斑疹傷寒立克次體IgG ELISA檢測試劑盒

Typhus group IgG ELISA Kit

廣州健侖生物科技有限公司

主要用途：用于檢測人血清中的斑疹傷寒立克次體IgG抗體

產(chǎn)品規(guī)格：96T/盒

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斑疹傷寒立克次體IgG ELISA檢測試劑盒

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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(hào)二期2幢101-3室
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線蟲發(fā)育的某一時(shí)刻，稱為錨細(xì)胞的一種特殊細(xì)胞打破密集的片狀膜，將線蟲的子宮從外陰分離出來，開拓線蟲的抗原抗體道。錨細(xì)胞是看不見的，所以它們需要某種信號(hào)來告訴它們該打破哪里。2009年舍伍德等人曾發(fā)現(xiàn)，錨細(xì)胞需要通過細(xì)胞外的netrin信號(hào)來確定自己的侵襲方向。
發(fā)表于2014年8月25日的《Journal of Cell biology》雜志上的一項(xiàng)研究中，該研究團(tuán)隊(duì)發(fā)現(xiàn)，netrin受體在細(xì)胞膜上來回抗原抗體，“搜尋”指引方向的netrin信號(hào)。
研究人員對線蟲錨細(xì)胞的侵襲過程進(jìn)行了顯微延時(shí)成像。他們看到，當(dāng)netrin生產(chǎn)被阻斷時(shí)，錨細(xì)胞上的netrin受體會(huì)間歇性的在細(xì)胞膜各處成簇、分散和重組。這樣的受體簇就位于肌動(dòng)蛋白纖維旁邊，這種纖維可以幫助細(xì)胞改變形態(tài)，形成侵襲所需的突出結(jié)構(gòu)。
有了這些受體組成的探測系統(tǒng)，錨細(xì)胞就不需要轉(zhuǎn)來轉(zhuǎn)去地找信號(hào)了。一旦受體定位了netrin信號(hào)，它們就會(huì)在離信號(hào)zui近的細(xì)胞膜區(qū)域中穩(wěn)定下來。
數(shù)十年來，人們一直認(rèn)為細(xì)胞定向系統(tǒng)是被動(dòng)應(yīng)答信號(hào)的。這項(xiàng)研究改寫了這個(gè)老觀點(diǎn)，研究人員指出，錨細(xì)胞并不是被動(dòng)應(yīng)答netrin信號(hào)的，它們一直在主動(dòng)的尋找信號(hào)。
此前，人們曾在一些zui致命的癌癥中發(fā)現(xiàn)，netrin能促進(jìn)癌細(xì)胞侵襲。研究人員指出，可以通過netrin探測系統(tǒng)，阻止癌細(xì)胞進(jìn)入血液或淋巴系統(tǒng)，避免癌癥在機(jī)體中擴(kuò)散。研究人員稱，下一步將篩選藥物，嘗試阻斷癌細(xì)胞侵襲的探測系統(tǒng)。
在神經(jīng)系統(tǒng)布線過程中，netrin也起到了關(guān)鍵的作用，引導(dǎo)神經(jīng)細(xì)胞生長并形成連接。中樞神經(jīng)系統(tǒng)的再生能力很有限，不過netrin探測器也許可以幫助神經(jīng)細(xì)胞再生，幫助人們治療帕金森癥和漸凍人癥，促進(jìn)受損脊髓恢復(fù)康復(fù)。
就像一個(gè)吹煙圈形成的那樣，類似于一個(gè)微型的肌肉夾的“收縮環(huán)”是酵母細(xì)胞分裂為二。細(xì)胞的分裂使生命成為可能，但這個(gè)基本過程中的實(shí)際機(jī)制已被證明難以牽制。
耶魯大學(xué)和哥倫比亞大學(xué)的研究人員zui近在計(jì)算機(jī)上，通過積累足夠的信息來模擬收縮環(huán)的形成和收縮，揭示了這個(gè)奧秘。

At some point in the development of a nematode, a special cell called an anchor cell breaks a dense sheetlike membrane that separates the neuteri's uterus from the vulva and opens up the nematode's antigen-antibody tract. Anchor cells are invisible, so they need some sort of signal to l them where to break. In 2009, Sherwood et al. Found that the anchoring cells need to determine their direction of invasion by extracellular signals of netrin.
In a study published in the August 25, 2014 issue of the Journal of Cell biology, the team found that netrin receptors cross-hatch antigen antibodies on the cell membrane, "searching" for netrin signaling.
The researchers conducted microscopic time-lapse imaging of the invasion of nematode anchors. They observed that when netrin production was blocked, the netrin receptors on the anchors would cluster, disperse and recombine intermittently throughout the cell membrane. This receptor cluster is located next to the actin fibers, which help cells change their morphology and form prominent structures needed for invasion.
With these receptor-based detection systems, anchor cells do not need to turn around to find the signal. Once the receptor has localized the netrin signal, they stabilize in the cell membrane closest to the signal.
For decades, people have always believed that the cell-oriented system is a passive response signal. The study rephrasing this old view, the researchers pointed out that anchor cells are not passive response netrin signal, they have been actively looking for the signal.
Earlier, it was found in some of the most deadly cancer, netrin can promote cancer invasion. The researchers pointed out that netrin detection system, to prevent cancer cells into the blood or lymphatic system, to prevent the spread of cancer in the body. The researchers said the next step would be screening drugs to try to block detection of cancer cells.
Netrin also plays a key role in the wiring of the nervous system, guiding nerve cells to grow and form connections. The regenerative capacity of the central nervous system is limited, but the netrin detector may help regenerate nerve cells, help people treat Parkinson's disease and freeze-thaw disease, and promote the recovery of damaged spinal cord.
Like a puff of smoke, a "contraction ring" resembling a miniature muscle clip splits yeast cells into two. Cell division makes life possible, but the actual mechanisms in this basic process have proven difficult to pin down.
Researchers at Yale and Columbia recently revealed the mystery on a computer by accumulating enough information to simulate the formation and contraction of a constriction ring.