* Allow all reagents to warm to room temperature for at least 30 minutes before opening.
* Pre-rinse the pipet tip with reagent, use fresh pipet tips for each sample, standard and reagent to avoid contamination.
* Unused wells must be kept desiccated at 4 degree C in the sealed bag provided.
* Mix Thoroughly is very important for the result. It is recommended using low frequency oscillator or slight hand shaking every 10 minutes.
* It is recommended that all samples and standards be assayed in duplicate or triplicate.
Background: Villin is a 92.5 kDa tissue-specific actin-binding protein associated with the actin core bundle of the brush border. Villin contains multiple gelsolin-like domains capped by a small (8.5 kDa) "headpiece" at the C-terminus consisting of a fast and independently-folding three-helix bundle that is stabilized by hydrophobic interactions. The headpiece domain is a commonly studied protein in molecular dynamics due to its small size and fast folding kinetics and short primary sequence.Villin is an actin binding protein expressed mainly in the brush border of the epithelium in vertebrates but sometimes it is ubiquitously expressed in protists and plants. Villin is found localized in the microvilli of the brush border of the epithelium lining of the gut and renal tubes in vertebrates.
NCBI and Uniprot Product Information
NCBI Description
This gene encodes a member of a family of calcium-regulated actin-binding proteins. This protein represents a dominant part of the brush border cytoskeleton which functions in the capping, severing, and bundling of actin filaments. Two mRNAs of 2.7 kb and 3.5 kb have been observed; they result from utilization of alternate poly-adenylation signals present in the terminal exon. [provided by RefSeq, Jul 2008]
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: Actin-binding; Motility/polarity/chemotaxis
Chromosomal Location of Human Ortholog: 2q35
Cellular Component: actin filament bundle; brush border; cytoplasm; filopodium; filopodium tip; lamellipodium; microvillus; nucleoplasm; plasma membrane; ruffle
Molecular Function: actin filament binding; calcium ion binding; caspase inhibitor activity; identical protein 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; barbed-end actin filament capping; D-glucose absorption; epidermal growth factor receptor signaling pathway; epithelial cell differentiation; negative regulation of caspase activity; positive regulation of actin filament bundle formation; positive regulation of actin filament depolymerization; positive regulation of cell migration; positive regulation of multicellular organism growth; protein complex assembly; regulation of actin nucleation; regulation of cell shape; regulation of microvillus length; response to bacterium
Research Articles on VIL1
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Product Notes
The Human VIL1 vil1 (Catalog #AAA9713724) is an ELISA Kit and is intended for research purposes only. The product is available for immediate purchase. The AAA9713724 ELISA Kit recognizes Human VIL1. It is sometimes possible for the material contained within the vial of "Villin-1 (VIL1), ELISA Kit" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.Precautions
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