EIAab
首页  >  重组蛋白  >  Human VIL1 Recombinant Protein
VIL1 (基因名), Villin-1 (蛋白名), vili_human.
产品名称:

Human VIL1/ Villin-1 Recombinant Protein
Villin-1

货号:

R0193h

商标:
EIAab®
监管等级:
别名:

VIL

序列号:
P09327
来源:
E.coli
种属:
Human
标签:
His
纯度:
>90% by SDS-PAGE
浓度:
Reconstitution Dependent
形态:
Liquid
内毒素水平:
Please contact protein@eiaab.com The technician for more information.
应用:
存储缓冲液:
50mM NaH2PO4, 500mM NaCl Buffer with 500mM Imidazole, 10%glycerol(PH8.0)
存储:
Store at -20°C. (Avoid repeated freezing and thawing.)
研究领域:
-
Human VIL1 Protein
规格 & 价格: cart
×
Human VIL1 Protein
邮箱 *
消息 *
Please 登录.
产品说明书
说明书: 下载说明书
MSDS: MSDS
在线询价


R&D 技术数据
更多信息,请参阅手册,或联系我们的技术支持: tech@eiaab.com.
基因位点
Cytogenetic band: 2q35 by HGNC 2q35 by Entrez Gene 2q35 by Ensembl
VIL1 Gene in genomic location: bands according to Ensembl, locations according to GeneLoc (and/or Entrez Gene and/or Ensembl if different)
基因位点
通用注释


亚单元:
Monomer. Homodimer; homodimerization is necessary for actin-bundling. Associates with F-actin; phosphorylation at tyrosine residues decreases the association with F-actin. Interacts (phosphorylated at C-terminus tyrosine phosphorylation sites) with PLCG1 (via the SH2 domains). Interacts (phosphorylated form) with PLCG1; the interaction is enhanced by hepatocyte growth factor (HGF).


功能:
Epithelial cell-specific Ca(2+)-regulated actin-modifying protein that modulates the reorganization of microvillar actin filaments. Plays a role in the actin nucleation, actin filament bundle assembly, actin filament capping and severing. Binds phosphatidylinositol 4,5-bisphosphate (PIP2) and lysophosphatidic acid (LPA); binds LPA with higher affinity than PIP2. Binding to LPA increases its phosphorylation by SRC and inhibits all actin-modifying activities. Binding to PIP2 inhibits actin-capping and -severing activities but enhances actin-bundling activity. Regulates the intestinal epithelial cell morphology, cell invasion, cell migration and apoptosis. Protects against apoptosis induced by dextran sodium sulfate (DSS) in the gastrointestinal epithelium. Appears to regulate cell death by maintaining mitochondrial integrity. Enhances hepatocyte growth factor (HGF)-induced epithelial cell motility, chemotaxis and wound repair. Upon S.flexneri cell infection, its actin-severing activity enhances actin-based motility of the bacteria and plays a role during the dissemination.


亚细胞位置:
Cytoplasm Cytoskeleton Cell projection Lamellipodium Cell projection Ruffle Cell projection Microvillus Cell projection Filopodium tip Cell projection Filopodium Relocalized in the tip of cellular protrusions and filipodial extensions upon infection with S.flexneri in primary intestinal epithelial cells (IEC) and in the tail-like structures forming the actin comets of S.flexneri. Redistributed to the leading edge of hepatocyte growth factor (HGF)-induced lamellipodia (By similarity). Rapidly redistributed to ruffles and lamellipodia structures in response to autotaxin, lysophosphatidic acid (LPA) and epidermal growth factor (EGF) treatment.


该产品尚未在任何出版物中被引用。

[1].
"Sequence of human villin: a large duplicated domain homologous with other actin-severing proteins and a unique small carboxy-terminal domain related to villin specificity."

[2].
"Differential effects of lysophosphatidic acid and phosphatidylinositol 4,5-bisphosphate on actin dynamics by direct association with the actin-binding protein villin."

[3].
"Autotaxin and lysophosphatidic acid stimulate intestinal cell motility by redistribution of the actin modifying protein villin to the developing lamellipodia."

[4].
"Villin severing activity enhances actin-based motility in vivo."

[5].
"Obligatory role for phospholipase C-gamma(1) in villin-induced epithelial cell migration."

[6].
"Dimerization and actin-bundling properties of villin and its role in the assembly of epithelial cell brush borders."

[7].
"Interaction of phospholipase C-gamma1 with villin regulates epithelial cell migration."

[8].
"Association of villin with phosphatidylinositol 4,5-bisphosphate regulates the actin cytoskeleton."

[9].
"Solution structures of the C-terminal headpiece subdomains of human villin and advillin, evaluation of headpiece F-actin-binding requirements."

[10].
"Functional dissection and molecular characterization of calcium-sensitive actin-capping and actin-depolymerizing sites in villin."
关闭
Sample Data
关闭
Sample Data
关闭
Sample Data
用户中心 close
购物车 close
我的收藏 close
我的足迹 close
清除
产品对比 close
用户中心
购物车
我的收藏
我的足迹
产品对比
回到顶部
通知
new 咨询
规格 数量 单价 (¥) 小计 1 (¥)
小计 2:
triangle
规格 数量 单价 (¥)
你想做我们的代理并得到更低的折扣吗?
请联系我们:
电话:027-59234612(+86)
传真:027-59234610(+86)
邮箱:sales@eiaab.com