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  • 产品名称：anti-Vimentinantibody(VIM)(FITC)

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  • 产品厂商：Acris-antibodies
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简单介绍：
anti-Vimentinantibody(VIM)(FITC)
详情介绍：
Immunogen Vimentin (purified from Bovine lens)
Clone VIM 3B4
Isotype IgG2a
Specificity This antibody is highly specific for the intermediate filament protein Vimentin. Polypeptide reacting: Mr 57 000 intermediate filament protein (Vimentin) of mesenchymal cells. 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). Clone VIM 3B4 has turned out to be the most avid mab to Vimentin. Tumors Specifically Detected: Sarcoma (including myosarcoma), lymphoma, melanoma. Tested Reactivities on Cultured Cell Lines: RD cells, glioma cells, fibroblasts (SV-80), MDCK.
Cross-Reactivity (Details) Species reactivity (tested):Human, Monkey, Bovine, Dog, Chicken, Amphibian (e.g. Xenopus leavis). Weaker Murine cross-reaction.
Purification Affinity Chromatography on Protein A
Alternative Name Vimentin (VIM Antibody Abstract)
Background Vimentin is an intermediate filament protein which is present in all cells of mesenchymal origin. Vimentin is the major subunit protein of the intermediate filaments of mesenchymal cells. It is believed to be involved with the intracellular transport of proteins between the nucleus and plasma membrane. Vimentin has been implicated to be involved in the rate of steroid synthesis via its role as a storage network for steroidogenic cholesterol containing lipid droplets. Vimentin phosphorylation by a protein kinase causes the breakdown of intermediate filaments and activation of an ATP and myosin light chain dependent contractile event. This results in cytoskeletal changes that facilitate the interaction of the lipid droplets within mitochondria, and subsequent transport of cholesterol to the organelles leading to an increase in steroid synthesis. Immunohistochemical staining for Vimentin is characteristic of sarcomas (of neural, muscle and fibroblast origin) compared to carcinomas which are generally negative. Melanomas, lymphomas and vascular tumors may all stain for Vimentin. Vimentin antibodies are thus of value in the differential diagnosis of undifferentiated neoplasms and malignant tumors. They are generally used with a panel of other antibodies including those recognizing cytokeratins, lymphoid markers, S100, desmin and neurofilaments.Synonyms: VIM
Gene ID 7431
NCBI Accession NP_003371
UniProt P08670
Research Area Lineage Markers, Cytoskeleton, Neural Stem Cell marker, Cell/Tissue Markers
Pathways Caspase Cascade in Apoptosis
Application Notes ELISA. Immunoblotting. Flow Cytometry. Immunofluorescence Microscopy (5-10 μg/mL recommended)Immunohistochemistry (dilute at least 1/10 with PBS, pH 7.4). Suitable for Frozen and Paraffin-Embedded tissue and Cytological Material. Withparaffin-embedded sections, protease pretreatment is required prior to antibodyapplication. Incubation Time: 1 h at RT, extended with paraffin.
Other applications not tested.
Optimal dilutions are dependent on conditions and should be determined by the user.
Restrictions For Research Use only
Format Liquid
Handling Advice Avoid repeated freezing and thawing.
Storage 4 °C/-20 °C
Storage Comment Store undiluted at 2-8 °C for one month or (in aliquots) at -20 °C for longer.
Background publications Koeser, Troyanovsky, Grund, Franke: "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).

Gomi, Yokoyama, Fujimoto, Ikeda, Katoh, Itoh, Itohara: "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, Janssen, Schliwa, Herrmann, Franke: "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).

Herrmann, Eckelt, Brettel, Grund, Franke: "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).

Bohn, Wiegers, Beuttenmüller, Traub: "Species-specific recognition patterns of monoclonal antibodies directed against vimentin." in: Experimental cell research, Vol. 201, Issue 1, pp. 1-7, 1992 (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).

Kasper, Stosiek, van Muijen, Moll: "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, Moll: "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, Franke: "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).