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|Application / Reactivity||Fish||Amphibian|
|Immunohistochemistry (IHC)||1 Antibodies|
|Immunohistochemistry (Frozen Sections) (IHC (fro))||1 Antibodies||4 Antibodies|
|Western Blotting (WB)||2 Antibodies||3 Antibodies|
|Enzyme Immunoassay (EIA)||3 Antibodies|
|Flow Cytometry (FACS)||2 Antibodies|
|Immunofluorescence (IF)||2 Antibodies|
|Immunohistochemistry (Paraffin-embedded Sections) (IHC (p))||3 Antibodies|
|Antigen||Vimentin (VIM) Antibodies|
|Reactivity||Amphibian, Fish Alternatives|
|Conjugate||This Vimentin antibody is un-conjugated Alternatives|
Immunohistochemistry (Frozen Sections) (IHC (fro)), Western Blotting (WB)
|4 references available|
|Supplier||Log in to see|
Product Details anti-Vimentin AntibodyTarget Details Vimentin Application Details Handling References for anti-Vimentin Antibody (ABIN126716) Images
|Immunogen||Vimentin from cytoskeletal fraction of XLKE cells (cultured Xenopus laevis kidney epithelial cells).|
Target Details VimentinProduct Details anti-Vimentin Antibody Application Details Handling References for anti-Vimentin Antibody (ABIN126716) Images back to top
|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|
|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 (ABIN126716) Images back to top
Immunohistochemistry on Frozen Sections. Western blotting. Immunoelectron Microscopy. Dilution buffer: 0.15 M PBS with 0.1 % BSA and 0.09 % Sodium Azide. Working Diutions: Ready-to-use for Immunohistochemistry.
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 (ABIN126716) Images back to top
|Buffer||0.09 % Sodium Azide|
|Precaution of Use||This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.|
|Storage Comment||Store the antibody undiluted at 2-8 °C.|
References for anti-Vimentin Antibody (ABIN126716)Product Details anti-Vimentin Antibody Target Details Vimentin Application Details Handling Images back to top
Rungger-Bra: "Retinal patterning by Pax6-dependent cell adhesion molecules." in: Developmental neurobiology, Vol. 70, Issue 11, pp. 764-80, 2010 (PubMed).
Zirwes, Kouzmenko, Peters et al.: "Topogenesis of a nucleolar protein: determination of molecular segments directing nucleolar association." in: Molecular biology of the cell, Vol. 8, Issue 2, pp. 231-48, 1997 (PubMed).
Herrmann, Munick, Brettel et al.: "Vimentin in a cold-water fish, the rainbow trout: highly conserved primary structure but unique assembly properties." in: Journal of cell science, Vol. 109 ( Pt 3), pp. 569-78, 1997 (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).