rev:January 17, 2002

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(anti-Human and others as indicated)

RDI Divison of researchd Industries Intl  offers a wide line of  antibodies. Since no one antibody works best for all applications (neutralization, blotting, histochemistry, ELISA, etc), we offer many different types of antibodies to help solve this problem. Please inquire for other applications or types of antibodies not listed below.


cat#RDI-PRO61013    $345.00/vial $312.00/vial 3+

also available  Biotin conjugated:cat#RDI-PRO61513 $470.00/0.25ml

                        FITC conjugated cat#RDI-PRO61413 $406.00/0.25ml

                        guinea pig anti-vimentin cat#RDI-PROGP53 $440.00/0.1ml

CLONE:                      VIM 3B4

ISOTYPE:                   IgG2a

PURIFICATION METHOD: Protein A affinity chromatography

Immunogen: vimentin (purified from bovine lens)

SPECIFICITY: The antibody is highly specific for the intermediate filament protein vimentin which is present in all cells of mesenchymal origin. Clone VIM 3B4 has turned out to be the most avid Mab to vimentin. Polpeptide reacting:Mr 57,000 intermediate filament protein (vimentin) of mesenchymal cells. Tumors specifically detected:sarcoma (including myosarcoma), lymphoma, melanoma.

Reactivities on Cultured Cell lines (tested so far) RD cells, glioma cells, fibroblasts (SV-80), MDCK

Antigen Recognized in  Species (tested so far) Human, monkey, dog, chicken, amphibia, rodent

APPLICATIONS: - Immunoblottig

                               - ELISA

                              - Immunofluorescence microscopy

                             - Immunohistochemistry

                             - Suitable for frozen and paraffin embedded tissue

                               Cytological material

Pretreatment: With paraffin embedded sections, protease pretreatment is required prior to antibody application

Reconstitution: Reconstitute in 1ml Dist. water (final solution contains 0.09% NaN3, 0.5% BSA in PBS buffer, pH 7.4

Working dilution: Dilute at least 1:10 with PBS, pH 7.4 for immunohistochemical application

Stability/Storage: One year after reconstitution when stored at 2-8 DEG C .Recommend aliquoting and store at -20 DEG C. Avoid frequent freeze thaw cycles.

1. Franke, W.W.and Moll, R.: Cytoskeletal components of lymphoid organs. I. Synthesis of cytokeratin 8 and 18 and Desmin in subpopulations of extrafollicular reticulum cells of human lymph nodes, tonsils and spleen. Differentiation 36, 145-163 (1987)

2. Heid, H.W., Moll, I. and Franke, W.W.: Patterns of expression of trichocytic and epithelial cytokeratins in mammalian tissues I: Human and bovine hair follicles. Differentiation 37, 137-157 (1988)

3. Jahn, L., Fouquet, B., Rohe, K. and Franke, W.W.: Cytokeratins in certain endothelial and smooth muscle cells of two taxonomically distant vertebrate species, Xenopus laevis and man. Differentiation 36, 234-254 (1987)

4. Kasper, M., Stosiek, P., van Muijen, G.N.P. and Moll, R.: Cell type heterogeneity of intermediate filament expression in epithelia of the human pituitary gland. Histochemistry 93, 93-103 (1989)

5. Kasper, M., Karsten, U., Stosiek, P., and 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)

6. Moll, I. and Moll, R.: Comparative cytokeratin analysis of sweat gland ducts and eccerine poromas. Arch Dermatol Res 283, 300-309 (1991).Rungger-Brädle, E., Achtstätter, Th and Franke, W.W.: An epithelium-type cytoskeleton in a glial cell: Astrocytes of amphibian optic nerves contain cytokeratin filaments connected desmosomes. J. Cell Biol. 109, 705-716 (1989)

7. Gomi, H., Yokoyama, T., Fujimoto, K., Ikeda, T., Katoh, A., Itoh, T. and Itohara, S.: Mice Devoid of the Glial Fibrillary Acidic Protein Develop Normally and Are Susceptible to Scrapie Prions. Neuron, Vol. 14, 29-41 (1995)

8. 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).

9. Bohn W., Wiegers W., Beuttenmuller M., and Traub P.: Species-specific recognition patterns of monoclonal antibodies directled against vimentin. xp Cell Res 201:1-7 (1992)

10. Hermann H., Hofmann I., Franke W.W.:Identification of a nonapeptide Motiff in the filament head domain involved in intermediate filament assembly. J. Mol. Biol. 223:637-650 (1992)

11. Rogers K.R., Eckelt A., Nimmrich V., Janssen K.-P., Schilwa M., Hermann H., Franke W.W:Truncation mutagenesis of the mon-alpha-helical carboxyterminal tail domain of vimentin reveals contributions to cellular localization but not to filament assembly. Eur. J. Cell Biol. 66:136-150 (1995)

see also our recombinant human Vimentin (pure antigen) cat#RDI-PRO62215 $410.00/100ug

natural bovine lens vimentin (pure antigen) cat#RDI-CBL62011 $500.00/250ug.

For Research Use Only

For research use only. Not supplied for use in human diagnostic or therapeutic procedures

RDI Divison of researchd Industries Intl

San Jose, 95123 CA Snell ave 658


or 408-780-0908

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