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anti-Vimentin FITC mouse monoclonal, VIM 3B4

The mouse monoclonal anti- Vimentin FITC antibody is an excellent marker for mesenchymal cells and mesenchyme-derived tumors (sarcoma, lymphoma, melanoma).

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€262.00
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Additional Information

Additional Information

Cat. No. 61413
Antibody Type monoclonal
Suitable for Flow Cytometry, ICC, IF, IHC / frozen sections, paraffin sections
Clone VIM 3B4
Dilution Dilution: 1:10
Host mouse
Quantity 250 µL
Species / Reactive with amphibia, bovine, chicken, human, monkey (inquire for murine cross-reaction)
Synonym VIM, VIM3B4
Isotype IgG2a
Presentation FITC Conjugate

Product Description

Details

Mouse monoclonal anti- Vimentin FITC 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, Stosiek P, van Muijen GNP, Moll R: Cell type heterogeneity of intermediate filament expression in epithelia of the human pituitary gland. Histochemistry 93, 93-103 (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)

Moll I and Moll R: Comparative cytokeratin analysis of sweat gland ducts and eccrine poromas. Arch Dermatol Res 283, 300-309 (1991).

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)

Demirkesen C, Hoede N, Moll R: Epithelial markers and differentiation in adnexal neoplasms of the skin: an immunohistochemical study including individual cytokeratins. J Cutan Pathol 22: 518-535 (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-a-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).

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