Villin-1 Blocking Peptide | VIL1 blocking peptide

Villin-1 Antibody (N-term) Blocking Peptide

• Gene Names: VIL1; VIL; D2S1471
• Synonyms: Villin-1; Villin-1 Antibody (N-term) Blocking Peptide; VIL1; VIL; VIL1 blocking peptide

• Specificity: The synthetic peptide sequence used to generate the antibody was selected from the N-term region of human Villin-1. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.
• Form/Format: Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.
• Sequence Length: 827

• 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).
• Preparation and Storage: Maintain refrigerated at 2-8 degree C for up to 6 months. For long term storage store at -20 degree C.

Related Product Information for VIL1 blocking peptide

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.

NCBI and Uniprot Product Information

• NCBI GI #: 224471905
• NCBI GeneID: 7429
• UniProt Accession #: P09327; Q53S11; Q96AC8; B2R9A7
• Molecular Weight: 46,567 Da
• NCBI Official Full Name: Villin-1
• NCBI Official Synonym Full Names: villin 1
• NCBI Official Symbol: VIL1
• NCBI Official Synonym Symbols: VIL; D2S1471
• 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_HUMAN

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: Motility/polarity/chemotaxis; Actin-binding

Chromosomal Location of Human Ortholog: 2q35

Cellular Component: actin filament bundle; brush border; 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; barbed-end actin filament capping; epidermal growth factor receptor signaling pathway; epithelial cell differentiation; positive regulation of actin filament bundle formation; positive regulation of actin filament depolymerization; positive regulation of cell migration; protein complex assembly; regulation of actin nucleation; regulation of cell shape; response to bacterium