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HEPPSO Sale

(Synonyms: 3-(羟乙基哌嗪)-2-羟基丙磺酸) 目录号 : GC60895

HEPPSO是一种两性离子缓冲剂。HEPPSO缓冲液的工作pH范围是7.1-8.5。HEPPSO显示出较高的结合铜(II)的能力,在2.0mM缓冲液浓度下的pKa值为7.84。

HEPPSO Chemical Structure

Cas No.:68399-78-0

规格 价格 库存 购买数量
10mM (in 1mL DMSO)
¥495.00
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500mg
¥450.00
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Sample solution is provided at 25 µL, 10mM.

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产品描述

HEPPSO is a zwitterionic buffer. The working pH range of HEPPSO buffer is 7.1-8.5. HEPPSO displays relatively high ability to bind copper(II), has a pKa of 7.84 at 2.0 mM buffer concentration[1][2].

[1]. Vasconcelos MT, et, al. Copper(II) complexation properties and surfactant activity of 3-[N, N-bis(2-hydroxyethyl)amino]-2-hydroxypropanesulfonic acid and N-(2-Hydroxyethyl)piperazine-N'-2-hydroxypropanesulfonic acid pH buffers which may affect trace metal speciation in in vitro studies. Anal Biochem. 1998 Dec 15; 265(2): 193-201. [2]. Mash HE, et, al. Complexation of copper by zwitterionic aminosulfonic (good) buffers. Anal Chem. 2003 Feb 1; 75(3): 671-7.

Chemical Properties

Cas No. 68399-78-0 SDF
别名 3-(羟乙基哌嗪)-2-羟基丙磺酸
Canonical SMILES O=S(CC(O)CN1CCN(CCO)CC1)(O)=O
分子式 C9H20N2O5S 分子量 268.33
溶解度 Water: 250 mg/mL (931.69 mM); DMSO: 250 mg/mL (931.69 mM) 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

制备储备液
1 mg 5 mg 10 mg
1 mM 3.7268 mL 18.6338 mL 37.2675 mL
5 mM 0.7454 mL 3.7268 mL 7.4535 mL
10 mM 0.3727 mL 1.8634 mL 3.7268 mL
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*在配置溶液时,请务必参考产品标签上、MSDS / COA(可在Glpbio的产品页面获得)批次特异的分子量使用本工具。

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动物体内配方计算器 (澄清溶液)

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)
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Research Update

Oligosaccharide binding in Escherichia coli glycogen synthase

Biochemistry 2009 Oct 27;48(42):10089-97.PMID:19761218DOI:10.1021/bi900916t.

Glycogen/starch synthase elongates glucan chains and is the key enzyme in the synthesis of glycogen in bacteria and starch in plants. Cocrystallization of Escherichia coli wild-type glycogen synthase (GS) with substrate ADPGlc and the glucan acceptor mimic HEPPSO produced a closed form of GS and suggests that domain-domain closure accompanies glycogen synthesis. Cocrystallization of the inactive GS mutant E377A with substrate ADPGlc and oligosaccharide results in the first oligosaccharide-bound glycogen synthase structure. Four bound oligosaccharides are observed, one in the interdomain cleft (G6a) and three on the N-terminal domain surface (G6b, G6c, and G6d). Extending from the center of the enzyme to the interdomain cleft opening, G6a mostly interacts with the highly conserved N-terminal domain residues lining the cleft of GS. The surface-bound oligosaccharides G6c and G6d have less interaction with enzyme and exhibit a more curled, helixlike structural arrangement. The observation that oligosaccharides bind only to the N-terminal domain of GS suggests that glycogen in vivo probably binds to only one side of the enzyme to ensure unencumbered interdomain movement, which is required for efficient, continuous glucan-chain synthesis.

Complexation of copper by zwitterionic aminosulfonic (good) buffers

Anal Chem 2003 Feb 1;75(3):671-7.PMID:12585500DOI:10.1021/ac0261101.

