Villin-1 (VIL1) Recombinant Protein | VIL1 recombinant protein

Recombinant Chicken Villin-1 (VIL1), partial

• Gene Names: VIL1; VIL
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Villin-1 (VIL1); Recombinant Chicken Villin-1 (VIL1); partial; VIL1 recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Length: 826

• Species: Chicken
• Preparation and Storage: Store at -20 degrees C. For long-term storage, store at -20 degrees C or -80 degrees C. Store working aliquots at 4 degrees C for up to one week. Repeated freezing and thawing is not recommended.

Related Product Information for VIL1 recombinant protein

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.

NCBI and Uniprot Product Information

• NCBI GI #: 45382125
• NCBI GeneID: 396423
• NCBI Accession #: NP_990773.1
• NCBI GenBank Nucleotide #: NM_205442.1
• UniProt Accession #: P02640
• Molecular Weight: 92,479 Da
• NCBI Official Full Name: villin-1
• NCBI Official Synonym Full Names: villin 1
• NCBI Official Symbol: VIL1
• NCBI Official Synonym Symbols: VIL
• NCBI Protein Information: villin-1
• UniProt Protein Name: Villin-1
• Protein Family: VIN3-like protein
• UniProt Gene Name: VIL1
• UniProt Synonym Gene Names: VIL

Uniprot Description

Epithelial cell-specific Ca2+-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 (). Its actin-bundling activity is inhibited by tropomyosin.