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Anti-Acetyl Cortactin (Lys309)
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  • 货号 ABT1378
  • 品牌 Merck millipore/默克密理博 ( 一级代理 )
  • CAS号 见包装
  • 规格/包装 100UL
  • 单位
  • 储存条件 见包装
  • 现货状态 询货

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Src substrate cortactin (UniProt: Q14247; also known as Amplaxin, Oncogene EMS1) is encoded by the CTTN (also known as EMS1) gene (Gene ID: 2017) in human. Cortactin is an F-actin binding protein that localizes to the cell cortex and contributes to the organization of the actin cytoskeleton and cell shape. It plays a role in the formation of lamellipodia and in cell migration and is considered to be important in the regulation of neuron morphology, axon growth and formation of neuronal growth cones. It is widely expressed in most adherent cells and is a prominent substrate of protein-tyrosine kinase Src in vivo and in vitro. Cortactin contains multiple amino-terminal tandem repeats of a unique 37-amino acid sequence, which associates with actin, and a Src homology 3 (SH3) domain at the carboxyl terminus. Cortactin is shown to shuttle between the cytoplasm and the nucleus under basal conditions and the acetylated form is mainly localized to the nucleus. It has two putative nuclear export sequences, NES1 and NES2, in the SH3 region. Acetylation of cortactin by histone acetyltransferase p300 reduces cell migration by inhibiting the binding of cortactin to Kelch-like ECH-associated protein 1 (Keap1). Cortactin is deacetylated by various proteins, including histone deacetylase 6 (HDAC6). Treatment with trichostatin and nicotinamide is reported to increases in the acetylation of cortactin in the presence of leptomycin B. In cells stimulated with growth factors, HDAC6 translocates together with cortactin to the cell periphery where HDAC6 deacetylates cortactin, leading to enhanced cortactin binding to F-actin and thereby stimulating cell migration. Cortactin can be phosphorylated on multiple tyrosine and serine/threonine residues in cells stimulated by numerous agents, including several growth factors. Tyrosine phosphorylation occurs primarily on Y421 and Y466 that are located within the proline-rich domain. Multiple serine residues are shown to be phosphorylated by PAK1, PAK3, MAP kinases, and protein kinase D. (Ref.: Ito, A., et al. (2015). Sci. Signal. 8(404):ra120; MacGrath, SM and Koleske, AJ (2012). J. Cell Sci. 125(7): 1621-1626),官网链接:https://www.sigmaaldrich.cn/product/mm/abt1378 默克 科研、开发、生产。 作为生命科学行业的全球领先供应商,我们致力于为科研、生物技术开发和生产,以及制药药物疗法开发和生产提供各类解决方案和服务。
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