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anti-Vimentin mouse monoclonal, VIM 3B4

Excellent marker for mesenchymal cells and mesenchyme-derived tumors (sarcoma, lymphoma, melanoma). The antibody is highly specific for the intermediate filament protein vimentin present in all cells of mesenchymal origin. Most avid mab to vimentin.

Mouse monoclonal anti- Vimentin antibody.

Delivery Time: usually 1-7 working days

€139.00
Excl. 19% Tax, excl. Shipping Cost

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Additional Information

Additional Information

Cat. No. 65013
Antibody Type monoclonal
Suitable for ICC, IHC, WB / frozen sections, paraffin (protease)
Clone VIM 3B4
Dilution Dilution for IHC: prediluted
Host mouse
Quantity 5 mL
Species / Reactive with amphibia, bovine, chicken, human, monkey (inquire for murine cross-reaction)
Isotype IgG2a
Presentation prediluted, purified

Product Description

Details

Mouse monoclonal anti- Vimentin antibody.

Reference

Reference

  • Heid HW, Moll I, Franke WW: Patterns of expression of trichocytic and epithelial cytokeratins in mammalian tissues I: Human and bovine hair follicles. Differentiation 37, 137-157 (1988) 
  • Herrmann H, Fouquet B, Franke WW: Expression of intermediate filament proteins during development of Xenopus laevis. I. cDNA clones encoding different forms of vimentin. Development 105, 279-298 (1989) 
  • Kasper M, Karsten U, Stosiek P, Moll R: Distribution of intermediate-filament proteins in the human enamel organ: Unusually complex pattern of coexpression of cytokeratin polypeptides and vimentin. Differentiation 40, 207-214 (1989) 
  • Gomi H, Yokoyama T, Fujimoto K, Ikeda T, Katoh A, Itoh T, Itohara S: Mice Devoid of the Glial Fibrillary Acidic Protein Develop Normally and Are Susceptible to Scrapie Prions. Neuron, 14, 29-41 (1995) 
  • Herrmann H, Eckelt A, Brettel M, Grund C, Franke WW: Temperature-sensitive intermediate filament assembly. Alternative structures of Xenopus laevis vimentin in vitro and in vivo. J Mol Biol 234: 99-113 (1993). 
  • Rogers KR, Eckelt A, Nimmrich V, Janssen K-P, Schliwa M, Herrmann H, Franke WW: Truncation mutagenesis of the non-α-helical carboxyterminal tail domain of vimentin reveals contributions to cellular localization but not to filament assembly. Eur J Cell Biol 66: 136-150 (1995). 
  • Bohn W, Wiegers W, Beuttenmüller M, Traub P: Species-specific recognition patterns of monoclonal antibodies directed against vimentin. Exp Cell Res 201: 1-7 (1992). 
  • Herrmann H, Hofmann I, Franke WW: Identification of a nonapeptide motif in the filament head domain involved in intermediate filament assembly. J Mol Biol 223: 637-650 (1992). Koeser J, Troyanovsky SM, Grund C, Franke WW: De novo formation of desmosomes in cultured cells upon transfection of genes encoding specific desmosomal components. Exp Cell Res 285, 114-130 (2003). 
  • Akat K, Mennel H-D, Kremer P, Gassler N, Bleck CKE, Kartenbeck J: Molecular characterization of desmosomes in meningiomas and arachnoidal tissue. Acta Neuropathol 106, 337-347 (2003) 
  • Moll R, Holzhausen H-J, Mennel H-D, Kuhn C, Baumann R, Taege C, Franke WW : The cardiac isoform of alpha-actin in regenerating and atrophic skeletal muscle, myopathies and rhabdomyomatous tumors: an immunohistochemical study using monoclonal antibodies. Virchows Arch 449(2), 175-191(2006)

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