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anti-Vimentin mouse monoclonal, VIM 3B4, FITC Conjugate

The mouse monoclonal anti- Vimentin FITC antibody is an excellent marker for mesenchymal cells and mesenchyme-derived tumors (sarcoma, lymphoma, melanoma).
Cat. No.: 61413
Quantity:  250 µL
No. of experiments:  ≤ 50 (IHC, 50 µl/slide)

Delivery Time: usually 1-7 working days

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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 FITC
Formulation contains 0.09% sodium azide
Storage store at 2-8°C
UniprotID P48616
No. of experiments ≤ 50 (IHC, 50 µl/slide)
Note centrifuge prior to opening
Intended use Research use only
Tested species reactivity bovine, chicken, dog, human, monkey (weaker murine cross-reaction)


Tested applications Tested dilutions
ELISA assay dependent
Immunocytochemistry (ICC)/ Immunofluorescence (IF) assay dependent
Immunohistochemistry (IHC) - frozen at least 1:10
Immunohistochemistry (IHC) - paraffin at least 1:10 (protease treatment and/or microwave treatment recommended)



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).

Tested 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).


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