Villin Antibody (YA3548)
Villin Antibody (YA3548) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to Villin.
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Host:
Rabbit
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Isotype:
IgG
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Application:
WB, IHC-P, IP
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Reactivity :
Human
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Formulation:
Supplied in 10mM PBS, pH 7.4, 150mM sodium chloride, 0.05% BSA, 0.02% sodium azide and 50% glycerol.
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Conjugation:
Non-conjugated
To place orders, for customer services and technical support, please contact: MedChemExpress USA
Tel: 609-228-6898 E-mail: [email protected] [email protected]
Applications
| Application |
WB
WB: Western Blot
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IHC-P
IHC-P: Immunohistochemistry-Paraffin
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IP
IP: Immunoprecipitation
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|---|---|---|---|
| Dilution Ratio | 1:500-1:1000 | 1:50-1:100 | 1:50 |
Product Details
Villin Antibody (YA3548) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to Villin.
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Host Rabbit
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Clonality Recombinant,Monoclonal
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Species ReactivityHuman
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Observed Molecular WeightObserved band size: 93 kDa
Note: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
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Calculated Molecular Weight Predicted band size: 93 kDa
A synthesized peptide derived from human Villin-1 aa640-693/827.
Endogenous
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Liquid
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Formulation
Supplied in 10mM PBS, pH 7.4, 150mM sodium chloride, 0.05% BSA, 0.02% sodium azide and 50% glycerol.
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
Background
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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
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Subcellular Localization
Cytoplasm, cytoskeleton; Cell projection, lamellipodium; Cell projection, ruffle; Cell projection, microvillus; Cell projection, filopodium tip; Cell projection, filopodium
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Expression
Tissue_specificity:It is specifically expressed on epithelial cells. It is a major component of the microvilli of intestinal epithelial cells and proximal tubular cells of the kidney. It is also expressed (at the protein level) in the capillary bile duct microvilli of hepatocytes. -
Isoforms & Post-Translational Modification
P09327 has 2 isomers: P09327-1: 92695 Da (predicted); P09327-2: 46567 Da (predicted).
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-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 -
Subunit
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) (By similarity)
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SwissProt ID
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Research Field
Signal Transduction
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