D-Fructose-6-phosphate (sodium salt)
(Synonyms: D-果糖-6-磷酸二钠) 目录号 : GC43431D-Fructose-6-phosphate(钠盐)是一种内源性代谢物。
Cas No.:26177-86-6
Sample solution is provided at 25 µL, 10mM.
Quality Control & SDS
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- Purity: >99.00%
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- SDS (Safety Data Sheet)
- Datasheet
D-Fructose-6-phosphate is a sugar intermediate of the glycolytic pathway formed by the isomerization of glucose-6-phosphate. It is in turn further phosphorylated to fructose-1,6-bisphosphate, which is one of the rate-limiting steps in glycolysis. Because cancer cells adopt glycolysis as a major source of metabolic energy production, this pathway has become a new target for cancer chemotherapy. D-Fructose-6-phophate can be used to help identify, differentiate, and characterize the enzymes in this process.
Cas No. | 26177-86-6 | SDF | |
别名 | D-果糖-6-磷酸二钠 | ||
Canonical SMILES | [O-]CC([C@H]([C@@H]([C@@H](COP(O)(O)=O)O)O)[O-])=O.[Na+].[Na+] | ||
分子式 | C6H11O9P•2Na | 分子量 | 304.1 |
溶解度 | ≤100mg/ml in Water | 储存条件 | Store at -20°C |
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 | |||
1 mg | 5 mg | 10 mg | |
1 mM | 3.2884 mL | 16.442 mL | 32.8839 mL |
5 mM | 0.6577 mL | 3.2884 mL | 6.5768 mL |
10 mM | 0.3288 mL | 1.6442 mL | 3.2884 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。
Activation of Thermus phosphofructokinase by monovalent cations
Biochim Biophys Acta 1979 Jul 11;569(1):6-12.PMID:157165DOI:10.1016/0005-2744(79)90075-5.
The presence of the monovalent cations Tl+, NH+4, K+, Rb+ or Cs+, in decreasing order of potency, produce a marked equivalent increase in the specific enzyme activity of phosphofructokinase (ATP:D-Fructose-6-phosphate 1-phosphotransferase, EC 2.7.1.11) purified from extreme thermophile, Thermus X-1. By contrast, the monovalent cations Li+, Na+ or CH3NH+3 produce no detectable catalyitic activation at concentrations up to 100 mM. The relative potency of these cations suggests that each polypeptide chain in the tetrameric enzyme possesses a cationbinding site having tetragonal symmetry and that the protein ligands are principally hydroxyl or carboxylate oxygens. Only the enzyme-cation complex and not the enzyme by itself exhibits cooperativity with respect to the dependence of catalytic rate on the concentration of the substrate, fructose 6-phosphate. In the presence of subsaturating but not saturating concentrations of substrate, the catalytic activation produced by monovalent cations is also cooperative. Exclusion chromatographic measurements indicate that the enzyme remains tetrameric at catalytic concentrations in the presence or absence of an activating monovalent cation.
The Arxula adeninivorans ATAL gene encoding transaldolase-gene characterization and biotechnological exploitation
Appl Microbiol Biotechnol 2007 Apr;74(6):1292-9.PMID:17221198DOI:10.1007/s00253-006-0785-8.
The yeast Arxula adeninivorans provides an attractive expression platform and can be exploited as gene source for biotechnologically interesting proteins. In the following study, a striking example for the combination of both aspects is presented. The transaldolase-encoding A. adeninivorans ATAL gene, including its promoter and terminator elements, was isolated and characterized. The gene includes a coding sequence of 963 bp encoding a putative 321 amino acid protein of 35.0 kDa. The enzyme characteristics analyzed from isolates of native strains and recombinant strains overexpressing the ATAL gene revealed a molecular mass of ca. 140 kDa corresponding to a tetrameric structure, a pH optimum of ca. 5.5, and a temperature optimum of 20 degrees C. The preferred substrates for the enzyme include D-erythrose-4-phosphate and D-Fructose-6-phosphate, whereas D-glyceraldehyde is not converted. The ATAL expression level under salt-free conditions was observed to increase in media supplemented with 5% NaCl rendering the ATAL promoter attractive for moderate heterologous gene expression under high-salt conditions. Its suitability was assessed for the expression of a human serum albumin (HSA) reporter gene.
Sucrose may play an additional role to that of an osmolyte in Synechocystis sp. PCC 6803 salt-shocked cells
Plant Physiol Biochem 2005 Feb;43(2):133-8.PMID:15820660DOI:10.1016/j.plaphy.2005.01.008.
The role of sucrose in cyanobacteria is still not fully understood. It is generally considered a salt-response molecule, and particularly, in Synechocystis sp. strain PCC 6803, it is referred as a secondary osmolyte. We showed that sucrose accumulates transiently in Synechocystis cells at early stages of a salt shock, which could be ascribed to salt activation of sucrose-phosphate synthase (SPS, UDP-glucose: D-Fructose-6-phosphate 2-alpha-D-glucosyltransferase; EC 2.4.1.14), the key enzyme in sucrose synthesis pathway, and to an increase of the expression of the SPS encoding gene. Experiments with a mutant strain impaired in sucrose biosynthesis showed that sucrose is essential in stationary phase cells to overcome a later salt stress. Taken together, these results led us to suggest a more intricate function for sucrose than to be an osmoprotectant compound.