Epitope mapped
Frequently used
Diagnostic marker

anti-Vimentin mouse monoclonal, VIM 3B4, liquid, purified, small






Cat. No: 690013S

Available, delivery time 1-7 days


Key Features
  • Purified, liquid, small
  • Mouse monoclonal
  • Suitable for ELISA, ICC/IF, IHC and WB
  • Reacts with amphibia, bovine, chicken, human and monkey
  • Isotype: IgG2a
Product description
Quantity 200 µl
Antibody Type Monoclonal
Host Mouse
Isotype IgG2a kappa
Conjugate Unconjugated
Purification Affinity chromatography
Reactivity Amphibia, Bovine, Chicken, Human, Monkey
Storage Short term at 2-8°C; long term storage in aliquots at -20°C; avoid freeze/thaw cycles
Intended use Research use only
Clone VIM 3B4
Immunogen Vimentin purified from bovine lens
Concentration 50 µg/ml
Formulation 0.09% sodium azide, 0.5% BSA in PBS buffer, pH 7.4
UniprotID P48616 (Bovine), P09654 (Chicken), P08670 (Human)
Synonym Vimentin, VIM
Tested applications Tested dilutions
Immunocytochemistry (ICC)/ Immunofluorescence (IF) Assay dependent
Immunohistochemistry (IHC) - frozen 1:100-1:200
Immunohistochemistry (IHC) - paraffin 1:100-1:200 (protease treatment and/or microwave treatment recommended)
ELISA Assay dependent
Western Blot (WB) 1:500

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: 57 kDa 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).

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).
Rogers KR, Eckelt A, Nimmrich V, Janssen K-P, Schliwa M, Herrmann H, Franke WW: 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: 136-150 (1995).

References/Publications (21)
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