纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | RRM2 |
Uniprot No | P31350 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-389aa |
氨基酸序列 | 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 |
预测分子量 | 47 kDa |
蛋白标签 | His tag N-Terminus |
缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
稳定性 & 储存条件 | 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. |
复溶 | 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. |
以下是关于RRM2重组蛋白的3篇参考文献示例(注:文献信息为模拟内容,实际引用时请核对准确性):
1. **《RRM2 promotes DNA damage response through modulating p53 activity》**
- 作者:Fan H, et al.
- 摘要:研究利用重组RRM2蛋白,揭示了其通过调控p53磷酸化参与DNA损伤修复的分子机制,为癌症治疗提供了新靶点。
2. **《Expression and purification of recombinant human RRM2 for functional studies》**
- 作者:Zhang Y, et al.
- 摘要:报道了人源RRM2重组蛋白在大肠杆菌中的高效表达与纯化方法,并验证其在体外催化核糖核苷酸还原的活性。
3. **《Targeting RRM2 overexpression enhances chemosensitivity in lung cancer》**
- 作者:Wang L, et al.
- 摘要:通过重组RRM2蛋白的体外实验,证明抑制RRM2可增强肺癌细胞对吉西他滨的敏感性,提示其作为化疗增敏剂的潜力。
**注意**:以上文献信息为示例,实际研究中建议通过PubMed或Web of Science等平台检索最新文献,并核实作者、标题及摘要的准确性。
**Background of Recombinant RRM2 Protein**
Ribonucleotide reductase regulatory subunit M2 (RRM2) is a critical component of the ribonucleotide reductase (RNR) enzyme complex, which plays an essential role in DNA synthesis and repair by catalyzing the conversion of ribonucleotides to deoxyribonucleotides. As a regulatory subunit, RRM2 works in conjunction with the catalytic subunit RRM1 to maintain optimal dNTP pool balance, ensuring genomic stability and cell cycle progression. Its expression is tightly regulated during the cell cycle, peaking in the S phase to meet the high demand for DNA replication. Dysregulation of RRM2 has been linked to various cancers, where its overexpression is associated with tumor proliferation, metastasis, and resistance to chemotherapy.
Recombinant RRM2 protein is produced using genetic engineering techniques, typically through expression in bacterial or mammalian systems, followed by purification to ensure high specificity and activity. This engineered protein retains the functional properties of native RRM2. enabling researchers to study its biochemical interactions, enzymatic mechanisms, and regulatory roles in vitro. Recombinant RRM2 is widely utilized in structural studies, enzyme activity assays, and screening for inhibitors that could target RNR as a therapeutic strategy. Additionally, it serves as a vital tool for investigating RRM2's interplay with other proteins, such as tumor suppressors or oncogenic signaling molecules, in pathways related to DNA damage response and cell survival.
The development of recombinant RRM2 has significantly advanced cancer research, particularly in understanding chemoresistance mechanisms and identifying novel anticancer agents. By modulating RRM2 activity, researchers aim to disrupt cancer cell proliferation while sparing normal cells, offering a potential avenue for precision therapies. Its role in maintaining genomic integrity also underscores its relevance in studying aging, neurodegenerative diseases, and other conditions linked to DNA repair defects. Overall, recombinant RRM2 remains a cornerstone protein in both basic and translational biomedical research.
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