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SAB4200532

Sigma-Aldrich

Anti-Villin-1 (C-terminal region) antibody produced in rabbit

~1.0 mg/mL, affinity isolated antibody

Synonym(s):

Anti-VIL, Anti-VIL1

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~95 kDa

species reactivity

human

concentration

~1.0 mg/mL

technique(s)

immunohistochemistry: 20-30 μg/mL using human small intestine.
immunoprecipitation (IP): 5-10 μg using Caco-2 cells.
indirect immunofluorescence: 5-10 μg/mL using Caco-2 cells.
western blot: 1-2 μg/mL using WiDR cells.

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... VIL1(7429)

General description

Villin also known as villin-1 or VIL1 is a Ca2+-regulated actin-binding protein and belongs to the gelsolin family. It is localized in the apical cytoplasm and brush borders of epithelial cells of the small and large intestinal mucosa, intrahepatic bile ducts, kidney proximal tubules, gall bladder epithelium and pancreatic ducts. Villin is located on the human chromosome at 2q35.

Specificity

Anti-Villin-1 (C-terminal region) specifically recognizes human villin-1.

Immunogen

synthetic peptide corresponding to a sequence at the C-terminal region of human villin-1, conjugated to KLH. The corresponding sequence is highly conserved (single amino acid substitution) in rat and mouse villin-1.

application

Anti-Villin-1 (C-terminal region) antibody produced in rabbit may be used in:
  • immunoblotting
  • immunoprecipitation
  • immunofluorescence
  • immunohistochemistry

Biochem/physiol Actions

Villin-1 is involved in modulating the structure and assembly of actin filaments. It also functions in regulating cell migration through its phosphorylation at Tyr-60, Tyr-81 and Tyr-256. Villin is involved in microvillus assembly and acts as a marker for epithelial cell differentiation. Its expression is stimulated during intestinal metaplasia observed in Barrett′s esophagus and chronic atrophic gastritis. Overexpression of villin is seen in human adenocarcinomas, such as colorectal cancer.

Physical form

Solution in 0.01 M phos­phate buffered saline, pH 7.4, containing 15 mM sodium azide.

Storage and Stability

For continuous use, store at 2-8 °C for up to one month. For extended storage, freeze in working aliquots. Repeated freezing and thawing, or storage in “frost-free” freezers,is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilutions should be discarded if not used within 12 hours.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class

10 - Combustible liquids

flash_point_f

Not applicable

flash_point_c

Not applicable


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Dendritic spine actin cytoskeleton in autism spectrum disorder
Joensuu M, et al.
Progress in Neuro-Psychopharmacology & Biological Psychiatry, 84(14), 362-381 (2018)
Villin expression is frequently lost in poorly differentiated colon cancer
Arango D, et al.
The American Journal of Pathology, 180(4), 1509-1521 (2012)
Dynamic effects of acid on Barrett's esophagus. An ex vivo proliferation and differentiation model.
Fitzgerald R C, et al.
The Journal of Clinical Investigation, 98(9), 2120-2128 (1996)
Seema Khurana et al.
FEBS letters, 582(14), 2128-2139 (2008-03-01)
Villin is a tissue-specific actin modifying protein that is associated with actin filaments in the microvilli and terminal web of epithelial cells. It belongs to a large family of actin-binding proteins which includes actin-capping, -nucleating and/or -severing proteins such as

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