Monoclonal Antibody to Villin (Clone: ABM4E64)
Fig-1: Western blot analysis of Villin. Anti-Villin antibody (Clone: ABM4E64) was tested at 0.5 µg/ml on h Kidney lysate.
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Format : | Purified |
Amount : | 100 µg |
Isotype : | Mouse IgG2b Kappa |
Purification : | Protein G Chromatography |
Content : | 25 µg in 50 µl/100 µg in 200 µl PBS containing 0.05% BSA and 0.05% sodium azide. Sodium azide is highly toxic. |
Storage condition : | Store the antibody at 4°C; stable for 6 months. For long-term storage; store at -20°C. Avoid repeated freeze and thaw cycles. |
Villin is a protein that belongs to the gelsolin family of calcium-regulated actin-binding proteins. It is expressed in differentiated epithelial cells with a brush border such as intestinal villi, proximal renal tubules, oviduct, and seminiferous ducts. Villin shares structural and functional homology with two conserved families of proteins. One family of proteins, which includes gelsolin and adseverin, shares the conserved domain(s) found in the villin core. Villin regulates cell migration, cell death, and epithelial-to-mesenchymal transition underscoring the significance of this protein to epithelial cell function.
Western blot analysis: 0.5-1 µg/ml; Immunohistochemical analysis-5-10 µg/ml
For Research Use Only. Not for use in diagnostic/therapeutics procedures.
Subcellular location: | Cytoplasm, Cell projection, Cell projection, Cell projection, Cell projection, Cell projection |
Post transnational modification: | 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. |
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). |
BioGrid: | 113270. 6 interactions. |
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