其他检测

今天分享下如何处理玻璃底培养皿、如何选择玻璃底培养皿，让细胞妥妥地贴壁，大家做共聚焦时候能够更得心应手。

细胞的免疫荧光实验是一个基础的细胞实验，传统的方法是在培养板中放入预先处理好的盖玻片，待细胞贴壁后，使用镊子将盖玻片拿出再开始进行固定，染色等系列工作。

是德科技的FE-SEM 8500采用热场发射电子枪，为用户提供高亮度、高分辨的成像性能。独特的设计使其可以在1kV条件下达到优于10nm的分辨率。创新的全静电透镜设计保证了重复性，并无需定期的调校。FE-SEM 8500提供多种成像模式：包括二次电子成像、背散射电子成像和形貌成像。

文章中采用了内皮细胞和巨噬细胞做为实验细胞。将细胞培养在ibidi通道载玻片中，之后使用含有纳米颗粒的培养基，以一定的剪切力刺激细胞，细胞吸收的纳米颗粒的量比静置状态下有显著的升高。 分享一下这个实验的细节，或许大家可以从中找到自己研究领域的灵感。

激光共聚焦显微镜可以观察到细胞内已经标记好的蛋白质和分子，为生物学研究提供了更直观的观测方法。如今，激光共聚焦成像已经是一个非常常规的实验操作，应用于生物学各个研究领域中。 在细胞实验中，如果要进行一次激光共聚焦成像，除了要知道相关的显微镜参数设置和操作以外，样品的准备也是非常重要的一环。

是德科技UTM T150 纳米力学测试系统适用于对多种材料的微纳米力学特性进行表征。T150系统对样品进行精确加载，在设计范围内对样品的静态和动态微拉伸和压缩性能进行精确测试与分析。 T150系统支持行业内最大的动态载荷范围（500mN），和市场上最高的测试精度（储存模量和损耗模量的测试范围横跨5个数量级），通过对各点进行精确测量，可对多种材料的动态性能进行分析。此外，T150系统也广泛用于对生物材料的拉伸/压缩性能进行测试。

是德科技AFM系列都可以选择配有专用接口平台，可方便地将高精度AFM成像部件直接与各类倒置显微镜联用，从而实现多种显微手段同时成像，既可以得到光学的明场像、暗场像、荧光图或激光共聚焦图，又可以轻松获得原子力图像；对用一个样品的同一个位置同时原位得到高衬度的光学图和高分辨的AFM图，这是生命科学领域用户最心仪的显微解决方案。 是德科技AFM还具有很强的兼容性，可与各个厂商的倒置显微镜和激光共聚焦联用，也可支持FRET，暗场和明场成像多种光学附件功能。

傅立叶变换红外 (FTIR) 成像是一项成熟的分析方法，可同时获得微米级范围的光谱和空间信息。这一技术已广泛用于多种不同的应用领域，从高分子科学到生物医学成像。近年来，人们越来越关注通过主要使用基于同步加速器的系统，来提高受到衍射极限制约的 FTIR 成像系统的空间分辨率。 在本应用简报中，我们展示了一项使用现有物镜实现放大增强的新型方法。最终，我们的 FTIR 系统显示出 1 ?m/像素级别的高空间分辨率成像能力。独特的是，这种构造在设置不同的放大倍率时不需更换物镜，从而保持了常规物镜相对较大的工作距离（约 21 mm）。

在细胞观察实验中，常常需要找回之前观察过的某个细胞。ibidi带格子培养皿可以让你快速找到你想要的细胞

对于HUVEC细胞而言，流动剪切力的培养环境更为贴近其自然生长的环境，我们实验说明在静置状态下并不能完全展现出HUVEC细胞的生理特性。

细胞趋化性（Chemotaxis，亦被称为化学趋向性）是趋向性的一种，指细胞、细菌及其他单细胞、多细胞生物依据环境中某些化学物质而趋向的运动。趋化性对细胞的发展和其他正常功能一样不可或缺。

细胞趋化性（Chemotaxis，亦被称为化学趋向性）是趋向性的一种，指细胞、细菌及其他单细胞、多细胞生物依据环境中某些化学物质而趋向的运动。趋化性对细胞的发展和其他正常功能一样不可或缺。

通过差示扫描量热仪（DSC）使用CSC Nano-DSC III测定蛋白质的热力学参数，需要大量相同的蛋白质做表面等离子体共振或荧光研究。由于Nano-DSC III 高度的敏感性和基线重复性，以及样品池的小体积(300 μL)和毛细管配置（能够延迟不可逆的蛋白质聚合和沉淀），一个完整的、可判断的、准确的扫描可以得到基本上所有的想要测试的蛋白质。?

通过活体组织提供一个直接的的定量检测同时测量热率产生和氧气利用率，意味着在代谢状态下面对改变生理和环境条件检测细微变化。The ratio of calorimetrically measured heat flux to the respirometrically measured oxygen flux is often called the “calorimetric-respirometric ratio” or CR ratio.

通过研究Methanosarcina mazei CorA 转运蛋白在两种洗涤剂中的四级结构，得到了相关谱图。对于同源CorA 的晶体结构研究表明，该功能蛋白以五聚体的形式存在，可引导离子跨过细胞膜。

多角度激光检测器与准弹性光散射（QELS）组件联用时，通过测定样品的流体力学半径和均方旋转半径，我们可以得到高分子的结构信息。在这篇应用文摘中，我们将会报道如何使用WYATT 的在线QELS 评价SEC 分离效果的好坏以及判断蛋白的构象。

The expression or replication of genes is affected by the binding of small molecule ligands and proteins to nucleic acid sequences. Such binding events are critical for the physiological integrity of organisms and therefore are of fundamental interest to life scientists. Recently, the thermodynamics driving these interactions have also become important to pharmaceutical scientists investigating the anticancer, antibacterial and antiviral potential of nucleic acid/ligand interactions. In addition, as the number of diseases identified as being due to a malfunction of cellular control processes increases, the possibility of treating disorders by manipulating gene expression is further focusing attention on the thermodynamics underlying nucleic acid binding affinity and specificity.

