TAPSO
目录号 : GC67631
TAPSO 是一种常用的生物缓冲剂和 pH 稳定试剂，有效 pH 范围为 7-8，pKa 范围为 7.5-9。TAPSO 具有 Tris 基团，表现出相当的反应活性，能够与两性离子甘氨酸肽相互作用。
Cas No.:68399-81-5
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >98.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
TAPSO is a common biological buffer, a pH stabilization reagent, with effective pH ranging from 7-8, and pKa values ranging from 7.5-9.0. TAPSO contains Tris groups and exhibits quite reactive activity with zwitterionic glycine peptides[1].
[1]. Machado CM, et al. Interpretation of non-Nernstian slopes in graphic analysis of data collected in pH range close to deprotonation of a ligand Part I. A glass electrode potentiometric and polarographic study of Cd-(TAPSO)x-(OH)y and Zn-(TAPSO)x-(OH)y syst
| Cas No. | 68399-81-5 | SDF | Download SDF |
| 分子式 | C7H17NO7S | 分子量 | 259.28 |
| 溶解度 | 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 | 3.8568 mL | 19.2842 mL | 38.5683 mL |
| 5 mM | 0.7714 mL | 3.8568 mL | 7.7137 mL |
| 10 mM | 0.3857 mL | 1.9284 mL | 3.8568 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。
Triple Archives Particle Swarm Optimization
IEEE Trans Cybern 2020 Dec;50(12):4862-4875.PMID:31613789DOI:10.1109/TCYB.2019.2943928.
There are two common challenges in particle swarm optimization (PSO) research, that is, selecting proper exemplars and designing an efficient learning model for a particle. In this article, we propose a triple archives PSO (TAPSO), in which particles in three archives are used to deal with the above two challenges. First, particles who have better fitness (i.e., elites) are recorded in one archive while other particles who offer faster progress, called profiteers in this article, are saved in another archive. Second, when breeding each dimension of a potential exemplar for a particle, we choose a pair of elite and profiteer from corresponding archives as two parents to generate the dimension value by ordinary genetic operators. Third, each particle carries out a specific learning model according to the fitness of its potential exemplars. Furthermore, there is no acceleration coefficient in TAPSO aiming to simplify the learning models. Finally, if an exemplar has excellent performance, it will be regarded as an outstanding exemplar and saved in the third archive, which can be reused by inferior particles aiming to enhance the exploitation and to save computing resources. The experimental results and comparisons between TAPSO and other eight PSOs on 30 benchmark functions and four real applications suggest that TAPSO attains very promising performance in different types of functions, contributing to both higher solution accuracy and faster convergence speed. Furthermore, the effectiveness and efficiency of these new proposed strategies are discussed based on extensive experiments.
Interpretation of non-Nernstian slopes in graphic analysis of data collected in pH range close to deprotonation of a ligand Part I. A glass electrode potentiometric and polarographic study of Cd-(TAPSO)x-(OH)y and Zn-(TAPSO)x-(OH)y systems
Talanta 2006 Jan 15;68(3):819-30.PMID:18970396DOI:10.1016/j.talanta.2005.06.003.
In this work, the complexation of cadmium and zinc ions by 3-[N-tris(hydroxymethyl)methylamine]-2-hydroxypropanesulfonic acid (TAPSO), a commercial biological buffer, was evaluated using three electrochemical techniques, at fixed total-ligand and total-metal concentration ratio and varied pH, at 25.0+/-0.1 degrees C and ionic strength set to 0.1M KNO(3). For both metal-ligand systems, complexation was evidenced in the pH range close to deprotonation of the ligand and the final models were optimised after a meticulous graphical analysis. For Cd-(TAPSO)(x)-(OH)(y) system, two complexes, CdL and CdL(2), were identified in the buffering region of the ligand. The proposed final model for this system is: CdL, CdL(2) and CdL(2)(OH) with stability constants, as logbeta, of 2.2, 4.2 and 8.6, respectively. For Zn-(TAPSO)(x)-(OH)(y) system, the complex ZnL is the main species formed in the buffering pH range. The proposed final model is ZnL, ZnL(OH) and ZnL(OH)(2) with overall refined stability constants (as logbeta) to be: 2.5, 7.2 and 13.2, respectively.
