N2,N2-Dimethylguanosine
(Synonyms: N2,N2-二甲基鸟苷) 目录号 : GC33140
A methylated purine nucleoside
Cas No.:2140-67-2
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >99.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
N2,N2-Dimethylguanosine is a methylated purine nucleoside formed during the degradation of tRNA.1 Serum levels of N2,N2-dimethylguanosine are elevated in patients with acute myelomonocytic leukemia (AMML) or large cell lung carcinoma.
1.Mitchell, E.P., Evans, L., Schultz, P., et al.Modified nucleosides in human serumJ. Chromatogr.581(1)31-40(1992)
| Cas No. | 2140-67-2 | SDF | |
| 别名 | N2,N2-二甲基鸟苷 | ||
| Canonical SMILES | OC[C@@H]1[C@H]([C@H]([C@H](N2C=NC3=C2N=C(N(C)C)NC3=O)O1)O)O | ||
| 分子式 | C12H17N5O5 | 分子量 | 311.29 |
| 溶解度 | DMSO : 15 mg/mL (48.19 mM) | 储存条件 | 4°C, protect from light |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 储备液的保存方式和期限：-80°C 储存时，请在 6 个月内使用，-20°C 储存时，请在 1 个月内使用。 为了提高溶解度，请将管子加热至37℃，然后在超声波浴中震荡一段时间。 |
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| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 制备储备液 | |||
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1 mg | 5 mg | 10 mg |
| 1 mM | 3.2124 mL | 16.0622 mL | 32.1244 mL |
| 5 mM | 0.6425 mL | 3.2124 mL | 6.4249 mL |
| 10 mM | 0.3212 mL | 1.6062 mL | 3.2124 mL |
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
| 第二步：请输入动物体内配方组成（配方适用于不溶于水的药物；不同批次药物配方比例不同，请联系GLPBIO为您提供正确的澄清溶液配方） | ||||||||||
| % DMSO % % Tween 80 % saline | ||||||||||
| 计算重置 | ||||||||||
计算结果:
工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
一定要按照顺序依次将溶剂加入，进行下一步操作之前必须保证上一步操作得到的是澄清的溶液，可采用涡旋、超声或水浴加热等物理方法助溶。
3. 以上所有助溶剂都可在 GlpBio 网站选购。
Enzymatic formation of N2,N2-Dimethylguanosine in eukaryotic tRNA: importance of the tRNA architecture
Biochimie 1995;77(1-2):54-61.PMID:7599276DOI:10.1016/0300-9084(96)88104-1.
In eukaryotic tRNA, guanosine at position 26 in the junction between the D-stem and the anticodon stem is mostly modified to N2,N2-Dimethylguanosine (m2(2)G26). Here we review the available information on the enzyme catalyzing the formation of this modified nucleoside, the SAM-dependent tRNA (m2(2)G26)-methyltransferase, and our attemps to identify the parameters in tRNA needed for efficient enzymatic dimethylation of guanosine-26. The required identity elements in yeast tRNA for dimethylation under in vitro conditions by the yeast tRNA(m2(2)G26)-methyltransferase (the TRM1 gene product) are comprised of two G-C base pairs at positions G10-C25 and C11-G24 in the D-stem together with a variable loop of at least five nucleotides. These positive determinants do not seem to act via base specific interactions with the methyltransferase; they instead ensure that G26 is presented to the enzyme in a favorable orientation, within the central 3D-core of the tRNA molecule. The anticodon stem and loop is not involved in such an interaction with the enzyme. In a heterologous in vivo system, consisting of yeast tRNAs microinjected into Xenopus laevis oocytes, the requirements for modification of G26 are less stringent than in the yeast homologous in vitro system. Indeed, G26 in several microinjected tRNAs becomes monomethylated, while in yeast extracts it stays unmethylated, even after extensive incubation. Thus either the X laevis tRNA(m2(2)G26)-methyltransferase has a more relaxed specificity than its yeast homolog, or there exist two distinct G26-methylating activities, one for G26-monomethylation, and one for dimethylation of G26.(ABSTRACT TRUNCATED AT 250 WORDS)
The tRNA N2,N2-dimethylguanosine-26 methyltransferase encoded by gene trm1 increases efficiency of suppression of an ochre codon in Schizosaccharomyces pombe
FEBS Lett 1999 Dec 24;464(1-2):67-70.PMID:10611485DOI:10.1016/s0014-5793(99)01679-8.
