Anti-Villin Rabbit Antibody [C5M3]

Catalog No.: F2588

Application: Reactivity: Human

Usage Information

Dilution
WB1:100 IP1:40 IHC1:100 FCM1:100

Application
WB, IP, IHC, FCM

Reactivity
Human

Source
Rabbit

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW
93 kDa

Datasheet & SDS

Biological Description

Specificity
Anti-Villin Rabbit Antibody [C5M3] detects endogenous levels of total villin protein.

Clone
C5M3

Synonym(s)
VIL, VIL1, Villin-1

Background
Villin is a calcium-regulated actin-binding protein that plays a central role in the organization and dynamics of the actin cytoskeleton, particularly in epithelial cells that form brush borders for nutrient absorption. Structurally, villin is composed of three domains: two homologous core domains related to other actin-severing proteins (like gelsolin) and a unique C-terminal headpiece domain responsible for actin bundling. Its expression is tightly regulated during embryogenesis and, in adults, is largely restricted to epithelial cells of the gastrointestinal and urogenital tracts, where it localizes at the apical pole along F-actin bundles of microvilli. Functionally, villin exhibits calcium- and phosphoinositide-dependent activities including actin severing, capping, nucleation, and bundling, with its headpiece domain enabling unique cross-linking of filaments. Through these activities, villin is a key determinant of microvilli morphogenesis, stability, and remodeling, making it both a marker of intestinal differentiation and a regulator of epithelial architecture.

Background

Villin is a calcium-regulated actin-binding protein that plays a central role in the organization and dynamics of the actin cytoskeleton, particularly in epithelial cells that form brush borders for nutrient absorption. Structurally, villin is composed of three domains: two homologous core domains related to other actin-severing proteins (like gelsolin) and a unique C-terminal headpiece domain responsible for actin bundling. Its expression is tightly regulated during embryogenesis and, in adults, is largely restricted to epithelial cells of the gastrointestinal and urogenital tracts, where it localizes at the apical pole along F-actin bundles of microvilli. Functionally, villin exhibits calcium- and phosphoinositide-dependent activities including actin severing, capping, nucleation, and bundling, with its headpiece domain enabling unique cross-linking of filaments. Through these activities, villin is a key determinant of microvilli morphogenesis, stability, and remodeling, making it both a marker of intestinal differentiation and a regulator of epithelial architecture.

References
https://pubmed.ncbi.nlm.nih.gov/2256904/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

Tech Support

Answers to questions you may have can be found in the inhibitor handling instructions. Topics include how to prepare stock solutions, how to store inhibitors, and issues that need special attention for cell-based assays and animal experiments.

Handling Instructions

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%