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|Application / Reactivity||Human||Chicken||Amphibian||Cow (Bovine)||Monkey|
|Western Blotting (WB)||445 Antibodies||33 Antibodies||3 Antibodies||41 Antibodies||20 Antibodies|
|Transfected Cell Culture (TCC)||1 Antibodies|
|Proximity Ligation Assay (PLA)||1 Antibodies|
|Luminex Assay (LMNX)||8 Antibodies|
|Intracellular Staining (ICS)||3 Antibodies|
|Immunoprecipitation (IP)||42 Antibodies||8 Antibodies||1 Antibodies|
|Immunohistochemistry (Paraffin-embedded Sections) (IHC (p))||133 Antibodies||20 Antibodies||3 Antibodies||18 Antibodies||7 Antibodies|
|Immunohistochemistry (IHC)||223 Antibodies|
|Antigen||Vimentin (VIM) Antibodies|
|Reactivity||Amphibian, Chicken, Cow (Bovine), Human, Monkey Alternatives|
|Conjugate||This Vimentin antibody is conjugated to Biotin Alternatives|
Enzyme Immunoassay (EIA), Flow Cytometry (FACS), Immunohistochemistry (Frozen Sections) (IHC (fro)), Immunohistochemistry (Paraffin-embedded Sections) (IHC (p))
|12 references available|
|Supplier||Log in to see|
Product Details anti-Vimentin AntibodyTarget Details Vimentin Application Details Handling References for anti-Vimentin Antibody (ABIN112307) Images
|Specificity||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).|
|Cross-Reactivity (Details)||Species reactivity (tested):Human, Monkey, Bovine, Dog, Chicken, Amphibia (eg. Xenopus leavis).|
|Purification||Protein A affinity chromatography|
|Immunogen||Vimentin (purified from bovine lens).|
Target Details VimentinProduct Details anti-Vimentin Antibody Application Details Handling References for anti-Vimentin Antibody (ABIN112307) Images back to top
|Alternative Name||Vimentin (VIM Antibody Abstract)|
|Background||Vimentin (57 kDa) is the intermediate filament protein (IFP) of mesenchymal cells. This IFP however often deviates from the tissue-specific and developmentally regulated pattern of expression. Besides its typical expression in most cultured cells, vimentin is also expressed together with several other IFPs during early stages of development. As differentiation proceeds, vimentin is exchanged for the tissue-specific intermediate filament type. Also in cancers, vimentin is often expressed in addition to the tissue-specific IFP.Synonyms: VIM|
|Research Area||Lineage Markers, Cytoskeleton, Neural Stem Cell marker, Cell/Tissue Markers|
|Pathways||TCR Signaling, Caspase Cascade in Apoptosis|
Application DetailsProduct Details anti-Vimentin Antibody Target Details Vimentin Handling References for anti-Vimentin Antibody (ABIN112307) Images back to top
ELISA. FACS. Cell sorting. Immunohistochemistry on frozen sections: 1: 10. Immunohistochemsitry on paraffin sections: 1: 10, 1 h at RT, protease pretreatmen t isrequired prior to antibody application.
Other applications not tested.
Optimal dilutions are dependent on conditions and should be determined by the user.
|Restrictions||For Research Use only|
HandlingProduct Details anti-Vimentin Antibody Target Details Vimentin Application Details References for anti-Vimentin Antibody (ABIN112307) Images back to top
|Buffer||PBS, pH 7.4|
|Storage Comment||Store the antibody undiluted at 2-8 °C.|
References for anti-Vimentin Antibody (ABIN112307)Product Details anti-Vimentin Antibody Target Details Vimentin Application Details Handling Images back to top
Koeser, Troyanovsky, Grund et al.: "De novo formation of desmosomes in cultured cells upon transfection of genes encoding specific desmosomal components." in: Experimental cell research, Vol. 285, Issue 1, pp. 114-30, 2003 (PubMed).
Demirkesen, Hoede, Moll: "Epithelial markers and differentiation in adnexal neoplasms of the skin: an immunohistochemical study including individual cytokeratins." in: Journal of cutaneous pathology, Vol. 22, Issue 6, pp. 518-35, 1996 (PubMed).
Herrmann, Eckelt, Brettel et al.: "Temperature-sensitive intermediate filament assembly. Alternative structures of Xenopus laevis vimentin in vitro and in vivo." in: Journal of molecular biology, Vol. 234, Issue 1, pp. 99-113, 1993 (PubMed).
Gomi, Yokoyama, Fujimoto et al.: "Mice devoid of the glial fibrillary acidic protein develop normally and are susceptible to scrapie prions." in: Neuron, Vol. 14, Issue 1, pp. 29-41, 1995 (PubMed).
Rogers, Eckelt, Nimmrich et al.: "Truncation mutagenesis of the non-alpha-helical carboxyterminal tail domain of vimentin reveals contributions to cellular localization but not to filament assembly." in: European journal of cell biology, Vol. 66, Issue 2, pp. 136-50, 1995 (PubMed).
Kasper, Stosiek, van Muijen et al.: "Cell type heterogeneity of intermediate filament expression in epithelia of the human pituitary gland." in: Histochemistry, Vol. 93, Issue 1, pp. 93-103, 1990 (PubMed).
Kasper, Karsten, Stosiek et al.: "Distribution of intermediate-filament proteins in the human enamel organ: unusually complex pattern of coexpression of cytokeratin polypeptides and vimentin." in: Differentiation; research in biological diversity, Vol. 40, Issue 3, pp. 207-14, 1989 (PubMed).
Heid, Moll, Franke: "Patterns of expression of trichocytic and epithelial cytokeratins in mammalian tissues. I. Human and bovine hair follicles." in: Differentiation; research in biological diversity, Vol. 37, Issue 2, pp. 137-57, 1988 (PubMed).
Jahn, Fouquet, Rohe et al.: "Cytokeratins in certain endothelial and smooth muscle cells of two taxonomically distant vertebrate species, Xenopus laevis and man." in: Differentiation; research in biological diversity, Vol. 36, Issue 3, pp. 234-54, 1988 (PubMed).
Moll, Moll: "Comparative cytokeratin analysis of sweat gland ducts and eccrine poromas." in: Archives of dermatological research, Vol. 283, Issue 5, pp. 300-9, 1991 (PubMed).
Bohn, Wiegers, Beuttenmüller et al.: "Species-specific recognition patterns of monoclonal antibodies directed against vimentin." in: Experimental cell research, Vol. 201, Issue 1, pp. 1-7, 1992 (PubMed).
Herrmann, Hofmann, Franke: "Identification of a nonapeptide motif in the vimentin head domain involved in intermediate filament assembly." in: Journal of molecular biology, Vol. 223, Issue 3, pp. 637-50, 1992 (PubMed).