Villin-1 Antibody (N-term)
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, IHC-P, FC, E |
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Primary Accession | P09327 |
Other Accession | Q29261, Q62468, Q3SZP7 |
Reactivity | Human, Mouse |
Predicted | Bovine, Pig |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 92695 Da |
Antigen Region | 180-207 aa |
Gene ID | 7429 |
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Other Names | Villin-1, VIL1, VIL |
Target/Specificity | This Villin-1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 180-207 amino acids from the N-terminal region of human Villin-1. |
Dilution | WB~~1:2000 IHC-P~~1:25 FC~~1:25 |
Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | Villin-1 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | VIL1 |
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Synonyms | VIL |
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. |
Cellular Location | Cytoplasm, cytoskeleton. Cell projection, lamellipodium. Cell projection, ruffle. Cell projection, microvillus Cell projection, filopodium tip. Cell projection, filopodium. Note=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. |
Tissue Location | 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). |
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Provided below are standard protocols that you may find useful for product applications.
Background
Villin-1 is 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.
References
Yamamichi,N., et.al., Exp. Cell Res. 315 (10), 1779-1789 (2009)
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