In the majority of eukaryotic tRNAs, the guanosine at position 26 is modified by a dimethyl group, but so far a function of this modification has not been detected. We isolated the Schizosaccharomyces pombe gene, trm1, encoding the tRNA N2, N2-dimethylguanosine-26 methyltransferase. Strains having the gene deleted completely lack N2,N2-Dimethylguanosine. In strains carrying the weak ochre tRNA suppressor sup3-i, deletion of trm1 abolishes suppression indicating that the trm1 deletion acts as an antisuppressor mutation. The result suggests that in vivo N2, N2-dimethylguanosine-26 increases the capacity of the sup3-i serine tRNA to translate the UAA (ochre) codon.
Isolation and characterization of the TRM1 locus, a gene essential for the N2,N2-Dimethylguanosine modification of both mitochondrial and cytoplasmic tRNA in Saccharomyces cerevisiae
J Biol Chem 1986 Jul 25;261(21):9703-9.PMID:2426253doi
The trm1 mutation of Saccharomyces cerevisiae is a single nuclear mutation that affects a specific base modification of both cytoplasmic and mitochondrial tRNA. Transfer RNA isolated from trm1 cells lacks the modified base N2,N2-Dimethylguanosine, and extracts from these cells do not have detectable N2,N2-dimethylguanosine-specific tRNA methyltransferase activity. As part of our efforts to determine how this mutation affects enzyme activities in two different cellular compartments we have isolated the TRM1 locus by genetic complementation. The TRM1 locus restores the N2,N2-Dimethylguanosine modification to both cytoplasmic and mitochondrial tRNA in trm1 cells. An open reading frame in this TRM1 gene is essential for complementation of the trm1 phenotype. Expression of this open reading frame in Escherichia coli converts the organism from one that neither makes N2,N2-Dimethylguanosine nor has N2,N2-dimethylguanosine-specific tRNA methyltransferase activity into one that does. This result suggests that the TRM1 locus is the structural gene for the tRNA modification enzyme and that both nuclear/cytoplasmic and mitochondrial forms of the methyltransferase are produced from the same gene.
Serum levels of N2, N2-dimethylguanosine and pseudouridine as determined by radioimmunoassay for patients with malignancy
J Natl Cancer Inst 1975 Feb;54(2):341-3.PMID:1117461doi
A sensitive, rapid, and specific radioimmunoassay procedure was used to determine levels of N2,N2-Dimethylguanosine and pseudouridine in sera of patients with acute leukemia and breast cancer. Elevated levels of both nucleosides were above standard deviations of the normal mean for patients in both disease categories.
Amino-terminal extension generated from an upstream AUG codon is not required for mitochondrial import of yeast N2,N2-dimethylguanosine-specific tRNA methyltransferase
Proc Natl Acad Sci U S A 1987 Aug;84(15):5172-6.PMID:3299379DOI:10.1073/pnas.84.15.5172.
The TRM1 gene of Saccharomyces cerevisiae is necessary for the N2,N2-Dimethylguanosine modification of both mitochondrial and cytoplasmic tRNAs. The DNA sequence of the TRM1 locus and the 5' ends of mRNAs expressed from this gene have been determined. The majority of the 5' ends map within a large open reading frame between two in-frame ATGs at positions +1 and +49. A small fraction of the 5' ends are located upstream of the first ATG. Both AUGs of the TRM1 mRNAs are used to initiate translation, and two forms of N2,N2-dimethylguanosine-specific tRNA methyltransferase, which differ by an amino-terminal extension of 16 amino acids, are made. Mitochondrial tRNAs are modified when the initiation of translation is limited to one or the other of the AUGs, suggesting that the amino-terminal extension is not necessary for import of the protein into mitochondria. Mitochondrial targeting information must, therefore, be located in a region of N2,N2-dimethylguanosine-specific tRNA methyltransferase that is found in both forms of the enzyme.