绒毛蛋白(鼠单克隆抗体)

Villin绒毛蛋白(鼠单克隆抗体)

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2017-12-27 09:41:03
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广州欧边生物制品有限公司

广州欧边生物制品有限公司

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Villin 绒毛蛋白(鼠单克隆抗体) 免疫组化 一抗二抗 我司为大家提供各种生物原料免疫组化产品,欢迎大家随时咨询。

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Villin 绒毛蛋白(鼠单克隆抗体)

广州健仑生物科技有限公司

Villin是与刷状缘微绒毛的微丝束有关的一种胃肠道相关性细胞骨架蛋白。正常组织中,Villin通常只表达于有刷状缘的细胞上,如胃肠道上皮细胞、胰腺和胆管上皮细胞以及肾实质的上皮细胞中(特别是近曲小管)。Villin作为肠道特异性参考依据,与CDX2联合应用,可用于肠上皮来源肿瘤与非肠上皮肿瘤的研究。Villin 也可作为胃肠道神经内分泌肿瘤研究的参考指标。

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Villin 绒毛蛋白(鼠单克隆抗体)

【产品介绍】

细胞定位:细胞浆/细胞膜

克隆号:CWWB1

同型:IgG

适用组织:石蜡/冰冻

阳性对照:结肠

抗原修复:热修复(EDTA)

抗体孵育时间:30-60min

产品编号抗体名称克隆型别
OB234T-bet(T盒子转录因子)MRQ-46
OB235TCL1试剂(T细胞淋巴瘤1)MRQ-7
OB236TdT(末端脱氧核苷酸转移酶)polyclonal
OB237TFE3试剂(转录因子E3)MRQ-37
OB238Thyroglobulin(甲状腺球蛋白)DAK-Tg6
OB239Thyroglobulin(甲状腺球蛋白)2H11+6E1 
OB240TIA-1(T细胞胞浆内抗原)2G9A10F5
OB241Topo Ⅱ α(拓扑异构酶Ⅱα)SD50
OB242TPO(甲状腺过氧化物酶)AC25
OB243TS(胸苷酸合成酶)TS106
OB244TSH 甲状腺刺激激素polyclonal
OB245TTF-1(甲状腺转录因子1)8G7G3/1
OB246TTF-1(甲状腺转录因子1)SPT24
OB247Tyrosinase(酪氨酸酶)T311
OB248Uroplakin III试剂(尿溶蛋白III)SP73
OB249VEGF(血管内皮生长因子)VG1
OB250VEGF(血管内皮生长因子)polyclonal
OB251Villin(绒毛蛋白)CWWB1
OB252Vimentin(波形蛋白)V9
OB253Vimentin(波形蛋白)SP20
OB254WT1(肾母细胞瘤) EP122
OB255ZAP-70试剂(Zeta链相关蛋白激酶70)2F3.2

Villin

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【公司名称】 广州健仑生物科技有限公司
【市场部】     欧

【】 
【腾讯  】 
【公司地址】 广州清华科技园创新基地番禺石楼镇创启路63号二期2幢101-103室

我们可以这样描述一个细胞的命运:多能状态的细胞位于山顶,细胞中的基础信号网络就像重力一样想把细胞拉下山,达到已分化状态。因此细胞重编程中的挑战是双重的:不仅要把已分化的细胞抬上山顶,还要沉默那些吸引细胞分化的因子。
细胞重编程zui初是通过逆转录病毒将OSKM引入细胞,不过后来其他组合的转录因子也获得了成功,这说明细胞重编程涉及了复杂的动态过程和状态转变。这种方法生成的iPSC存在较高的异质性,会引发细胞突变,重编程效率也比较低。要将iPSC用于临床,需要考虑避开逆转录病毒的其他方法。 (延伸阅读:Nature发表山中伸弥新成果,iPS校正环状染色体)
正因如此,人们开发了多种第二代iPS方法,其中已经有一些表现出了更好的安全性。逆转录病毒的可重复性和简便性,使其依然活跃在体外研究中。然而在再生医学领域,附加体型载体(episomal plasmid)更受青睐。其他方法还包括腺病毒、仙台病毒、合成蛋白和RNA。不过,这些方法尽管更为安全,但技术要求比较高,对重编程效率也并无改善。zui近有研究显示,仅通过小分子就可完成细胞重编程。这意味着,间接靶标与多能性有关的分子通路,就足以重新决定细胞的命运。
理解上述分子通路,可以帮助人们防止已进入多能状态的细胞回到已分化状态。多能细胞和已分化细胞之间,存在DNA甲基化和组蛋白乙酰化的差异。另外,靶标表观遗传学机制的小分子,能够提升重编程效率。总的来说,在提升重编程效率的工作中需要特别注意表观遗传学因子的改变。

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.

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