| Field | Specification |
|---|---|
| Mfr No | |
| Alternative Names | Villin-1;VIL1;VIL; |
| Cellular Localization | |
| Clonality | |
| Concentration | |
| Host | |
| 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. |
| Isotype | |
| Molecular Weight | |
| Product Type | |
| Reactivity | |
| Reconstitution | |
| Target | |
| UniProt # |
Overview
This antibody is intended for detection of VIL1 (Villin-1) in biological samples using common immunoassay formats. It is typically selected based on target identity, species reactivity, clonality/clone information, and detection modality.
Vendor notes: Boster Bio Anti-Villin/VIL1 Antibody Picoband® catalog # PB9457. Tested in Flow Cytometry, IF, IHC, WB applications. This antibody reacts with Human, Mouse, Rat. The brand Picoband indicates this is a premium antibody that guarantees superior quality, high affinity, and strong signals with minimal background in Western blot applications. Only our best-performing antibodies are designated as Picoband, ensuring unmatched performance.
Key elements and design rationale
- Antibody format: Rabbit Polyclonal Rabbit IgG
- Immunogen / epitope context: A synthetic peptide corresponding to a sequence at the C-terminus of human Villin, different from the related mouse sequence by three amino acids.
- Molecular weight context: reported MW: 93 kDa; calculated MW: 92695 MW
- Reactivity: Human,Mouse,Rat
- Applications: Flow Cytometry, IF, IHC, WB
As a polyclonal antibody, the reagent recognizes multiple epitopes on the target, which can improve detection robustness but may increase sensitivity to sample-dependent epitope changes.
Biological background
Villin-1; Villin-1. 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. Functional note: 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. . Reported localization: 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. . Expression/tissue context: 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). .
Research relevance and current trends
- Actin Binding Proteins: Researchers commonly examine how VIL1 (Villin-1) relates to this theme using model systems and orthogonal readouts.
- Actin: Researchers commonly examine how VIL1 (Villin-1) relates to this theme using model systems and orthogonal readouts.
- etc.: Researchers commonly examine how VIL1 (Villin-1) relates to this theme using model systems and orthogonal readouts.
Common research applications
- Western blotting: compare relative VIL1 (Villin-1) levels across conditions; band patterns may reflect isoforms and processing.
- IHC/IHC-F: assess spatial distribution of VIL1 (Villin-1) across tissue regions and cell types using matched controls.
- IF/ICC: evaluate subcellular localization and co-localization patterns; signal can depend on fixation/permeabilization and epitope accessibility.
- Flow cytometry: quantify target-positive populations and shifts in expression; gating strategy and background staining controls are essential.
Notes for experimental interpretation
- Specificity notes: No cross reactivity with other proteins.
- Cross-reactivity: No cross-reactivity with other proteins
- Family / similarity context: Belongs to the villin/gelsolin family.
- Isoforms and PTMs: Apparent size and signal patterns can differ across splice isoforms, proteolytic processing, and post-translational modifications.
- Controls: Include an isotype control (as relevant), no-primary control for imaging, and orthogonal validation such as KD/KO samples when available.
Customization & Add-ons: Can’t find the antibody you need—or require a custom format for your assay? We can help you source the best match or support custom antibody solutions for diverse research needs, including species and isotype selection, conjugations and labeling (e.g., HRP/AP, biotin, fluorophores), purification grade options (Protein A/G, affinity purified), formulation preferences (buffer selection, carrier-free, glycerol-free), custom concentrations and aliquoting, low-endotoxin options for cell-based work, and application-focused QC/validation support (project dependent). Click Talk to a Scientist to submit a request, email us at support@biohippo.com, or explore our Research Services for additional support—our team will follow up with feasibility details and next steps.