Biacore 3000 Biosensor

申请人提供的描述）：我们要求资金购买BIAcore 3000，用于马里兰州大学（UM）学校的生物传感器核心设施 医学（SoM）BIAcore使用表面等离子体共振（SPR）检测 分子或其它材料与衍生的金表面的结合。许多 这些特性使3000成为核心设施的理想选择。(i)SPR检测a 各种生物材料，无论是蛋白质，核酸，脂质， 碳水化合物、病毒或细胞。(ii)各种稳定的表面化学性质 可以从BIAcore获得，允许分析许多不同种类的 配体。(iii)BIAcore有4个独立监控的通道， 同时比较对照样品和实验样品。（四） 信噪比高，反应条件精确控制 允许可靠地监测结合。(v)BIAcore可以精确测量 小分子的结合。(vi)液压系统最大限度地减少了 使用的样品，并促进结合样品的回收。(vii)该单位是 易于自动化，允许长时间无人值守使用。 BIAcore 3000将主要由5名研究者使用，其中4名在UM SoM， 一个在UM生物技术高级研究中心（CARB）。R.布洛赫， 主要研究者，将利用BIAcore技术研究相互作用 膜蛋白和细胞骨架蛋白之间的联系。F. 马戈利斯将研究嗅觉标记蛋白与 使用相展示文库鉴定的蛋白质。E.温曼将研究 上皮细胞Na，H-交换调节因子的寡聚化及其对细胞增殖的影响 与其他调节蛋白、细胞骨架蛋白和转运蛋白结合。J. Fondell 将定量分析辅激活蛋白与 甲状腺激素依赖性核受体。R. Mariuzza（CARB），将研究 抗原与抗体和T细胞受体的结合。Mariuzza博士 具有较早BIAcore模型的丰富经验;所有其他四个主要用户 在蛋白质-蛋白质结合的研究中使用了SPR技术， 公布了他们的结果。 BIAcore 3000将置于UM SoM的生物传感器核心设施中， 将由经验丰富的蛋白质化学家J. Ursitti博士指导， 已经接受过BIAcore BIA基础培训的分子生物学家。 该机构将配备一名经过BIAcore培训的全职技术人员。一个 内部咨询委员会由Bloch、Fondell和Mariuzza博士组成 将监督该设施，以确保其顺利运作， 所有主要用户。新装修的办公空间已分配给 设施由生理学系，并提供资金，以确保顺利启动 以及持续的支持已承诺由SoM和该计划， 细胞与分子生物学我们预计，该设施将提供其 主要用户，以及最终在SoM和巴尔的摩地区的其他用户， 最先进的生物传感器技术

DESCRIPTION provided by the applicant): We request funds to purchase a BIAcore 3000 for use in a Biosensor Core Facility at the Univ. of Maryland (UM) School of Medicine (SoM). BIAcore uses surface plasmon resonance (SPR) to detect binding of molecules or other materials to a derivatized gold surface. Many features make the 3000 ideal for a core facility. (i) SPR detects binding of a variety of biological materials, be they protein, nucleic acids, lipids, carbohydrates, viruses or cells. (ii) A variety of stable surface chemistries are available from BIAcore, allowing analysis of many different kinds of ligands. (iii) The BIAcore has 4 independently monitored channels, facilitating simultaneous comparisons of control and experimental samples. (iv) Signal-to-noise ratios are high, and precise control of reaction conditions permits reliable monitoring of binding. (v) The BIAcore can accurately measure binding of small molecules. (vi) The hydraulic system minimizes the volume of samples used and facilitates the recovery of bound sample. (vii) The unit is readily automated, permitting unattended use for extended periods of time. The BIAcore 3000 will be used primarily by 5 investigators, 4 at the UM SoM and one at the UM Center for Advanced Research in Biotechnology (CARB). R. Bloch, principal investigator, will utilize BIAcore technology to study interactions between membrane proteins and cytoskeletal proteins of excitable cells. F. Margolis will examine the interactions of olfactory marker protein with proteins identified using a phase display library. E. Weinman will study oligomerization of the epithelial Na,H-exchanger regulatory factor and its binding to other regulatory, cytoskeletal, and transport proteins. J. Fondell will analyze quantitatively the interactions of coactivator proteins with the thyroid hormone-dependent nuclear receptor. R. Mariuzza (CARB), will study binding of antigen to antibody and to the T-cell receptor. Dr. Mariuzza hs extensive experience with an earlier BIAcore model; all four other major users have used SPR technology in studies of protein-protein binding, and two have published their results. The BIAcore 3000 will be housed in a Biosensor Core Facility at the UM SoM and will be directed by Dr. J. Ursitti, an experienced protein chemist and molecular biologist who has already received BIA basics training from BIAcore. The facility will be staffed by a full-time, BIAcore-trained technician. An Internal Advisory committee consisting of Drs. Bloch, Fondell, and Mariuzza will oversee the facility to ensure its smooth functioning, equitable access for all the major users. Newly renovated space has been allocated for the facility by the Department of Physiology, and funds to ensure a smooth start-up as well as ongoing support have been committed by the SoM and the program in Cell and Molecular Biology. We anticipate that this facility will provide its primary users, and ultimately others at the SoM and in the Baltimore area, with state-of-the-art biosensor technology.