Product Name
Anti-Vimentin antibody produced in rabbit, affinity isolated antibody
biological source
rabbit
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen 53 kDa
species reactivity
human, rat, mouse
concentration
~1 mg/mL
technique(s)
ELISA: 1:10000
immunohistochemistry: 1:50-1:100
western blot: 1:500-1:1000
NCBI accession no.
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
unmodified
Quality Level
Gene Information
human ... VIM(7431)
Application
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Immunocytochemistry (1 paper)
Immunocytochemistry (1 paper)
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.
Features and Benefits
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General description
Anti-Vimentin Antibody detects endogenous levels of total Vimentin protein.
Immunogen
The antiserum was produced against synthesized peptide derived from human Vimentin.
Immunogen Range: 411-460
Immunogen Range: 411-460
Physical form
Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
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Storage Class
10 - Combustible liquids
wgk
nwg
flash_point_f
Not applicable
flash_point_c
Not applicable
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Nurdan Özkucur et al.
Brain and behavior, 5(1), 24-38 (2015-02-28)
The disruption of neuron arrangement is associated with several pathologies. In contrast to action potentials, the role of resting potential (Vmem) in regulating connectivity remains unknown. Neuron assemblies were quantified when their Vmem was depolarized using ivermectin (Ivm), a drug
Richard A Lasher et al.
Journal of tissue engineering, 3(1), 2041731412455354-2041731412455354 (2012-08-25)
Quantifying structural features of native myocardium in engineered tissue is essential for creating functional tissue that can serve as a surrogate for in vitro testing or the eventual replacement of diseased or injured myocardium. We applied three-dimensional confocal imaging and
Krizelle Mae M Alcantara et al.
Oncology reports, 41(4), 2103-2116 (2019-03-01)
Inactivation of the tumor suppressor protein Merlin leads to the development of benign nervous system tumors in neurofibromatosis type2 (NF2). Documented causes of Merlin inactivation include deleterious mutations in the encoding neurofibromin2 gene (NF2) and aberrant Merlin phosphorylation leading to
Ingrid Jurickova et al.
Inflammatory bowel diseases, 28(7), 988-1003 (2022-03-09)
Perturbagen analysis of Crohn's disease (CD) ileal gene expression data identified small molecules including eicosatetraynoic acid (ETYA), which may exert an antifibrotic effect. We developed a patient-specific human intestinal organoid (HIO) model system to test small molecule regulation of mitochondrial
Heping Lin et al.
Oncology letters, 16(2), 1809-1814 (2018-07-17)
The long noncoding RNA (lncRNA) colon cancer-associated transcript 1 (CCAT1) has been identified as an oncogene in multiple types of human malignancy, and the aberrant expression of CCAT1 has been associated with the tumorigenesis and progression of cancer. However, the
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