Mouse Villin-1 ELISA Kit | Vil1 elisa kit

Mouse Villin-1 ELISA Kit

Cat. Num. AAA2885904

• Gene Names: Vil1; Vil
• Reactivity: Mouse
• Synonyms: Villin-1; Mouse Villin-1 ELISA Kit; Vil1; Vil; Vil1 elisa kit

• Reactivity: Mouse
• Sequence Length: 827

• Assay Type: Sandwich
• Detection Range: 0.156-10 ng/mL
• Sensitivity: 0.078 ng/mL
• Intra-Assay CV: <=4.1%
• Inter-Assay CV: <=7.2%
• Recovery: 86%
• Preparation and Storage: For long term storage, please store the entire kit at -20 degree C.

Typical Testing Data/Standard Curve (for reference only)

NCBI and Uniprot Product Information

• NCBI GI #: 190684696
• NCBI GeneID: 22349
• NCBI Accession #: NP_033535.2
• NCBI GenBank Nucleotide #: NM_009509.2
• UniProt Accession #: Q62468; Q149B6; Q91WH4
• Molecular Weight: 92,775 Da
• NCBI Official Full Name: villin-1
• NCBI Official Synonym Full Names: villin 1
• NCBI Official Symbol: Vil1
• NCBI Official Synonym Symbols: Vil
• NCBI Protein Information: villin-1
• UniProt Protein Name: Villin-1
• Protein Family: Villin
• UniProt Gene Name: Vil1
• UniProt Synonym Gene Names: Vil
• UniProt Entry Name: VILI_MOUSE

Uniprot Description

Villin: 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. Monomer. Homodimer; homodimerization is necessary for actin-bundling. Associates with F-actin; phosphorylation at tyrosines 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). Specifically expressed in epithelial cells. Major component of microvilli of intestinal epithelial cells and kidney proximal tubule cells. Expressed in canalicular microvilli of hepatocytes. Belongs to the villin/gelsolin family.

Protein type: Motility/polarity/chemotaxis; Actin-binding

Cellular Component: actin filament bundle; brush border; cell projection; cytoplasm; cytoskeleton; filopodium; filopodium tip; lamellipodium; microvillus; nucleoplasm; plasma membrane; ruffle

Molecular Function: actin binding; actin filament binding; calcium ion binding; caspase inhibitor activity; identical protein binding; metal ion binding; phosphatidylinositol-4,5-bisphosphate binding; protein binding; protein homodimerization activity

Biological Process: actin filament capping; actin filament depolymerization; actin filament polymerization; actin filament severing; actin nucleation; apoptosis; barbed-end actin filament capping; cytoskeleton organization and biogenesis; D-glucose absorption; epidermal growth factor receptor signaling pathway; microvillus biogenesis; positive regulation of actin filament bundle formation; positive regulation of actin filament depolymerization; positive regulation of cell migration; positive regulation of multicellular organism growth; regulation of actin nucleation; regulation of cell shape; regulation of microvillus length; response to bacterium