Anti-VIL1 Antibody


Reactivity: Human
Applications: ELISA,IHC
Conjugation: Various

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Rabbit Anti-VIL1 Antibody (CSB-PA025855ESR1HU)


Alternative names:

Villin-1 Antibody,VIL1 Antibody,VIL Antibody

More alternative names for the antibody
D2S1471 antibody|OTTHUMP00000164145 antibody|VIL antibody|VIL1 antibody|VILI_HUMAN antibody|Villin 1 antibody|Villin-1 antibody|Villin1 antibody
Anti-Villin antibody [SP145] (ab130751)

Recommended applications: ELISA, IHC

Recommended dilution: Recommended dilution:IHC:1:20-1:200

Recommended protocols: check protocols


Anti-VIL1 Antibody

Catalogue No.





Recombinant human Villin-1 protein (1-350AA)











Molecular weight

92 kDa


Antigen Affinity Purified


Shipped at 4 Celcius Degree. Upon delivery aliquot and store at -20 Celcius Degree or -80 Celcius Degree. Avoid repeated freeze.

Protein function

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. .

Protein tissue specificity

Specifically expressed in epithelial cells. Major component of microvilli of intestinal epithelial cells and kidney proximal tubule cells. Expressed in canalicular microvilli of hepatocytes (at protein level). .

Involvement in disease

Note=Biliary atresia is a chronic and progressive cholestatic liver disease of chilhood characterized by an abnormal villin gene expression and severe malformation of canalicular microvillus structure.

Protein sequence and domain

Belongs to the villin/gelsolin family. Consists of a large core fragment in the N-terminal portion and a small headpiece (HP) in the C-terminal portion. The core fragment is necessary for both actin-nucleating and -severing activities, whereas the HP binds F-actin strongly in both the presence and absence of calcium and is necessary in actin-bundling activity. The Gelsolin-like 1 repeat is necessary for the actin-capping activity. The entire core fragment is necessary for the actin-severing activity. Two major calcium-sensitive sites are involved in conformational changes and determine separate functional properties: the first site (Glu-25, Asp-44 and Glu-74) regulates the actin-capping and actin-severing activities; while the second site (Asp-61, Asp-86 and Ala-93) regulates only the actin-severing activity.

Protein post-translational modifications

Tyrosine phosphorylation is induced by epidermal growth factor (EGF) and stimulates cell migration (By similarity). Phosphorylated on tyrosine residues by SRC. The unphosphorylated form increases the initial rate of actin-nucleating activity, whereas the tyrosine-phosphorlyated form inhibits actin-nucleating activity, enhances actin-bundling activity and enhances actin-severing activity by reducing high Ca(2+) requirements. The tyrosine-phosphorlyated form does not regulate actin-capping activity. Tyrosine phosphorylation is essential for cell migration: tyrosine phosphorylation sites in the N-terminus half regulate actin reorganization and cell morphology, whereas tyrosine phosphorylation sites in the C-terminus half regulate cell migration via interaction with PLCG1. .

Protein cellular localization

Cytoplasm, cytoskeleton. Cell projection, lamellipodium. Cell projection, ruffle. Cell projection, microvillus. Cell projection, filopodium tip . Cell projection, filopodium . Note=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. .

Research area

<a href="">All research areas</a>><a href="">Structural Proteins</a>><a href="">Villin</a><br><a href=""&gt; (View all antibody categories related to Structural Proteins)</a>


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Product type

Primary antibody


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