驽巴贝西虫免疫荧光玻片

babesia caballi IFA Substrate slide

广州健仑生物科技有限公司

主要用途：用于检测马血清中的驽巴贝西虫IgG/IgM抗体

产品规格：12 孔/张,10 张/盒

主要产品包括：包柔氏螺旋体菌、布鲁氏菌、贝纳特氏立克次体、土伦杆菌、钩端螺旋体、新型立克次体、恙虫病、立克次体、果氏巴贝西虫、马焦虫、牛焦虫、利什曼虫、新包虫、弓形虫、猫流感病毒、猫冠状病毒、猫疱疹病毒、犬瘟病毒、犬细小病毒等病原微生物的 IFA、MIF、ELISA试剂。

驽巴贝西虫免疫荧光玻片

我司还提供其它进口或国产试剂盒：登革热、疟疾、西尼罗河、立克次体、无形体、蜱虫、恙虫、利什曼原虫、RK39、汉坦病毒、深林脑炎、流感、A链球菌、合胞病毒、腮病毒、乙脑、寨卡、黄热病、基孔肯雅热、克锥虫病、违禁品滥用、肺炎球菌、军团菌、化妆品检测、食品安全检测等试剂盒以及日本生研细菌分型诊断血清、德国SiFin诊断血清、丹麦SSI诊断血清等产品。

欢迎咨询

欢迎咨询2042552662

二维码扫一扫

【公司名称】 广州健仑生物科技有限公司
【】    杨永汉 
【】 
【腾讯 】 2042552662
【公司地址】 广州清华科技园创新基地番禺石楼镇创启路63号二期2幢101-3室
【企业文化】

研究结果已发表在JouRNAl of Controlled Release杂志上，目前研究仍然处于早期阶段，接下来的步骤是通过小鼠体内试验来测试其功效。
自从1969年已故诺贝尔奖得主Dorothy C. Hodgkin阐明胰岛素的存储结构以来，胰岛素已经改善了世界上5亿多人糖尿病患者的健康，并延长了他们的寿命。病患者的健康，并延长了他们的寿命。然而，这种关键激素如何与身体器官中的靶细胞结合?
现在，由Michael A. Weiss博士(克里夫兰凯斯西储大学医学院)和Michael C. Lawrence博士(沃尔特和伊莱扎研究所和澳大利亚墨尔本大学)共同的研究小组，解释了胰岛素分子如何利用一种“保护铰链”来参与胰岛素受体内的主要结合位点。相关文章发表于2014年8月4日的《PNAS》杂志上。
在本次调查研究中，Weiss、Lawrence及其同事们在胰岛素内发现了一个保护铰链，当它关闭时，可确保激素存储为一种安全的形式，直到它适时地打开——这种结构的转变可允许其对接到肌肉、肝脏、脂肪和其他组织靶细胞的表面。这种对接是代谢信号的*步，例如，这可使靶细胞能够吸收葡萄糖(糖构建模块)，从而避免血液中葡萄糖的积聚(高血糖)——糖尿病的基本特征。
研究人员通过观察晶体结构(在其构建模块中，一个单一的胰岛素分子结合到胰岛素受体片段上)中可视化的复杂结构特征，发现了保护性铰链。过去的研究，包括胰岛素结构Hodgkin在内，都集中在缺乏受体的6个胰岛素分子组(六聚体)。这种封闭形式的胰岛素，关系到它如何存储在体内或制备在药物制剂中。六聚体含有三对胰岛素分子(二聚体)。每个二聚体包含八个芳香环的交叉点，四个来自每个胰岛素分子。(芳香环是分子内的碳原子形成的闭环结构)。在激素开放和活跃形式的新图像中，这些芳香环驻留在细胞受体的口袋内。因此，胰岛素打开一个铰链，接触其功能表面。
Weiss称：“我们相信，胰岛素的关闭形式进化到允许其高效地生产并储存在胰腺内。然而，在这种状态下稳定的胰岛素变异形式，没有生物活性。”

The findings, published in the JouRNAl of Controlled Release, are still in their early stages and the next step is to test their efficacy in mice in vivo.
Since the late 1969 Nobel laureate Dorothy C. Hodgkin clarified the structure of insulin stores, insulin has improved the health and long-lived lives of more than 500 million people with diabetes in the world. The sick's health and prolong their life expectancy. However, how does this key hormone bind to target cells in body organs?
Now a team led by Dr. Michael A. Weiss (Case Western Reserve University of Cleveland) and Dr. Michael C. Lawrence (Walter & Eliza Institute and University of Melbourne, Australia) explained that insulin molecules How to use a "protective hinge" to participate in the major binding sites within the insulin receptor. The article was published in PNAS magazine on August 4, 2014.
In this study, Weiss, Lawrence, and colleagues found a protective hinge within insulin that when stored, ensures that hormones are stored in a safe form until it opens in a timely fashion - The transition allows it to dock to the surface of muscle, liver, fat and other tissue target cells. This docking is the first step in the metabolic signal, for example, which allows the target cells to absorb glucose (sugar building blocks) and thus avoids the accumulation of glucose in the blood (hyperglycemia), the essential feature of diabetes.
The researchers found protective hinges by looking at the complex structural features that are visualized in the crystal structure (in which a single insulin molecule binds to the insulin receptor fragment in its building block). Past research, including insulin structural pioneer Hodgkin, has focused on the six insulin molecule sets (hexamers) lacking the receptor. This closed form of insulin is related to how it is stored in the body or prepared in a pharmaceutical formulation. Hexamers contain three pairs of insulin molecules (dimers). Each dimer contains the intersection of eight aromatic rings and four from each insulin molecule. (Aromatic rings are closed-loop structures formed by intramolecular carbon atoms). In new images of hormone-opening and active forms, these aromatic rings reside in the pockets of cellular receptors. Therefore, insulin opens a hinge that contacts its functional surface.
"We believe the closed form of insulin evolved to allow it to be efficiently produced and stored within the pancreas," said Weiss, however, the steady variant forms of insulin in this state are not biologically active. "