美國Seracare大腸桿菌O111:H8物種陽性對照

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廣州健侖長期供應(yīng)各種生物原料，主要代理品牌：美國Seracare、西班牙Certest、美國Fuller等等。

主要產(chǎn)品包括各種標(biāo)準(zhǔn)品、陽性對照品、陽性質(zhì)控品、單克隆抗原抗體。

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美國Seracare大腸桿菌O111:H8物種陽性對照

我司還提供其它進(jìn)口或國產(chǎn)試劑盒：登革熱、瘧疾、流感、A鏈球菌、合胞病毒、腮病毒、乙腦、寨卡、黃熱病、基孔肯雅熱、克錐蟲病、違禁品濫用、肺炎球菌、軍團(tuán)菌、化妝品檢測、食品安全檢測等試劑盒以及日本生研細(xì)菌分型診斷血清、德國SiFin診斷血清、丹麥SSI診斷血清等產(chǎn)品。

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當(dāng)來自英國牛津大學(xué)的科研人員減少了布氏錐蟲錐鞭毛體的一種稱為ClpGM6的蛋白質(zhì)表達(dá)的時候，這個細(xì)胞切換到了一種類似于短膜蟲期的形態(tài)。動基體接近核或者在其之前，而且鞭毛的一長部分伸出了細(xì)胞。這些寄生蟲與短膜蟲期不一樣——它們?nèi)狈σ娪谶@個生命階段的一種*的表面蛋白——但是它們有能力存活并且繁殖超過40代。
ClpGM6位于鞭毛的附著區(qū)，而且很可能有助于把鞭毛與細(xì)胞體連接。失去ClpGM6導(dǎo)致鞭毛的幫助確定細(xì)胞尺寸和形狀的附著區(qū)縮短。這項研究提出，在生命周期中以及在寄生蟲進(jìn)化中出現(xiàn)的顯著形態(tài)變化可能是由于幾個關(guān)鍵蛋白質(zhì)層次上的調(diào)整造成的，而不是源于寄生蟲蛋白質(zhì)或DNA內(nèi)容的大量變化。
蛋白質(zhì)是來自DNA的分子馬達(dá)，執(zhí)行對生命*的任務(wù)，它們是萊斯大學(xué)理論生物物理學(xué)研究中心(CTBP)的José Onuchic及其同事研究的主要焦點。研究人員使用他們的能量全景圖理論(energy landscape theory)，來確定一段未折疊的氨基酸鏈zui終成為一種功能蛋白所采用的途徑。這涉及到，計算鏈中每一個氨基酸的結(jié)合模式以及折疊進(jìn)行中周圍環(huán)境的影響。
當(dāng)幾年前Jianpeng Ma遇見Onuchic時，他意識到一個機會，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。

美國Seracare

我司還提供其它進(jìn)口或國產(chǎn)試劑盒：登革熱、瘧疾、流感、A鏈球菌、合胞病毒、腮病毒、乙腦、寨卡、黃熱病、基孔肯雅熱、克錐蟲病、違禁品濫用、肺炎球菌、軍團(tuán)菌、食品安全、化妝品檢測、藥物濫用檢測等試劑盒以及日本生研細(xì)菌分型診斷血清、德國SiFin診斷血清、丹麥SSI診斷血清等產(chǎn)品。

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【公司名稱】 廣州健侖生物科技有限公司
【市場部】    楊永漢

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【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101-103室

When researchers from the University of Oxford in the United Kingdom reduced the protein expression of ClpGM6, a member of the Trypanosoma brucei conidia, the cell switched to a morphology similar to the meiosis stage. The moving body approaches the nucleus or before it, and a long portion of the flagellum protrudes out of the cell. These parasites are not the same as the meiosis - they lack a unique surface protein found at this stage of their life - but they are capable of surviving and breeding for more than 40 generations.
ClpGM6 is located in the attachment region of the flagella and probably helps to connect the flagella to the cell body. Lack of ClpGM6 Leads to Flagella Help to Determine Cell Size and Shape Attachment Area Shortens. This study suggests that significant morphological changes that occur during life cycles and during parasite evolution may be due to adjustments at several key protein levels rather than a substantial change in parasite proteins or DNA content.
Proteins, a molecular motor derived from DNA, perform mission-critical tasks that are the main focus of José Onuchic and his colleagues at the Center for Theoretical Biophysics (CTBP) at Rice University. Researchers use their energy landscape theory to determine the pathway by which an unfolded amino acid chain eventually becomes a functional protein. This involves calculating the mode of binding for each amino acid in the chain and the impact of the environment in which the fold is in progress.
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.