Anti-VIL1 antibody (601-650 aa) (STJ98578)
SPECIFICATIONS
ClonalityPolyclonal
HostRabbit
ConjugationUnconjugated
IsotypeIgG
ImmunogenSynthesized peptide derived from Villin at the amino acid range 601-650
General Information
| Short Description | Rabbit polyclonal anti-Villin-1 (601-650 aa) for use in WB and ELISA in Human, Mouse and Rat samples. Datasheet included with dilution recommendations, and related reagents. |
| Applications | WB/ELISA |
| Host | Rabbit |
| Reactivity | Human/Mouse/Rat |
| Note | STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
Product Properties
| Clonality | Polyclonal |
| Isotype | IgG |
| Conjugation | Unconjugated |
| Concentration | 1 mg/mL |
| Purification | The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen. |
| Dilution Range | WB 1:500-2000ELISA 1:10000-20000 |
| Formulation | Liquid in PBS containing 50% Glycerol, 0.5% BSA and 0.02% Sodium Azide. |
| Storage Instruction | Store at-20ยฐC for up to 1 year from the date of receipt, and avoid repeat freeze-thaw cycles. |
Target Information
| Gene Symbol | VIL1 |
| Gene ID | 7429 |
| Uniprot ID | VILI_HUMAN |
| Immunogen | Synthesized peptide derived from Villin at the amino acid range 601-650 |
| Immunogen Region | 601-650 aa |
| Specificity | Villin Polyclonal Antibody detects endogenous levels of Villin |
Additional Info
| Post Translational Modifications | Tyrosine phosphorylation is induced by epidermal growth factor (EGF) and stimulates cell migration. Phosphorylated on tyrosine residues by SRC. The unphosphorylated form increases the initial rate of actin-nucleating activity, whereas the tyrosine-phosphorylated form inhibits actin-nucleating activity, enhances actin-bundling activity and enhances actin-severing activity by reducing high Ca(2+) requirements. The tyrosine-phosphorylated form does not regulate actin-capping activity. Tyrosine phosphorylation is essential for cell migration: tyrosine phosphorylation sites in the N-terminus half regulate actin reorganization and cell morphology, whereas tyrosine phosphorylation sites in the C-terminus half regulate cell migration via interaction with PLCG1. |
| 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. |
| Protein Name | Villin-1 |
| Database Links | |
| Cellular Localisation | CytoplasmCytoskeletonCell ProjectionLamellipodiumRuffleMicrovillusFilopodium TipFilopodiumRelocalized In The Tip Of Cellular Protrusions And Filipodial Extensions Upon Infection With SFlexneri In Primary Intestinal Epithelial Cells (Iec) And In The Tail-Like Structures Forming The Actin Comets Of SFlexneriRedistributed To The Leading Edge Of Hepatocyte Growth Factor (Hgf)-Induced LamellipodiaRapidly Redistributed To Ruffles And Lamellipodia Structures In Response To AutotaxinLysophosphatidic Acid (Lpa) And Epidermal Growth Factor (Egf) Treatment |
| Alternative Antibody Names | Anti-Villin-1 antibodyAnti-VIL1 antibodyAnti-VIL antibody |
Information sourced from Uniprot.org