Simultaneous measurements of the rates of heat production and oxygen utilization by living tissues provides a direct quantitative means of detecting subtle changes in metabolic state in the face of altered physiological and environmental conditions. The ratio of calorimetrically measured heat flux to the respirometrically measured oxygen flux is often called the “calorimetric-respirometric ratio” or CR ratio. This can be used to partition total metabolic energy flux into its aerobic and anaerobic components by comparison of the experimental CR ratio with the theoretical “oxycaloric equivalent” for fully aerobic respiration. Such information is most important when evaluating the physiological effect of environmental stress.

Microcalorimetric instruments and methods are now essential tools for the general understanding of binding thermodynamics of biological macromolecules and specific biological systems. Provided that the enthalpy of binding is of appropriate magnitude, it is possible to determine affinities, KD, in the order of 10 nM (K=l08 M-1) for 1:1 complexes. One of the most important issues with ITC is the time needed to obtain a full binding isotherm. ITC inherently suffers from the relatively small number of binding experiments that are possible to perform per day. The focus has so far been on improving calorimetric response time of the instruments by various means, like assigning instrumental time constants and applying Tian’s equation to dynamically correct the raw calorimetric signal from a fast step-wise titration. Notably, nothing has so far been done to improve the experimental procedure. At the moment 2-3 h is needed to complete an ITC binding experiment. The number of data points that can be obtained, 20-30 points, limits the range of equilibrium constants that can be resolved from the data. For ITC this range is 1 ≤ KCM ≤ 1000, where K is the equilibrium constant and CM is the concentration of the reactant in the vessel. In this Application Note we show the possibility to shorten the time of an ITC experiment by slow continuous titration into the calorimetric vessel, cITC.

Proteomics research is uncovering a vast array of new proteins, including enzymes. It is now clear that the old assumption that one gene encodes one protein in incorrect. One gene can encode for several proteins, and many proteins have multiple functions: which function is displayed is controlled by the protein’s molecular environment. The structure and function of a protein are controlled by interactions with macromolecules such as other proteins, nucleic acids and lipids. Studying a protein in isolation (for example, obtaining the crystal or NMR structure of a purified protein) is critical to establishing a structural basis for the protein’s function(s). However, true functional characterization of the protein generally requires manipulation of multi-component systems under stringently-controlled conditions, and evaluating the roles of the physical characteristics of the protein. Proteomics has highlighted the need for a technique that can quantify the interactions between molecules under physiologically-relevant conditions.

When two proteins interact and bind, conformational changes in the proteins, and rearrangement of the solvent in the vicinity of the binding site, result in the absorption or generation of heat. Quantification of this reaction heat by ITC provides a complete thermodynamic description of the binding interaction, the stoichiometry of binding, and the association constant; in addition, if structural information is available, the contributions of specific amino acids mediating the binding event can be identified and their thermodynamic contributions quantified.

Continuous isothermal titration calorimetry (cITC) is ideal for studying rapid binding events typical of many biological recognition and binding reactions. The binding constant, stoichiometry and enthalpy of the reaction are accurately determined in significantly less time than that required using incremental isothermal titration calorimetry.

All enzymatic reactions generate heat, so all enzymatic reactions can in principle be directly studied by calorimetry. Calorimetric experiments do not require extensive protocol development, and measurements are direct, rapid, non-destructive and sensitive. In addition to kinetics data, ITC also generates thermodynamic information which can help correlate enzyme stability to reaction rates and substrate specificity.

Various techniques yield either structural or functional information about a protein, but DSC uniquely provides insights into both the three-dimensional arrangement and the functional properties of a protein’s structural components.

DSC is the most direct and sensitive approach for characterizing the thermodynamic parameters controlling noncovalent bond formation (and therefore stability) in proteins and other macromolecules. In an experiment requiring only a few micrograms of material, the protein is thermally unfolded, allowing the relationship between enthalpy and entropy of the denaturation process to be established in about one hour. Correlating thermodynamic properties to stability is necessary for the rational design of engineered proteins and protein therapeutics.

Although membrane proteins are very difficult to work with, ultra-sensitive calorimetry can over-come the limitations of many other physical characterization techniques to provide insights into the factors driving membrane protein/lipid assembly and controlling the stability of the conplexes.

采用行星式球磨机对胶原纤维进行分散处理，用激光粒度仪对纤维的粒径分布进行表征，并对不同分散处理样品的温度变化进行了分析。结果表明：通过筛分可提高原料的均一性，采用干磨法、一定级配的研磨介质、球料比为10:1、球磨机的转速为600r/min、，研磨时间60-120min，可得到均一性好、纤维较长的胶原纤维。

操作简单，重现性高，样品通量大，可同时平行处理48个样品；可有效用于动、植物体中DNA或RNA的快速提取。

2015 年3 月，北京易科泰生态技术公司为河南中医学院安装调试了一套FMS 便携式 动物呼吸代谢观测系统，用于模型动物代谢性疾病实验测量，该系统不仅可用于以家兔、 大小鼠、家蚕等为模型的肥胖及衰老的代谢机理研究，还可直接用于人体代谢性疾病的测 量分析，测量参数包括O2、CO2、耗氧量、呼吸强度（CO2 排放率）、呼吸商、温度等。

开放式呼吸计（open-flow respirometry）是测量生物能量代谢比较常用的方法，受到世界各国动物生理生态学、生物医学等领域科学家的长久青睐。