F and RRM2 proteins, thus constituting a dual regulatory circuit. PMID: 25980818 A significant association has been found between RRM2 rs6759180 (located in the 5'UTR, 10126436G>A) and the risk for developing non-small cell lung cancer. PMID: 26718430 Data show that ribonucleotide reductase M2 (RRM2) is associated with increased nuclear factor kappa B (NF-kappaB) activity. PMID: 26333382 our findings establish a signaling role for RRM2 in gastric cancer cells and identify that the RRM2/AKT/NF-kappaB signaling pathway is essential for tumor invasiveness in gastric cancer cells PMID: 27348973 HBV exploits the Chk1-E2F1 axis of the DNA damage response pathway to induce R2 expression in a cell cycle-independent manner. PMID: 26026873 High expression level of RRM2 might be negative prognostic factor for resected NSCLC patients. PMID: 26663950 We suggest that MNNG-stimulated ATR/CHK1 signaling stabilizes E2F3 by S124 phosphorylation, and then E2F3 together with NFY co-transactivate RRM2 expression for DNA repair. PMID: 26921499 In non-small cell lung cancer, RRM2 expression was predictive of disease-specific survival in women, non-smokers and former smokers. Higher expression was associated with worse survival. This was not the case for men, and current or recently quit smokers. PMID: 26001082 These results suggested that RRM2 supported the growth of human OSCC cells and that targeting of RRM2, e.g., via GEM treatment, may be a promising therapeutic strategy for OSCC. PMID: 25738429 Understanding the role of E2F1 in activating RRM2 transcription will help to explain the relationship between E2F1 and RRM2 in colorectal cancer PMID: 26093293 R2 and p53R2 small subunits are subject to caspase-dependent degradation PMID: 25878246 Results showed that RRM2 overexpression impacted the survivability of breast cancer patients.[Meta-Analysis] PMID: 25213022 Our study suggests for evaluating RRM2-associated metabolites as noninvasive markers for tamoxifen resistance PMID: 25016594 RRM2 is a new molecular marker for the diagnosis and clinical outcomes of cervical cancer. It is involved in cervical carcinogenesis and predicts poor survival. PMID: 24637958 these findings suggest that RRM2 plays a crucial role in gastric tumorigenesis and may serve as a potential prognostic marker and therapeutic target in gastric cancer. PMID: 24756820 Data indicate that the expression of ribonucleotide reductase small subunit M2 (RRM2) positively associated with biochemical recurrence of prostate cancer (PCa). PMID: 24360663 HPVE7 induces upregulation of RRM2, which then promotes cervical carcinogenesis via ROS-ERK1/2-HIF-1alpha-VEGF-induced angiogenesis. PMID: 24423925 Data indicate that transfection of the wild-type M2 but not the K95E mutant rescued the G1/S phase cell cycle arrest and cell growth inhibition caused by the siRNA knockdown of M2. PMID: 24253041 RRM2 small interfering RNA-mediated treatment is an effective strategy to inverse chemosensitivity of tumor cells to cisplatin, enhance the efficacy of Gem-induced cytotoxicity and promote apoptosis of cisplatin-resistant ovarian cancer cells in vitro. PMID: 23466567 Our novel findings add to the knowledge of RRM2 in regulating expression of the antiapoptotic protein Bcl-2 and reveal a critical link between RRM2 and Bcl-2 in apoptosis signaling. PMID: 23719266 p21-mediated RNR2 repression restricts HIV-1 replication in macrophages by inhibiting dNTP biosynthesis pathway. PMID: 24082141 The crystal structure of RRM1/2 complexed with target mRNA has been solved; comparison of the two structures show that RNA-binding protein RRM1/2 undergoes conformational changes upon RNA binding. PMID: 23519412 RRM2 was found to be a key determinant of both inherent and acquired gemcitabine with reduced let-7 expression likely to contribute to RRM2-mediated inherent chemoresistance in poorly differentiated pancreatic cancer cells. PMID: 23335963 RRM2 may be a facilitating factor in colorectal tumorigenesis and UV-induced DNA damage repair. PMID: 23002339 High tumor expression of RRM2 and ERCC1 are associated with reduced recurrence free survival and overall survival after resection of pancreas cancer. PMID: 22569992 RRM2 expression closely correlates with the development of ovarian tumor and may serve as a novel predictive marker for diagnosis and prognosis of the disease. PMID: 22884145 After DNA damage, cyclin F is downregulated in an ATR-dependent manner to allow accumulation of RRM2. Defective elimination of cyclin F delays DNA repair and sensitizes cells to DNA damage, a phenotype that is reverted by expressing a nondegradable RRM2 mutant. PMID: 22632967 RRM2 protein expression in pancreatic adenocarcinoma is neither prognostic nor predictive of adjuvant gemcitabine benefit in patients with resectable pancreatic adenocarcinoma. PMID: 22670179 Recombinant RRM2 translocates from the cytoplasm to the nucleus in a time-dependent manner, leading to stabilization of urokinase mRNA. Overexpression of RRM2 inhibits urokinase protein and mRNA expression through destabilization of uPA mRNA. PMID: 22166006 Knockdown of the ribonucleotide RR2 subunit leads to decreased cisplatin-induced gap-filling synthesis in nucleotide excision repair and a reduced 2'-deoxyadenosine triphosphate (dATP) level in the G2/M phase of the cell cycle. PMID: 21875941 HDM-2 inhibition suppresses expression of ribonucleotide reductase subunit M2, and synergistically enhances gemcitabine-induced cytotoxicity in mantle cell lymphoma. PMID: 21844567 p53R2 expression seems more important than that of hRRM2 in prognosis of early-stage lung cancer. PMID: 21965764 Under serum-starved conditions, the expression level of RRM2 protein increased in HCT116 cells compared to HKe3 cells (HCT116 cells with a disruption in oncogenic KRAS), and the re-expression of KRAS in HKe3 cells induced the expression of RRM2. PMID: 21873171 We have shown frequent overexpression of RRM2 protein and its possible role in bladder cancer. PMID: 21166702 High RRM2 is associated with gemcitabine resistance in pancreatic cancer. PMID: 20927319 Ribonucleotide reductase M2 subunit overexpression could be associated with the gastric cancer progression. PMID: 20825972 This study correlates the distinct catalytic mechanisms of the small subunits hp53R2 and hRRM2 with a hydrogen-bonding network. PMID: 20484015

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.