鼠型斑疹伤寒立克次体IgG ELISA试剂盒

R. typhi IgG ELISA Kit 

广州健仑生物科技有限公司

主要用途：用于检测人血清中的鼠型斑疹伤寒立克次体IgG抗体

产品规格：96T/盒

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鼠型斑疹伤寒立克次体IgG ELISA试剂盒

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【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】

了解这种转换有可能促成一些新的策略，在心脏病发作后、衰老过程中或在诸如糖尿病及高血压等疾病中再生和生成新的心肌。
Hatzopoulos说：“如果我们可以了解损伤后发生的这种命运转换的分子调控机制，或许我们就可以采用某种化合物或药物来恢复再生，生成肌肉而不是瘢痕。我们认为这是一次机会来改善我们对心肌梗死后来到诊所的患者的治疗方式。
绿脓杆菌在免疫系统较弱的人当中，可以引起严重的皮肤和肺部炎症，特别是那些患有遗传性疾病囊胞性纤维症的人。当细菌进入人体细胞后，Gb3脂质结合LecA蛋白并使细胞膜弯曲。荷兰瓦格宁根大学的Christian Fleck教授在新研究中通过计算得出，这种结合足以将细菌包裹起来。
之前，研究人员只熟悉细菌侵染的方法，包括操控宿主细胞内的信号。这项信号可控制肌动蛋白纤维——细胞的肌肉：这些纤维可使来自内部的细胞被膜弯曲，并形成膜泡，细菌被吸收进其中。
为了证明没有肌动蛋白该过程一样能运行，德国佛莱堡大学BIOSS生物信号研究中心生物研究所II的Thorsten Eierhoff博士和Winfried R?mer教授带领的一个研究小组，观察了假单胞菌(Pseudomonas bacteria)对合成膜泡的影响。膜泡既不包含肌动蛋白，也不包含其他细胞组分，只有脂质Gb3。当离体膜停靠到表面上时，就在细菌周围折叠和关闭。然而，只有当细菌产生LecA蛋白时，才会发生这个包装过程。实验表明，假单胞菌使用这种脂质拉链，使其自身进入细胞，而无需操控肌动蛋白。
研究人员证明，LecA和Gb3对于细菌到人类肺细胞的入侵也非常重要：当这一对分子消失时，透过细胞的细菌数量减少了70%。这些研究结果使R?mer的研究小组能够发现一种潜在的药物，来对抗绿脓杆菌。美国华盛顿州立大学的科学家已经确定DNA修复的关键步骤，这有可能有助于开发遗传性疾病的靶向基因治疗法，如“月球来的孩子”和结肠癌的常见形式。
这种疾病是由错误的DNA修复系统引起的，该系统提高患癌症和其它条件的风险。相关文章发表于2014年8月18日的《PNAS》杂志上。
董事教授Michael Smerdon和博士后研究员Peng Mao发现，当DNA被破坏时，一个特定的蛋白质首先必须被“解开扣子”，以方便获取DNA的“修理队”。如果没有蛋白解开这一过程，进入受损位点的这一过程会被染色质的紧凑排列的基因和蛋白质阻拦。

Understanding this transition may lead to new strategies to regenerate and generate new myocardium during a heart attack, during aging or in diseases such as diabetes and hypertension.
Hatzopoulos said: "If we can understand the molecular mechanisms of this fate shift that occur after a lesion, perhaps we could use a compound or drug to regain regeneration and produce muscle instead of scar, and we think this is an opportunity to improve us Treatment of patients who come to the clinic after myocardial infarction.
Pseudomonas aeruginosa can cause severe skin and lung inflammation in people with weakened immune systems, especially those with hereditary cystic fibrosis. When bacteria enter human cells, Gb3 lipids bind LecA protein and bend the cell membrane. Professor Christian Fleck from Wageningen University in the Netherlands calculated in a new study that this combination is enough to encapsulate the bacteria.
Previously, researchers were only familiar with methods of bacterial infection, including manipulating signals in host cells. This signal controls the actin fibers - the cells' muscles: these fibers bend the envelope of cells from inside and form vesicles, into which bacteria are absorbed.
To demonstrate that this process works without actin, a team led by Dr. Thorsten Eierhoff and Prof. Winfried Römer at the Institute of Biology II at the BIOSS Biosignal Research Center, University of Freiburg, Freiburg, Germany, observed that Pseudomonas bacteria on synthetic vesicles. The vesicles neither contain actin nor other cellular components, only lipid Gb3. When the detachment membrane stops on the surface, it folds and closes around the bacteria. However, this process of packaging occurs only when the bacteria produce LecA protein. Experiments have shown that Pseudomonas uses this lipid zipper to allow itself to enter cells without manipulating actin.
Researchers have demonstrated that LecA and Gb3 are also important for the invasion of bacteria into human lung cells: When the pair of molecules disappears, the number of bacteria that pass through the cells is reduced by 70%. These findings led R? Mer's team to discover a potential drug against Pseudomonas aeruginosa. Scientists at Washington State University have identified key steps in DNA repair that could potentially help target gene therapy for the development of genetic diseases such as the common form of "child from the moon" and colon cancer.
The disease is caused by a faulty DNA repair system that increases the risk of cancer and other conditions. The article was published in PNAS magazine on August 18, 2014.
Director Professor Michael Smerdon and postdoctoral fellow Peng Mao have found that a particular protein must first be "unbuttoned" to facilitate access to DNA's "repair team" when the DNA is destroyed. Without this process of protein unwinding, the process of getting into a damaged site is blocked by tightly packed genes and proteins in the chromatin.