Get this product for free
Submit your validation data for this product and get a full refund. I want to validate this productRelevance Score | ABIN | Application | Conjugate | Host | Isotype | Epitope | Supplier | Clonality | References | Details |
---|---|---|---|---|---|---|---|---|---|---|
1 | ABIN112308 | EIA FACS IHC (fro) IF IHC (p) WB | FITC | Mouse | IgG2a | Log in to see | VIM 3B4 | 11 | ||
1 | ABIN126716 | IHC (fro) WB | Mouse | IgG1 | Log in to see | XL-VIM-14-13 | 4 |
General |
|
---|---|
Antigen | Vimentin (VIM) Antibodies |
Reactivity | Amphibian, Chicken, Cow (Bovine), Human, Monkey Alternatives |
Host | Mouse Alternatives |
Clonality (Clone) | |
Conjugate | This Vimentin antibody is un-conjugated Alternatives |
Application |
Enzyme Immunoassay (EIA), Immunohistochemistry (Frozen Sections) (IHC (fro)), Immunofluorescence (IF), Immunohistochemistry (Paraffin-embedded Sections) (IHC (p)), Western Blotting (WB)
Alternatives
|
![]() |
10 references available |
Supplier | Log in to see |
Product Details anti-Vimentin AntibodyTarget Details Vimentin Application Details Handling References for anti-Vimentin antibody (ABIN112306) 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). |
Purification | Protein A Affinity Chromatography. |
Immunogen | Vimentin (purified from bovine lens) |
Clone | VIM 3B4 |
Isotype | IgG2a |
Plasmids, Primers & others | |
Target Details VimentinProduct Details anti-Vimentin Antibody Application Details Handling References for anti-Vimentin antibody (ABIN112306) Images back to top |
|
Antigen | |
Alternative Name | Vimentin (VIM Antibody Abstract) |
Background | 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 with 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 |
Pathways | Caspase Cascade in Apoptosis |
Application DetailsProduct Details anti-Vimentin Antibody Target Details Vimentin Handling References for anti-Vimentin antibody (ABIN112306) Images back to top |
|
Application Notes |
Immunoblotting. ELISA. Immunofluorescence Microscopy. Immunohistochemistry on Frozen Sections: 1/100. Immunohistochemistry on Paraffin Sections: 1/100, 1 h at RT, protease pretreatment 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 (ABIN112306) Images back to top |
|
Reconstitution | Restore in 1 mL dist. water |
Buffer | Final Solution contains 0.09 % Sodium Azide as presevative and 0.5 % BSA as stabilizer in PBS, pH 7.4. |
Preservative | Sodium azide |
Precaution of Use | This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only. |
Handling Advice | This product is photosensitive and should be protected from light |
Storage | 4 °C |
Storage Comment | Prior to and following reconstitution store the antibody undiluted at 2-8 °C. DO NOT FREEZE! |
References for anti-Vimentin antibody (ABIN112306)Product Details anti-Vimentin Antibody Target Details Vimentin Application Details Handling Images back to top |
|
Background publications |
Akat, Mennel, Kremer, Gassler, Bleck, Kartenbeck: "Molecular characterization of desmosomes in meningiomas and arachnoidal tissue." in: Acta neuropathologica, Vol. 106, Issue 4, pp. 337-47, 2003 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 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 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 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 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 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 Herrmann, Fouquet, Franke: "Expression of intermediate filament proteins during development of Xenopus laevis. I. cDNA clones encoding different forms of vimentin." in: Development (Cambridge, England), Vol. 105, Issue 2, pp. 279-98, 1989 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 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 |