本公司经销phospho-Afadin（Ser1721），磷酸化丝状肌动蛋白结合蛋白抗体，克隆类型为polyclonal，宿主来源是Rabbit，phospho-Afadin（Ser1721）磷酸化丝状肌动蛋白结合蛋白抗体可应用于WB、elisa、IP、IF、IHC等实验，欢迎垂询订购！

货号：BY-3072R
英文名称：Anti-phospho-Afadin（Ser1721）
中文名称：磷酸化丝状肌动蛋白结合蛋白抗体
其他名称：p-Afadin（Ser1718）; MLLT4; Protein AF6; AF6; Afadin; AFAD_HUMAN; ALL1-fused gene from chromosome 6 protein; Protein AF-6.
抗体来源：Rabbit
克隆类型：polyclonal
蛋白分子量：predicted molecular weight: 201kDa
纯化方法：affinity purified by Protein A
交叉反应：hu, mo, rat
产品介绍：Afadin is a cell-cell adherens junction F-actin binding multidomain protein. Two splice variants of afadin have been described: l-afadin, which is ubiquitously expressed, ａnd the smaller s-afadin, which is abundantly expressed in neural tissue. l-Afadin contains one PDZ domain near its middle followed by three proline-rich ａnd one F-actin-binding region at the carboxyl-terminal. l/s-Afadin is localized to cell-cell junctions ａnd binds several cytoplasmic proteins such as the small GTPase Ras, the tight junction protein ZO-1, ａnd the vinculin binding protein ponsin/SH3P12. Function : Belongs to an adhesion system, probably together with the E-cadherin-catenin system, which plays a role in the organization of homotypic, interneuronal ａnd heterotypic cell-cell adherens junctions （AJs）. Nectin- ａnd actin-filament-binding protein that connects nectin to the actin cytoskeleton.Subunit : Homodimer. Interacts with F-actin, nectin ａnd PVRL3/nectin-3. Essential for the association of nectin ａnd E-cadherin. Isoform 1/s-afadin does not interact with F-actin. Interacts with ZO-1 ａnd occludin, but probably in an indirect manner. Interacts with RIT1 ａnd RIT2 （By similarity）. Interacts with NRXN1 ａnd BCR.Subcellular Location : Cell junction, adherens junction. Note=Not found at cell-matrix AJs.DISEASE : Note=A chromosomal aberration involving MLLT4 is associated with acute leukemias. Translocation t（6;11）（q27;q23） with MLL/HRX. The result is a rogue activator protein.Similarity : Contains 1 dilute domain.Contains 1 FHA domain. Contains 1 PDZ （DHR） domain. Contains 2 Ras-associating domains