Villin 絨毛蛋白（鼠單克隆抗體）

廣州健侖生物科技有限公司

Villin是與刷狀緣微絨毛的微絲束有關(guān)的一種胃腸道相關(guān)性細(xì)胞骨架蛋白。正常組織中，Villin通常只表達(dá)于有刷狀緣的細(xì)胞上，如胃腸道上皮細(xì)胞、胰腺和膽管上皮細(xì)胞以及腎實(shí)質(zhì)的上皮細(xì)胞中（特別是近曲小管）。Villin作為腸道特異性參考依據(jù)，與CDX2聯(lián)合應(yīng)用，可用于腸上皮來(lái)源腫瘤與非腸上皮腫瘤的研究。Villin 也可作為胃腸道神經(jīng)內(nèi)分泌腫瘤研究的參考指標(biāo)。

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Villin 絨毛蛋白（鼠單克隆抗體）

【產(chǎn)品介紹】

細(xì)胞定位：細(xì)胞漿/細(xì)胞膜

克隆號(hào)：CWWB1

同型：IgG

適用組織：石蠟/冰凍

陽(yáng)性對(duì)照：結(jié)腸

抗原修復(fù)：熱修復(fù)（EDTA）

抗體孵育時(shí)間：30-60min

Villin

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【公司名稱】 廣州健侖生物科技有限公司
【市場(chǎng)部】     歐

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【騰訊  】 
【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101-103室

我們可以這樣描述一個(gè)細(xì)胞的命運(yùn)：多能狀態(tài)的細(xì)胞位于山頂，細(xì)胞中的基礎(chǔ)信號(hào)網(wǎng)絡(luò)就像重力一樣想把細(xì)胞拉下山，達(dá)到已分化狀態(tài)。因此細(xì)胞重編程中的挑戰(zhàn)是雙重的：不僅要把已分化的細(xì)胞抬上山頂，還要沉默那些吸引細(xì)胞分化的因子。
細(xì)胞重編程zui初是通過(guò)逆轉(zhuǎn)錄病毒將OSKM引入細(xì)胞，不過(guò)后來(lái)其他組合的轉(zhuǎn)錄因子也獲得了成功，這說(shuō)明細(xì)胞重編程涉及了復(fù)雜的動(dòng)態(tài)過(guò)程和狀態(tài)轉(zhuǎn)變。這種方法生成的iPSC存在較高的異質(zhì)性，會(huì)引發(fā)細(xì)胞突變，重編程效率也比較低。要將iPSC用于臨床，需要考慮避開(kāi)逆轉(zhuǎn)錄病毒的其他方法。 (延伸閱讀：Nature發(fā)表山中伸彌新成果，iPS校正環(huán)狀染色體)
正因如此，人們開(kāi)發(fā)了多種第二代iPS方法，其中已經(jīng)有一些表現(xiàn)出了更好的安全性。逆轉(zhuǎn)錄病毒的可重復(fù)性和簡(jiǎn)便性，使其依然活躍在體外研究中。然而在再生醫(yī)學(xué)領(lǐng)域，附加體型載體(episomal plasmid)更受青睞。其他方法還包括腺病毒、仙臺(tái)病毒、合成蛋白和RNA。不過(guò)，這些方法盡管更為安全，但技術(shù)要求比較高，對(duì)重編程效率也并無(wú)改善。zui近有研究顯示，僅通過(guò)小分子就可完成細(xì)胞重編程。這意味著，間接靶標(biāo)與多能性有關(guān)的分子通路，就足以重新決定細(xì)胞的命運(yùn)。
理解上述分子通路，可以幫助人們防止已進(jìn)入多能狀態(tài)的細(xì)胞回到已分化狀態(tài)。多能細(xì)胞和已分化細(xì)胞之間，存在DNA甲基化和組蛋白乙?；牟町悺Ａ硗?，靶標(biāo)表觀遺傳學(xué)機(jī)制的小分子，能夠提升重編程效率?？偟膩?lái)說(shuō)，在提升重編程效率的工作中需要特別注意表觀遺傳學(xué)因子的改變。

We can describe the fate of a cell in such a way that the pluripotent cells are located on the top of a mountain and the underlying signaling network in cells is like a gravity that wants to pull the cell down to reach a differentiated state. So the challenge in cell reprogramming is twofold: not only to lift the differentiated cells to the top of the hill, but also to silence those factors that attract cell differentiation.
Cell reprogramming originally introduced OSKM into cells via retroviruses, but other combinations of transcription factors were also successful later on, suggesting that cellular reprogramming involves complex dynamic processes and state transitions. The iPSC generated by this method has high heterogeneity, which leads to cell mutation and low reprogramming efficiency. To use iPSC clinically, there are other ways to avoid retroviruses. (Extended reading: Nature published Shinya Yamanaka new results, iPS correction of circular chromosomes)
Because of this, a number of second-generation iPS approaches have been developed, some of which have shown better security. The reproducibility and simplicity of retroviruses make them still active in in vitro studies. However, in the field of regenerative medicine, episomal plasmid is more favored. Other methods include adenovirus, Sendai virus, synthetic protein and RNA. However, these methods, while more secure, have higher technical requirements and no improvement in reprogramming efficiency. Recent studies have shown that cell reprogramming can be accomplished with only small molecules. This means that indirect target molecular pathways associated with pluripotency are sufficient to regain the cell's fate.
Understanding the molecular pathways described above can help people to prevent cells that have entered the pluripotent state from returning to their differentiated state. Differences between DNA methylation and histone acetylation exist between pluripotent cells and differentiated cells. In addition, small molecules of the target epigenetic mechanism enhance reprogramming efficiency. In general, special attention needs to be paid to changes in epigenetic factors in the promotion of reprogramming efficiency.

Villin is a gastrointestinal-associated cytoskeletal protein associated with microfilament-like microvasculars on the brush border. In normal tissues, Villin is usually expressed only on brush border cells, such as gastrointestinal epithelial cells, pancreatic and biliary epithelial cells, and renal parenchymal epithelium (especially proximal tubules). Villin as a gut-specific reference, combined with CDX2, can be used for intestinal epithelial tumors and non-intestinal epithelial tumor research. Villin can also be used as a reference indicator for gastrointestinal neuroendocrine tumors.