Interactions of TRIS [tris(hydroxymethyl)aminomethane] and related buffers with peptide backbone: thermodynamic characterization
Phys Chem Chem Phys 2010 Oct 21;12(39):12840-50.PMID:20820555DOI:10.1039/c0cp00253d.
In a situation which is far from ideal, many buffers have been found to be quite reactive, besides maintaining their stable pH values. On the basis of apparent transfer free energies (ΔG(tr)'), through solubility measurements the interactions of zwitterionic glycine peptides: glycine (Gly), diglycine (Gly(2)), triglycine (Gly(3)), and tetraglycine (Gly(4)), with several common neutral pH, amine-based buffers have been studied. The biological buffers studied in this work, including TRIS, TES, TAPS, TAPSO, and TABS are structurally related and all contain TRIS groups. These buffers have pK(a) values ranging from 7.5-9.0, which allow them to be used in biological, biochemical or environmental studies. We observed negative values of ΔG(tr)' for Gly(3) and Gly(4) from water to buffer, indicating that the interactions are favorable. However, the ΔG(tr)' values are positive for Gly and Gly(2), revealing unfavorable interactions, which except for the latter in TRIS buffer are negative. The surprising result in our data is the unexpected extraordinarily high favorable interactions between TRIS buffer and peptides (in comparison with the effect of the most common denaturants, urea and guanidine hydrochloride). The transfer free energies (ΔG(tr)') of the peptide backbone unit (-CH(2)C=O-NH-) contributions have been estimated from ΔG(tr)' values. We have also investigated the interactions of TRIS buffer with Bovine Serum Albumin (BSA), as a globular protein, using dynamic light scattering (DLS), zeta potential, UV-Visible absorption, fluorescence and Raman spectroscopy measurements. The results indicated that TRIS buffer stabilized the BSA molecules.
Effects of oxygen and transition metals on the advanced Maillard reaction of proteins with glucose
Biosci Biotechnol Biochem 1996 Nov;60(11):1820-5.PMID:8987858DOI:10.1271/bbb.60.1820.
The generation of fluorescence and 3-deoxyglucosone (3DG), browning, polymerization, and impairment of the amino acid residues of lysozyme incubated with glucose were investigated at 37 degrees C and 50 degrees C at pH 7.4 in a phosphate or TAPSO buffer under aerobic and non-aerobic conditions with or without DETAPAC as a chelating reagent. Browning, the generation of fluorescence, and polymerization were accelerated under the non-aerobic, compared to aerobic, conditions. Moreover, the formation of 3DG was also significantly increased under non-aerobic conditions. The incubation of both reaction systems resulted in noticeable losses of arginine and lysine residues. DETAPAC significantly inhibited the advanced Maillard reaction under both aerobic and non-aerobic conditions. However, DETAPAC had no effect on the impairment of lysine and arginine residues. The generation of fluorescence, browning and polymerization of lysozyme in the TAPSO buffer were markedly inhibited under both aerobic and non-aerobic conditions. These observations suggest that transition metals in the phosphate buffer may have accelerated the formation of Amadori compounds via Schiff's base. In addition, under non-aerobic conditions, the formation of advanced glycation end products from 3DG via Amadori compounds is presumed to be the major pathway, because the formation of N epsilon-(carboxymethyl)lysine, glyoxal, and glucosone was accelerated by an oxidative reaction catalyzed with transition metal ions. These presumptions are supported by the results from a lysozyme-3DG reaction system.
Synthetic organic pH buffers can support fertilization of guinea pig eggs, but not as efficiently as bicarbonate buffer
Gamete Res 1988 Feb;19(2):123-9.PMID:3209176DOI:10.1002/mrd.1120190203.
Bicarbonate ions (HCO3-) in the medium are not absolutely essential for the fertilization of guinea pig eggs. However, fertilization takes place most efficiently in HCO3- -buffered medium. Capacitation, the acrosome reaction, and zona penetration by spermatozoa can occur in HCO3- -free media with synthetic organic buffers (i.e., MOPS, TES, HEPES, Tris, and TAPSO) but not as efficiently as in the HCO3- -buffered medium. It appears that HCO3- functions as more than just a pH-buffering molecule.