Antibody data
- Antibody Data
- Antigen structure
- References [10]
- Comments [0]
- Validations [0]
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- Product number
- ABIN112306 - Provider product page
- Provider
- antibodies-online
- Product name
- anti-Vimentin (VIM) antibody
- Antibody type
- Monoclonal
- Description
- Protein A Affinity Chromatography.
- Reactivity
- Human, Bovine, Chicken/Avian, Simian
- Host
- Mouse
- Isotype
- IgG
- Antibody clone number
- VIM 3B4
- Vial size
- 50 μg
- Storage
- Prior to and following reconstitution store the antibody undiluted at 2-8°C. DO NOT FREEZE!
- Handling
- This product is photosensitive and should be protected from light
Submitted references Molecular characterization of desmosomes in meningiomas and arachnoidal tissue.
De novo formation of desmosomes in cultured cells upon transfection of genes encoding specific desmosomal components.
Mice devoid of the glial fibrillary acidic protein develop normally and are susceptible to scrapie prions.
Truncation mutagenesis of the non-alpha-helical carboxyterminal tail domain of vimentin reveals contributions to cellular localization but not to filament assembly.
Temperature-sensitive intermediate filament assembly. Alternative structures of Xenopus laevis vimentin in vitro and in vivo.
Species-specific recognition patterns of monoclonal antibodies directed against vimentin.
Identification of a nonapeptide motif in the vimentin head domain involved in intermediate filament assembly.
Distribution of intermediate-filament proteins in the human enamel organ: unusually complex pattern of coexpression of cytokeratin polypeptides and vimentin.
Expression of intermediate filament proteins during development of Xenopus laevis. I. cDNA clones encoding different forms of vimentin.
Patterns of expression of trichocytic and epithelial cytokeratins in mammalian tissues. I. Human and bovine hair follicles.
Akat K, Mennel HD, Kremer P, Gassler N, Bleck CK, Kartenbeck J
Acta neuropathologica 2003 Oct;106(4):337-47
Acta neuropathologica 2003 Oct;106(4):337-47
De novo formation of desmosomes in cultured cells upon transfection of genes encoding specific desmosomal components.
Koeser J, Troyanovsky SM, Grund C, Franke WW
Experimental cell research 2003 Apr 15;285(1):114-30
Experimental cell research 2003 Apr 15;285(1):114-30
Mice devoid of the glial fibrillary acidic protein develop normally and are susceptible to scrapie prions.
Gomi H, Yokoyama T, Fujimoto K, Ikeda T, Katoh A, Itoh T, Itohara S
Neuron 1995 Jan;14(1):29-41
Neuron 1995 Jan;14(1):29-41
Truncation mutagenesis of the non-alpha-helical carboxyterminal tail domain of vimentin reveals contributions to cellular localization but not to filament assembly.
Rogers KR, Eckelt A, Nimmrich V, Janssen KP, Schliwa M, Herrmann H, Franke WW
European journal of cell biology 1995 Feb;66(2):136-50
European journal of cell biology 1995 Feb;66(2):136-50
Temperature-sensitive intermediate filament assembly. Alternative structures of Xenopus laevis vimentin in vitro and in vivo.
Herrmann H, Eckelt A, Brettel M, Grund C, Franke WW
Journal of molecular biology 1993 Nov 5;234(1):99-113
Journal of molecular biology 1993 Nov 5;234(1):99-113
Species-specific recognition patterns of monoclonal antibodies directed against vimentin.
Bohn W, Wiegers W, Beuttenmüller M, Traub P
Experimental cell research 1992 Jul;201(1):1-7
Experimental cell research 1992 Jul;201(1):1-7
Identification of a nonapeptide motif in the vimentin head domain involved in intermediate filament assembly.
Herrmann H, Hofmann I, Franke WW
Journal of molecular biology 1992 Feb 5;223(3):637-50
Journal of molecular biology 1992 Feb 5;223(3):637-50
Distribution of intermediate-filament proteins in the human enamel organ: unusually complex pattern of coexpression of cytokeratin polypeptides and vimentin.
Kasper M, Karsten U, Stosiek P, Moll R
Differentiation; research in biological diversity 1989 Jun;40(3):207-14
Differentiation; research in biological diversity 1989 Jun;40(3):207-14
Expression of intermediate filament proteins during development of Xenopus laevis. I. cDNA clones encoding different forms of vimentin.
Herrmann H, Fouquet B, Franke WW
Development (Cambridge, England) 1989 Feb;105(2):279-98
Development (Cambridge, England) 1989 Feb;105(2):279-98
Patterns of expression of trichocytic and epithelial cytokeratins in mammalian tissues. I. Human and bovine hair follicles.
Heid HW, Moll I, Franke WW
Differentiation; research in biological diversity 1988;37(2):137-57
Differentiation; research in biological diversity 1988;37(2):137-57
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