新孢子蟲IgG免疫熒光試劑盒（檢測馬）

Neospora caninum IgG IFA Kit

廣州健侖生物科技有限公司

主要用途：用于檢測馬血清中的新孢子蟲IgG抗體

產(chǎn)品規(guī)格：12 孔/張,10 張/盒

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新孢子蟲IgG免疫熒光試劑盒（檢測馬）

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【公司名稱】 廣州健侖生物科技有限公司
【】    楊永漢 
【】 
【騰訊 】 2042552662
【公司地址】 廣州清華科技園創(chuàng)新基地番禺石樓鎮(zhèn)創(chuàng)啟路63號二期2幢101-3室
【企業(yè)文化】

當(dāng)幾年前Jianpeng Ma遇見Onuchic時，他意識到一個機(jī)會，他說：“我告訴他，病毒系統(tǒng)有一個非常重要的特征，將對他的能量全景圖方法非常理想。”
長期以來，研究人員已經(jīng)通過X光散射技術(shù)觀察到了血球凝集素的初始和zui終結(jié)構(gòu)。但是，由于變化發(fā)生得如此之快，我們不可能捕獲到運(yùn)輸過程中的糖蛋白圖像。Ma說，阻止流感的關(guān)鍵可能是，攻擊這些中間結(jié)構(gòu)。
能量全景圖理論預(yù)測一個蛋白如何折疊，無論它發(fā)生的有多快。在血清凝集素的情況下，解折疊和重折疊發(fā)生在幾秒鐘的時間內(nèi)。在這個過程中，蛋白質(zhì)的一部分“破裂”并釋放融合肽。
本文共同作者、萊斯大學(xué)博士后研究人員Jeffrey Noel稱：“融合肽是分子zui重要的部分。血清凝集素附著到病毒膜上，當(dāng)這些肽被釋放時，它們就將自己嵌入到目標(biāo)細(xì)胞的細(xì)胞膜中，從而在兩者之間產(chǎn)生關(guān)聯(lián)。”
Ma說：“血球凝集素的目的是，在兩層膜之間戳一個洞。它們必須融合，這樣遺傳物質(zhì)才會被注入到人體細(xì)胞中。”
血球凝集素被宿主細(xì)胞表面的多糖受體所識別，當(dāng)細(xì)胞吞噬它時被吸收。zui初，該蛋白的一部分形成一個帽，可保護(hù)內(nèi)部的片段。
酸性條件可以使帽脫落，蛋白質(zhì)開始重構(gòu)自我。Ma說：“融合肽zui初隱匿在血球凝集素內(nèi)部，它的釋放是由巨大的構(gòu)象變化所觸發(fā)的。”
Noel稱：“當(dāng)帽未脫落時，整個蛋白質(zhì)是穩(wěn)定的。我們在模擬中看到的是，融合肽隱匿其中的疏水袋極不穩(wěn)定，一旦帽脫落了就想要破裂。”
通過利用來自X光散射技術(shù)的實(shí)驗結(jié)構(gòu)信息，粗略估計血球凝集素的整個能量全景圖，研究人員現(xiàn)在可以捕獲參與其重構(gòu)的步驟的粗略畫面，包括肽的釋放點(diǎn)。Ma說：“目前，我們*次繪制了整個過程，從狀態(tài)A到狀態(tài)B，這個過程的能量學(xué)。”
Ma表示，帽的頻繁突變有助于病毒避開抗體;這就是人每年都需要接種流感疫苗的原因。但是他懷疑，蛋白質(zhì)的內(nèi)部是高度保守的。他說：“我們正在靶定病毒不能改變的部分。因此，這為開發(fā)治療藥物提供了更多的希望。”這些藥物可能會帶來一種受益終生的通用流感疫苗。

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.