- Catalog number
- PB9457-APC
- Size / count
- 100 µg/Vial
- Dry ice
- No
- Hazardous
- No
- Discontinued
- No
- Background
- Villin is known as VIL1. 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. In vertebrates, the villin proteins help to support the microfilaments of the microvilli of the brush border. It may play a role in cell plasticity through F-actin severing.
- Synonyms
- Villin-1;VIL1;VIL;
- Gene Name
- Villin-1
- UniProt
- P09327
- Host
- Rabbit
- Reactivity
- Human,Mouse,Rat
- Cross Reactivity
- No cross-reactivity with other proteins
- Immunogen
- A synthetic peptide corresponding to a sequence at the C-terminus of human Villin, different from the related mouse sequence by three amino acids.
- Clonality
- Polyclonal
- 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). .
- Applications
- Flow Cytometry,IF,IHC,WB
- Purification
- Immunogen affinity purified.
- Concentration
- Adding 0.2 ml of distilled water will yield a concentration of 500 μg/ml.
- Form
- Lyophilized
- Reconstitution
- Add 0.2ml of distilled water will yield a concentration of 500ug/ml.
- 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. .
- Storage Conditions
- Store at -20℃ for one year from date of receipt. After reconstitution, at 4℃ for one month. It can also be aliquotted and stored frozen at -20℃ for six months. Avoid repeated freeze-thaw cycles.
- Fragment
- Rabbit IgG
- Applications Notes
- Western blot, 0.1-0.5μg/ml, Human, Mouse, Rat<br>
Immunohistochemistry (Paraffin-embedded Section), 0.5-1μg/ml, Human, Mouse, Rat, By Heat<br>
Immunofluorescence, 2μg/ml, Human, Mouse, Rat<br>
Flow Cytometry (Fixed), 1-3μg/1x10<sup>6</sup> cells, Human<br>
- Subcellular Location
- Cytoplasm, cytoskeleton. Cell projection, lamellipodium. Cell projection, ruffle. Cell projection, microvillus. Cell projection, filopodium tip . Cell projection, 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 (By similarity). Rapidly redistributed to ruffles and lamellipodia structures in response to autotaxin, lysophosphatidic acid (LPA) and epidermal growth factor (EGF) treatment. .
- Sequence Similarities
- Belongs to the villin/gelsolin family.
- Protein Name
- Villin-1