• Formalin-fixed, paraffin-embedded human colon stained with anti-villin antibody using peroxidase-conjugate and DAB chromogen. Note brush border and cytoplasmic staining of epithelial cells

Anti-Villin antibody (179-311aa) [ZR155] (STJ180547)

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STJ180547

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Host: Rabbit
Applications: IHC-P
Reactivity: Human
Note: STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.
Short Description: Rabbit monoclonal antibody anti-Villin (179-311aa) is suitable for use in Immunohistochemistry research applications.
Clonality: Monoclonal
Clone ID: ZR155
Conjugation: Unconjugated
Isotype: IgG
Formulation: Tris-HCI buffer containing stabilizing protein (BSA) and <0.1% ProClin
Purification: Affinity purified
Dilution Range: 1:100-200
Storage Instruction: Store at 2‐8°C for up to 24 months. Predilute: Ready to use, no reconstitution necessary. Concentrate: Use dilution range and appropriate lab‐standardized diluent. Stability after dilution: 7 days at 24°C, 3 months at 2‐8°C, 6months at ‐20°C.
Gene Symbol: VIL1
Gene ID: 7429
Uniprot ID: VILI_HUMAN
Immunogen Region: 179-311aa
Specificity: Positive control: Colon carcinoma, small intestine
Immunogen: Recombinant human Villin fragment (around aa179-311)
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).
Post Translational Modifications Tyrosine phosphorylation is induced by epidermal growth factor (EGF) and stimulates cell migration. Phosphorylated on tyrosine residues by SRC. The unphosphorylated form increases the initial rate of actin-nucleating activity, whereas the tyrosine-phosphorylated form inhibits actin-nucleating activity, enhances actin-bundling activity and enhances actin-severing activity by reducing high Ca(2+) requirements. The tyrosine-phosphorylated 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.
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 Name Villin-1
Cellular Localisation Cytoplasm
Cytoskeleton
Cell Projection
Lamellipodium
Ruffle
Microvillus
Filopodium Tip
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
Rapidly Redistributed To Ruffles And Lamellipodia Structures In Response To Autotaxin
Lysophosphatidic Acid (Lpa) And Epidermal Growth Factor (Egf) Treatment
Alternative Antibody Names Anti-Villin-1 antibody
Anti-VIL1 antibody
Anti-VIL antibody

Information sourced from Uniprot.org

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