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廣州健侖生物科技有限公司

主要用途：用于檢測牛血清中的牛雙芽巴貝西蟲IgG/IgM抗體

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牛雙芽巴貝西蟲免疫熒光玻片

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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
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自噬作用主要發(fā)揮為細胞清除損傷和毒性蛋白的作用。那些并沒有罹患Ⅱ型糖尿病的機體，自噬作用可以預防IAPP毒性蛋白的累積;而罹患Ⅱ型糖尿病的病患，這一過程沒有正常工作，反而發(fā)揮破壞β細胞的作用。而β細胞分泌的胰島素在維持血糖健康方面起重要作用。此前已有少量研究揭示過自噬作用對于β細胞功能的發(fā)揮和存活相當重要，但是并沒有揭示這一過程對于導致Ⅱ型糖尿病的淀粉樣蛋白的調(diào)節(jié)作用。
此次研究利用三個實驗模型，分別是胰腺β細胞，表達人類IAPP的小鼠中分離出的胰島細胞，人類胰島。研究發(fā)現(xiàn)，自噬作用從胰腺β細胞清除IAPP過程中發(fā)揮重要作用。為了證實這一發(fā)現(xiàn)，研究人員構(gòu)建了一個新型小鼠模型，該小鼠β細胞的自噬作用缺失，且還能表達人類胰島淀粉樣多肽。研究人員發(fā)現(xiàn)該小鼠毒性蛋白IAPP水平升高，這導致了β細胞的死亡。結(jié)果，這些小鼠進一步發(fā)展成糖尿病。除以上研究發(fā)現(xiàn)，此次研究再次證實Ⅱ型糖尿病和阿爾茨海默病，以及其他因毒性淀粉樣蛋白的累積為標志的神經(jīng)退行性疾病之間存在類似性。自噬作用同樣在這些疾病過程中發(fā)揮重要作用。
此次研究旨在研究β細胞受損的細胞機制，以便確定β細胞保護的抗原抗體靶點。此次發(fā)現(xiàn)有助于開發(fā)新一代治療Ⅱ型糖尿病方法。
近日，有名雜志《自然—結(jié)構(gòu)和分子生物學》(Nature Structural & molecular biology) 在線刊登了中國科學院生物物理研究所秦燕研究員的科研成果“A conserved proline switch on the ribosome facilitates the recruitment and binding of trGTPases，”，文章中，研究者報道了核糖體招募翻譯因子的重要分子機理。
核糖體是蛋白質(zhì)翻譯工廠，信使RNA上攜帶的遺傳信息在這里被翻譯成蛋白質(zhì)。完成蛋白質(zhì)的生物合成過程需要核糖體和眾多翻譯因子協(xié)調(diào)完成，核糖體招募翻譯因子的過程錯綜復雜，一直以來沒有定論。

The main role of autophagy for cell damage and toxic protein damage role. Autophagy can prevent the accumulation of IAPP toxic proteins in those with no type 2 diabetes. In patients with type 2 diabetes, this process does not work properly and instead destroys beta cells. The insulin secreted by beta cells plays an important role in maintaining glycemic health. A few studies have previously revealed that autophagy is important for the function and survival of beta cells but does not reveal the regulatory effect of this process on amyloidosis leading to type 2 diabetes.
The study utilized three experimental models, pancreatic islet cells, islet cells isolated from mice expressing human IAPP, and human islets. The study found that autophagy plays an important role in the clearance of IAPP from pancreatic β cells. To confirm this finding, the researchers constructed a novel mouse model that lacked autophagy in the mouse β-cell and also expressed human amylin. The researchers found that the mice increased the level of IAPP, a toxic protein, which led to the death of beta cells. As a result, these mice further developed into diabetes. In addition to the above findings, this study again confirms the similarities between type 2 diabetes and Alzheimer's disease, as well as other neurodegenerative diseases that are marked by the accumulation of toxic amyloid. Autophagy also plays an important role in these diseases.
The aim of this study was to investigate the cellular mechanisms of beta-cell damage in order to determine the target of the beta-cell-protected antigen-antibody. The discovery helps to develop a new generation of treatments for type 2 diabetes.
Recently, the world-renowned journal Nature Structural & Molecular Biology published the latest research results of Qin Yan, a researcher at the Institute of Biophysics, Chinese Academy of Sciences, "A conserved proline switch on the ribosome facilitates the recruitment and binding of trGTPases, "the article reports on the important molecular mechanisms by which ribosomes recruit translation factors.
Ribosomes are protein translation factories where the genetic information carried on the messenger RNA is translated into protein. Completion of the protein biosynthesis process requires the coordination of ribosomes and a large number of translation factors, the process of ribosome recruitment of translation factors is complex and has not been conclusive.