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D-Fructose-6-phosphate (sodium salt) Sale

(Synonyms: D-果糖-6-磷酸二钠) 目录号 : GC43431

D-Fructose-6-phosphate(钠盐)是一种内源性代谢物。

D-Fructose-6-phosphate (sodium salt) Chemical Structure

Cas No.:26177-86-6

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10mM (in 1mL Water)
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50mg
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产品描述

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.

Chemical Properties

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。
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。

溶解性数据

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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
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Research Update

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.