Mouse Anti-Villin (ready to ues) antibody

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VIL; VIL1; Villin 1; Villin-1; Villin1; D2S1471; OTTHUMP00000164145; VILI_HUMAN.

Cat:

SH0137

Species Reactivity：

Human,

Immunogen：

Recombinant human villin protein

Format：

Liquid

Storage instructions：

Shipped at 4℃. Store at -20 °C for one year. Avoid repeated freeze/thaw cycles.

Clonality：

Monoclonal

Isotype：

IgG2b

Applications：

IHC-P=IHC-F=ICC=IF=（Paraffin sections need to do antigen repair）not yet tested in other applications.optimal dilutions/concentrations should be determined by the end user.

Host：

Mouse

Product Overview：

Paraformaldehyde-fixed, paraffin embedded (human colon); Antigen retrieval by boiling in sodium citrate buffer (pH6.0) for 15min; Block endogenous peroxidase by 3% hydrogen peroxide for 20 minutes; Blocking buffer (normal goat serum) at 37°C for 30min; Antibody incubation with (Villin) Monoclonal Antibody, Unconjugated (SH0137) at 1:200 overnight at 4°C, followed by operating according to SP Kit(Mouse)(sp-0024) instructionsand DAB staining.

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Unit:

Price: $92.00

Product PDFs

Datasheet: Down Datasheet

Other Information
Citations
Protein Attributes
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Villin can cap, nucleate, sever and bundle actin in a calcium and phosphoinositide regulated manner. It is associated with the microvillar actin core bundle of intestinal and renal brush border implicated in adsorption. Villin is composed of six repeats, each containing 150 residues that together constitute the core domain followed by the carboxyl terminal headpiece domain of 87 residues. The core domain retains the calcium dependent capping nucleating and severing activity, whereas the headpiece domain contributes towards actin filament bundling and binding F actin, independently of Calcium.

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.

Subunit:
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 SLCterminus tyrosine phosphorylation sites) with PLCG1 (via the SH2 domains). Interacts (phosphorylated form) with PLCG1; the interaction is enhanced by hepatocyte growth factor (HGF) (By similarity).

Subcellular Location:
Cytoplasm, cytoskeleton. Cell projection, lamellipodium. Cell projection, ruffle. Cell projection, microvillus. Cell projection, filopodium tip (By similarity). Cell projection, filopodium (By similarity). 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 Specificity:
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).

Post-translational modifications:
Tyrosine phosphorylation is induced by epidermal growth factor (EGF) and stimulates cell migration (By similarity). Phosphorylated on tyrosine residues by SRC. The unphosphorylated form increases the initial rate of actin-nucleating activity, whereas the tyrosine-phosphorlyated form inhibits actin-nucleating activity, enhances actin-bundling activity and enhances actin-severing activity by reducing high Ca(2+) requirements. The tyrosine-phosphorlyated 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 SLCterminus half regulate cell migration via interaction with PLCG1.

DISEASE:
Note=Biliary atresia is a chronic and progressive cholestatic liver disease of chilhood characterized by an abnormal villin gene expression and severe malformation of canalicular microvillus structure.

Similarity:
Belongs to the villin/gelsolin family.
Contains 6 gelsolin-like repeats.
Contains 1 HP (headpiece) domain

SWISS:
P09327

Gene ID:
7429

Database links:

Entrez Gene: 7429 Human

Entrez Gene: 22349 Mouse

Omim: 193040 Human

SwissProt: P09327 Human

SwissProt: Q62468 Mouse

Unigene: 654595 Human

Unigene: 471601 Mouse

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