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human skin (courtesy of J.Heß, University Hospital Heidelberg) Zoom

human skin (courtesy of J.Heß, University Hospital Heidelberg)

anti-Vimentin mouse monoclonal, VIM 3B4, prediluted, purified

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.
highly_published external_validation
Cat. No.: 65013
Quantity:  5 mL
No. of experiments:  ≤ 100 (IHC, 50 µl/slide)

Delivery Time: usually 1-7 working days

$174.00
Excl. VAT, excl. Shipping Cost

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Specifications

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Product description

Host mouse
Antibody Type monoclonal
Isotype IgG2a
Clone VIM 3B4
Immunogen Vimentin (purified from bovine lens)
Purification protein A affinity chromatography
Conjugate unconjugated
Formulation PBS pH 7.4 with 0.5% BSA and 0.09% sodium azide
Storage short term at 2-8°C; long term storage in aliquots at -20°C; avoid freeze/ thaw cycles
No. of experiments ≤ 100 (IHC, 50 µl/slide)
Intended use Research use only
Tested species reactivity amphibia, bovine, chicken, dog, human, monkey (weaker murine cross-reaction)

Applications

Tested applications Tested dilutions
ELISA assay dependent
Immunocytochemistry (ICC)/ Immunofluorescence (IF) assay dependent
Immunohistochemistry (IHC) - frozen ready-to-use
Immunohistochemistry (IHC) - paraffin ready-to-use (protease treatment and/or microwave treatment recommended)
Western Blot (WB) assay dependent

Background

Details

The antibody is highly specific for the intermediate filament protein vimentin which is present in all cells of mesenchymal origin. VIM 3B4 has turned out to be the most avid mab to vimentin.
Polypeptide reacting: Mr 57 000 intermediate filament protein (vimentin) of mesenchymal cells. Tumors specifically detected: sarcoma (including myosarcoma), lymphoma, melanoma. The binding region of monoclonal antibody VIM3B4 has been characterized by Bohn et al.(1992).
According to these authors, the epitope has been localized on the alpha-helical part of vimentin (rod domain coil 2).
Due to an aa substitution at position of aa 353 in murine vimentin (that could explain for the weak cross-reaction of the antibody with murine vimentin) they were able to narrow down the binding region around position 353.
These findings were confirmed by truncation mutagenesis experiments using human vimentin (Rogers et al., 1995).
Reactivity on cultured cell lines: fibroblasts (SV-80)


Rogers, K. R. et al. Truncation mutagenesis of the non-alpha-helical carboxyterminal tail domain of vimentin reveals contributions to cellular localization but not to filament assembly. Eur. J. Cell Biol. 66, 136–50 (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).

Reference

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