Copper binding properties were investigated for several popular zwitterionic buffers. The two buffers 4-morpholinoethanesulfonic acid (MES) and 3-N-morpholinopropanesulfonic acid (MOPS) did not bind copper and would be good choices for metal speciation studies within their operational pH range. Conversely, 3-(N-morpholino)-2-hydroxypropanesulfonic acid (MOPSO) was observed to weakly bind copper directly (log Kc 2.02). Moreover, strong copper binding was observed for 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid (HEPES), 4-(2-hydroxyethyl)piperazine-1-propanesulfonic acid (HEPPS), and N-(2-hydroxyethyl)piperazine-N'-(2-hydroxypropanesulfonic acid) (HEPPSO). Log Kc values range from 7.04 to 7.68 and are indicative of strong copper binding ligands. The latter buffer also exhibited weak binding characteristics with a log Kc of 2.05. The strong Cu binding ligands were present in HEPES, HEPPS, and HEPPSO at much lower concentrations than the total buffer concentration. MES, HEPES, MOPSO, and HEPPSO were analyzed by electrospray-ionization quadrapole time-of-flight mass spectroscopy. The most prominent feature of the spectra for each buffer analyzed was the presence of multiple oligomers, indicating a propensity of interaction between buffer molecules. In addition, the presence of several contaminants was identified in the mass spectrum of the HEPES matrix, including a prominent contaminant (at m/z 131) present in levels similar to those obtained from the modeling of the copper titration data. Other contaminants were found in the other matrixes but were not identified as possible copper binding agents.

Copper(II) complexation properties and surfactant activity of 3-[N, N-bis(2-hydroxyethyl)amino]-2-hydroxypropanesulfonic acid and N-(2-Hydroxyethyl)piperazine-N'-2-hydroxypropanesulfonic acid pH buffers which may affect trace metal speciation in in vitro studies

Anal Biochem 1998 Dec 15;265(2):193-201.PMID:9882392DOI:10.1006/abio.1998.2884.

Disadvantages of the some zwitterionic pH buffers are (i) that they can interact with metal ions as well as protons, and (ii) that they may have a surfactant effect in chemical or in vitro biological or biochemical studies. This has to be taken into account when a buffer is selected. Here, the copper-complexing capacity and the surfactant activity of three compounds, 3-[N,N-bis (2-hydroxyethyl)amino]-2-hydroxypropanesulfonic acid (DIPSO), N-(2-hydroxyethyl)piperazine-N'-(2-hydroxypropanesulfonic acid) (HEPPSO), and piperazine-N,N'-bis(2-ethanesulfonic acid) (Pipes), were investigated. Global stability constants (log betaabc) of copper(II)-buffer complexes were determined, at 25 degrees C, 0.5 M ionic strength, and at 0.8 mM buffer concentration, by pH and pCu ion-selective electrode measurements. Here, betaabc corresponds to the equilibrium: aCu2+ + bL- + cH+ left and right arrow (CuaLbHc)(2a-b+c); HL = DIPSO or HEPPSO; c: +1 = proton; -1 = hydroxide. Using SUPERQUAD constants were calculated, giving: DIPSO: log beta110 = 5.02, log beta120 = 8.99, log beta130 = 13.0, log beta140 = 16.3, log beta14-1 = 9.26, log beta14-2 = 0.645, log beta150 = 20.5, log beta160 = 24.3, log beta16-1 = 16.1, log beta16-2 = 8.98; HEPPSO: log beta110 = 4.29, log beta120 = 8.35, log beta130 = 12.1, log beta140 = 15.9, log beta150 = 19.6, log beta160 = 23.4, log beta16-1 = 14.9. The pKa values were determined at higher buffer concentrations, giving a value 7.33 for DIPSO and 7.84 for HEPPSO at 2.0 mM buffer concentration. Effects of buffer concentration on stability and acidity constants were investigated and compared with measurements using voltammetric and potentiometric stripping analysis, confirming no copper(II) complexation by Pipes. Surfactant activities were determined using alternating current polarography, confirming marked surface activity of 10 mM of DIPSO or HEPPSO.

Effect of zwitterionic buffers on measurement of small masses of protein with bicinchoninic acid

Anal Biochem 1986 Sep;157(2):291-4.PMID:3777432DOI:10.1016/0003-2697(86)90629-9.

Linear standard curves were obtained for 1 to 10 micrograms of bovine serum albumin measured in the presence of 50 mM Mes, Mops, Pipes, Caps, Bes, Hepes, HEPPSO, and Tes zwitterionic buffers using bicinchoninic acid for detection. The zwitterionic buffers Ada, Tricine, and Bicine that strongly bind Cu2+. Tris, and Bistris, each at 50 mM, inhibited color development to prevent quantitative measurement of protein mass.