新孢子虫IgG免疫荧光试剂盒（检测马）

Neospora caninum IgG IFA Kit

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新孢子虫IgG抗体

产品规格：12 孔/张,10 张/盒

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新孢子虫IgG免疫荧光试剂盒（检测马）

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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】

当几年前Jianpeng Ma遇见Onuchic时，他意识到一个机会，他说：“我告诉他，病毒系统有一个非常重要的特征，将对他的能量全景图方法非常理想。”
长期以来，研究人员已经通过X光散射技术观察到了血球凝集素的初始和zui终结构。但是，由于变化发生得如此之快，我们不可能捕获到运输过程中的糖蛋白图像。Ma说，阻止流感的关键可能是，攻击这些中间结构。
能量全景图理论预测一个蛋白如何折叠，无论它发生的有多快。在血清凝集素的情况下，解折叠和重折叠发生在几秒钟的时间内。在这个过程中，蛋白质的一部分“破裂”并释放融合肽。
本文共同作者、莱斯大学博士后研究人员Jeffrey Noel称：“融合肽是分子zui重要的部分。血清凝集素附着到病毒膜上，当这些肽被释放时，它们就将自己嵌入到目标细胞的细胞膜中，从而在两者之间产生关联。”
Ma说：“血球凝集素的目的是，在两层膜之间戳一个洞。它们必须融合，这样遗传物质才会被注入到人体细胞中。”
血球凝集素被宿主细胞表面的多糖受体所识别，当细胞吞噬它时被吸收。zui初，该蛋白的一部分形成一个帽，可保护内部的片段。
酸性条件可以使帽脱落，蛋白质开始重构自我。Ma说：“融合肽zui初隐匿在血球凝集素内部，它的释放是由巨大的构象变化所触发的。”
Noel称：“当帽未脱落时，整个蛋白质是稳定的。我们在模拟中看到的是，融合肽隐匿其中的疏水袋极不稳定，一旦帽脱落了就想要破裂。”
通过利用来自X光散射技术的实验结构信息，粗略估计血球凝集素的整个能量全景图，研究人员现在可以捕获参与其重构的步骤的粗略画面，包括肽的释放点。Ma说：“目前，我们*次绘制了整个过程，从状态A到状态B，这个过程的能量学。”
Ma表示，帽的频繁突变有助于病毒避开抗体;这就是人每年都需要接种流感疫苗的原因。但是他怀疑，蛋白质的内部是高度保守的。他说：“我们正在靶定病毒不能改变的部分。因此，这为开发治疗药物提供了更多的希望。”这些药物可能会带来一种受益终生的通用流感疫苗。

When Jianpeng Ma met Onuchic a few years ago, he realized there was an opportunity. He said: "I told him that the virus system has a very important feature that would be ideal for his energy panorama."
For a long time, researchers have observed the initial and final structure of hemagglutinin by X-ray scattering. However, because changes are happening so fast, we can not capture images of glycoproteins during transport. Ma said the key to stopping the flu could be to attack these intermediaries.
Energy panorama theory predicts how a protein folds, no matter how fast it occurs. In the case of serum lectin, unfolding and refolding occur in seconds. During this process, a portion of the protein "cracks" and releases the fusion peptide.
Co-author Jeffrey Noel, a postdoctoral researcher at Rice University, said: "Fusion peptides are the most important part of the molecule. Serum lectins attach to viral membranes and when these peptides are released they embed themselves into the cell membrane of the target cell In the relationship between the two.
Ma said: "The purpose of hemagglutinin is to poke a hole between two membranes, and they must be fused so that genetic material can be injected into human cells."
Hemagglutinin is recognized by polysaccharide receptors on the surface of host cells and is absorbed by cells as they are phagocytosed. Initially, a portion of the protein forms a cap that protects the internal fragments.
Acidic conditions can break the cap off and the protein begins to reconstitute itself. Ma said: "The fusion peptide was initially hidden inside the hemagglutinin and its release was triggered by a huge conformational change."
"The entire protein is stable when the cap is not shedding," says Noel. "What we see in the simulation is that the hydrophobic bag in which the fusion peptide is secreted is extremely unstable and wants to rupture once the cap has detached."
By using the experimental structure information from X-ray scattering techniques to roughly estimate the entire energy panorama of hemagglutinin, researchers can now capture a rough picture of the steps involved in their reconstruction, including the point of release of the peptide. Ma said: "At present, for the first time, we have drawn the entire process from state A to state B, the energetics of this process."
Ma said frequent changes in the cap help the virus avoid antibodies; that's why people need flu vaccinations every year. But he doubts that the interior of the protein is highly conserved. He said: "We are targeting parts of the virus that can not be changed, so this offers more hope for the development of therapeutics." These drugs may bring a universal flu vaccine that benefits lifelong.