Vil1 Polyclonal Antibody for Mouse(Mus musculus) | EIAab.comVil1 Polyclonal Antibody for Mouse(Mus musculus)

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Vil1 (Gene name),

Villin-1 (Protein name ), VILI_MOUSE from NCBI database.

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General Annotation

Antigen Annotation

Predicted Eptitope

Vaild Sequence

Related Databases

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Gene name:

Vil1(Vil);

Protein name:

Villin-1;

Alternative:

Organism:

Mouse (Mus musculus).

General Annotation

Sub Unit:

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) (By similarity). Interacts (phosphorylated form) with PLCG1; the interaction is enhanced by hepatocyte growth factor (HGF).

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.

Subcellular Location:

Cytoplasm cytoskeleton Cell projection microvillus Cell projection lamellipodium Cell projection ruffle Cell projection filopodium tip Cell projection filopodium Rapidly redistributed to ruffles and lamellipodia structures in response to autotaxin, lysophosphatidic acid (LPA) and epidermal growth factor (EGF) treatment (By similarity). 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.

Protein Attributes:

Sequence length:

827

Sequence:

50:

100:

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827:

ALGMTPAAFS | ALPRWKQQNI | KKEKGLF

3D Structure:

N/A

Predicted Eptitope:

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Vaild Sequence:

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Related Databases

Pfam:

PF00626

String:

Q62468

KEGG:

mmu:22349

SMR:

Q62468

UniGene:

Mm.471601

Uniprot:

Q62468

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ELISA Kit for Mouse Villin-1

Cat.:

E0193h

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96T

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ELISA Kit for Mouse Villin-1

Cat.:

E0193m

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96T

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ELISA Kit for Mouse Villin-1

Cat.:

E0193p

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96T

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ELISA Kit for Mouse Villin-1

Cat.:

E0193c

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96T

ELISA Kit for Mouse Villin-1

Cat.:

E0193b

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96T

CLIA Kit for Mouse Villin-1

Cat.:

U0193h

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96T

CLIA Kit for Mouse Villin-1

Cat.:

U0193c

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96T

CLIA Kit for Mouse Villin-1

Cat.:

U0193b

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MSDS:

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96T

CLIA Kit for Mouse Villin-1

Cat.:

U0193m

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96T

CLIA Kit for Mouse Villin-1

Cat.:

U0193p

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96T

Polyclonal Antibody for Mouse Villin-1

Cat.:

P0193Rb-m

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Packing:

40ug/0.2ml

Polyclonal Antibody for Mouse Villin-1

Cat.:

P0193Rb-h

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40ug/0.2ml

Polyclonal Antibody for Mouse Villin-1

Monoclonal Antibody for Mouse Villin-1

Protein for Mouse Villin-1

R&D Technical Data

For more information, please refer to the manual,Or contact our technical support: tech@eiaab.com.

Precision

For more information, please refer to the manual,Or contact our technical support: tech@eiaab.com.

Recovery

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Linearity

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References

1.

"Expression and localization of villin, fimbrin, and myosin I in differentiating mouse F9 teratocarcinoma cells."
Ezzell R.M. , Leung J. , Collins K. , Chafel M.M. , Cardozo T.J. , Matsudaira P.T.
Dev. Biol.151:575-585(1992) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA]
2.

"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res.14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]
strain: FVB/N.
tissue: Brain.
tissue: Kidney.
3.

"In vivo, villin is required for Ca(2+)-dependent F-actin disruption in intestinal brush borders."
Ferrary E. , Cohen-Tannoudji M. , Pehau-Arnaudet G. , Lapillonne A. , Athman R. , Ruiz T. , Boulouha L. , El Marjou F. , Doye A. , Fontaine J.J. , Antony C. , Babinet C. , Louvard D. , Jaisser F. , Robine S.
J. Cell Biol.146:819-830(1999) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: DISRUPTION PHENOTYPE;SUBCELLULAR LOCATION;TISSUE SPECIFICITY
4.

"Villin enhances hepatocyte growth factor-induced actin cytoskeleton remodeling in epithelial cells."
Athman R. , Louvard D. , Robine S.
Mol. Biol. Cell14:4641-4653(2003) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION;TYROSINE PHOSPHORYLATION;DISRUPTION PHENOTYPE;SUBCELLULAR LOCATION
5.

"Shigella flexneri infection is dependent on villin in the mouse intestine and in primary cultures of intestinal epithelial cells."
Athman R. , Fernandez M.I. , Gounon P. , Sansonetti P. , Louvard D. , Philpott D. , Robine S.
Cell. Microbiol.7:1109-1116(2005) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION IN SHIGELLA FLEXNERI INFECTION;DISRUPTION PHENOTYPE;SUBCELLULAR LOCATION;TISSUE SPECIFICITY
6.

"A novel role for villin in intestinal epithelial cell survival and homeostasis."
Wang Y. , Srinivasan K. , Siddiqui M.R. , George S.P. , Tomar A. , Khurana S.
J. Biol. Chem.283:9454-9464(2008) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION;DISRUPTION PHENOTYPE

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