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Human Monoclonal VIL1 Primary Antibody for IHC (p) - ABIN180459
Fath, Burgess: Microvillus assembly. Not actin alone. in Current biology : CB 1995
Show all 2 references for ABIN180459
Human Polyclonal VIL1 Primary Antibody for IHC, IHC (p) - ABIN4365288
Kiflemariam, Andersson, Asplund, Pontén, Sjöblom: Scalable in situ hybridization on tissue arrays for validation of novel cancer and tissue-specific biomarkers. in PLoS ONE 2012
Human Polyclonal VIL1 Primary Antibody for FACS, IHC (p) - ABIN390742
Yamamichi, Inada, Furukawa, Sakurai, Tando, Ishizaka, Haraguchi, Mizutani, Fujishiro, Shimomura, Oka, Ichinose, Tsutsumi, Omata, Iba: Cdx2 and the Brm-type SWI/SNF complex cooperatively regulate villin expression in gastrointestinal cells. in Experimental cell research 2009
villin directly interacts with a transcriptional corepressor and ligand of the Slug (show SNAI2 Antibodies) promoter, ZBRK1 (show ZNF350 Antibodies).
Data indicate an association between highly fucosylated glycans and caudal type homeobox 1 (CDX1 (show CDX1 Antibodies)) and/or villin mRNA expression that both correlate with cell differentiation.
study demonstrates that G. duodenalis-mediated disruption of villin is, at least, in part dependent on activation of myosin light chain kinase (show MYLK Antibodies)
Thus, villin plays an important role in establishing the balance between actin polymerization and actin severing to facilitate the initial steps of Salmonella entry.
Collective expression pattern of tensin (show TNS1 Antibodies)/profilin-1 (show PFN1 Antibodies)/villin-1/talin could be a biomarker to estimate the prognosis of esophageal squamous cell carcinoma patients.
harmonin (show USH1C Antibodies) and villin autoantibodies are sensitive and specific markers of IPEX (show FOXP3 Antibodies), differentiate IPEX (show FOXP3 Antibodies), including atypical cases, from other early childhood disorders associated with enteropathy
villin immunohistochemistry is a reliable and superior adjunct in the diagnosis of microvillus inclusion disease
Discriminated small-cell lung carcinoma from large-cell neuroendocrine lung carcinoma with immunohistochemical markers BAI3 (show BAI3 Antibodies), CDX2 (show CDX2 Antibodies) and VIL1.
We demonstrated that the VIL1 gene is a potential candidate molecular marker for high serum AFP (show AFP Antibodies)-associated HCC (show FAM126A Antibodies) and a predictive candidate for the postoperative recurrence and poorer prognosis of HCC (show FAM126A Antibodies).
study confirmed finding of VIL1 as a diagnostic marker of cervical adenocarcinoma
Competition between tryptophan fluorescence and electron transfer during unfolding of the villin headpiece.
villin severs F-actin to ensure microvillus depolarization and enterocyte remodeling upon intestinal injury
Villin-Cre(+);Klf4 (show KLF4 Antibodies)(fl/fl (show FLT3LG Antibodies)) have greater susceptibility to chemical-induced gastric carcinogenesis and increased rates of gastric tumor progression than control mice.
The data establish that meprins interact with and cleave villin and actin, and these cytoskeletal proteins are substrates for meprins.
a lack of villin does not significantly alter basal and secretagogue-stimulated electrolyte movements across the epithelium of the mouse jejunum in vivo
These results indicate that an important patterning event involving villin expression occurs in the gut (show GUSB Antibodies) epithelium at 16 days, which may define the epithelial boundary between stomach and intestine.
different regulatory sequences of the villin gene regulate expression in the intestinal epithelium
Data show that villin, characteristic markers of brush borders, become abnormally distributed along these atypical basolateral membranes in gal3 (show LGALS3 Antibodies)(-/-) mice.
Villin is an actin regulatory protein that organizes, integrates and regulates multiple epithelial cell functions.
VLN1 does not protect individual actin filaments from severing by VLN3.
This gene encodes a member of a family of calcium-regulated actin-binding proteins. This protein represents a dominant part of the brush border cytoskeleton which functions in the capping, severing, and bundling of actin filaments. Two mRNAs of 2.7 kb and 3.5 kb have been observed\; they result from utilization of alternate poly-adenylation signals present in the terminal exon.