Vimentin (FLJ36605, VIM)

Vimentin is an intermediate filament with a molecular weight of ~58kD, and an average diameter of 10 nm. Within the same species, the central domain of the filament is 30% homologous to cytokeratin, desmin, neurofilaments, and glial fibrillary acidic protein. Vimentin is ubiquitously expressed in mesenchymal cells such as fibroblasts, smooth muscle cells, and endothelium. It is usually co-expressed with cytokeratin in some epithelial cells such as Sertoli cells. Vimentin expression may change as a tumor becomes more aggressive, as in the case of hyperplastic prostate where prostatic intraepithelial neoplasia strongly expresses vimentin (91%), but invasive carcinoma is minimally reactive with Mouse anti-Vimentin. Vimentin is useful as part of an antibody panel for differential diagnostic purposes. It may be included in an antibody panel for differentiating soft tissue tumors. For example, co-expression of vimentin and cytokeratin is indicative of epitheloid sarcoma. In one case, a differential antibody panel using vimentin, cytokeratin, CEA, and EMA distinguished reactive mesothelial cells from malignant epithelial cells in the cytodiagnosis of serous effusions in 39/46 cases (85%).\n\nThe binding region of this antibody 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).\n\nApplications:\nSuitable for use in Immunoblot, ELISA, Immunofluorescence microscopy and Immunohistochemistry . Other applications not tested.\n\nRecommended Dilution:\nImmunohistochemistry (frozen and paraffin-embedded tissue and cytological material): 1:100 with PBS, Incubation Time 1 hr at RT; extended with paraffin. Pretreatment with paraffin-embedded sections, protease pretreatment is required prior to antibody application. Optimal dilutions to be determined by the researcher.\n\nPositive Controls: \nCultured RD cells, glioma cells, fibroblasts (SV-80), MDCK. Tumors specifically detected: sarcoma (including myosarcoma), lymphoma, melanoma. \n\nStorage and Stability:\nLyophilized powder may be stored at 4 degrees C for short-term only. Reconstitute to nominal volume by adding sterile 40-50% glycerol and store at -20 degrees C. Reconstituted product is stable for 12 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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SPECIFICATIONS

Catalog Number

V2122-03A

Size

50ug

Applications

ELISA, IF, IHC, WB

Hosts

Mouse

Reactivities

Hum, Bov, Can, Ch/Bird, NHP

Form

Supplied as a lyophilized powder in PBS, pH 7.4, 0.5% BSA, 0.09% sodium azide. Reconstitute to a final volume of 1ml.

P Type

Mab

Purity

Purified by Protein A affinity chromatography.

Isotype

IgG2a

References

Heid HW, Moll I, Franke WW: Patterns of expression of trichocytic and epithelial cytokeratins in mammalian tissues I: Human and bovine hair\nfollicles. Differentiation 37, 137-157 (1988)\nJahn L, Fouquet B, Rohe K, Franke WW: Cytokeratins in certain endothelial and smooth muscle cells of two taxonomically distant vertebrate\nspecies, Xenopus laevis and man. Differentiation 36, 234-254 (1987)\nKasper M, Stosiek P, van Muijen GNP, Moll R: Cell type heterogeneity of intermediate filament expression in epithelia of the human pituitary\ngland. Histochemistry 93, 93-103 (1989)\nKasper M, Karsten U, Stosiek P, Moll R: Distribution of intermediate-filament proteins in the human enamel organ: Unusually complex pattern of\ncoexpression of cytokeratin polypeptides and vimentin. Differentiation 40, 207-214 (1989)\nMoll I and Moll R: Comparative cytokeratin analysis of sweat gland ducts and eccrine poromas. Arch Dermatol Res 283, 300-309 (1991).\nGomi H, Yokoyama T, Fujimoto K, Ikeda T, Katoh A, Itoh T Itohara S: Mice Devoid of the Glial Fibrillary Acidic Protein Develop Normally and Are\nSusceptible to Scrapie Prions. Neuron, 14, 29-41 (1995)\nDemirkesen C, Hoede N, Moll R: Epithelial markers and differentiation in adnexal neoplasms of the skin: an immunohistochemical study\nincluding individual cytokeratins. J Cutan Pathol 22: 518-535 (1995).\nHermann H, Eckelt A, Brettel M, Grund C, Franke WW: Temperature-sensitive intermediate filament assembly. Alternative structures of\nXenopus laevis vimentin in vitro and in vivo. J Mol Biol 234: 99-113 (1993).\nRogers KR, Eckelt A, Nimmrich V, Janssen K-P, Schliwa M, Hermann H, Franke WW: Truncation mutagenesis of the non-a-helical\ncarboxyterminal tail domain of vimentin reveals contributions to cellular localization but not to filament assembly. Eur J Cell Biol 66: 136-150\n(1995).\nBohn W, Wiegers W, Beuttenm

Additional Info

Recognizes the intermediate filament protein vimentin at 57kD, which is present in all cells of mesenchymal origin. Species Crossreactivity: Human, monkey, bovine, canine, chicken, amphibia.