Cell Signaling Technology

Product Pathways - Cytoskeletal Signaling

Vimentin (R28) Antibody #3932

Applications Reactivity Sensitivity MW (kDa) Source
W IF-IC H M R Mk Endogenous 57, 50 Rabbit

Applications Key:  W=Western Blotting  IF-IC=Immunofluorescence (Immunocytochemistry)
Reactivity Key:  H=Human  M=Mouse  R=Rat  Mk=Monkey
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

Vimentin (R28) Antibody detects endogenous levels of total vimentin protein.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Arg28 of human vimentin. Antibodies are purified by peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell lines using Vimentin (R28) Antibody.

IF-IC

IF-IC

Confocal immunofluorescent analysis of HeLa cells using Vimentin (R28) Antibody (green). Actin filaments have been labeled with DY-554 phalloidin (red). Blue pseudocolor = DRAQ5® #4084 (fluorescent DNA dye).

Background

The cytoskeleton consists of three types of cytosolic fibers: microfilaments (actin filaments), intermediate filaments, and microtubules. Major types of intermediate filaments are distinguished by their cell-specific expression: cytokeratins (epithelial cells), glial fibrillary acidic protein (GFAP) (glial cells), desmin (skeletal, visceral, and certain vascular smooth muscle cells), vimentin (mesenchyme origin), and neurofilaments (neurons). GFAP and vimentin form intermediate filaments in astroglial cells and modulate their motility and shape (1). In particular, vimentin filaments are present at early developmental stages, while GFAP filaments are characteristic of differentiated and mature brain astrocytes. Thus, GFAP is commonly used as a marker for intracranial and intraspinal tumors arising from astrocytes (2). Research studies have shown that vimentin is present in sarcomas, but not carcinomas, and its expression is examined in conjunction with that of other markers to distinguish between the two (3). Vimentin's dynamic structural changes and spatial re-organization in response to extracellular stimuli help to coordinate various signaling pathways (4). Phosphorylation of vimentin at Ser56 in smooth muscle cells regulates the structural arrangement of vimentin filaments in response to serotonin (5,6). Remodeling of vimentin and other intermediate filaments is important during lymphocyte adhesion and migration through the endothelium (7).

  1. Eng, L.F. et al. (2000) Neurochem. Res. 25, 1439-1451.
  2. Goebel, H.H. et al. (1987) Acta Histochem. Suppl. 34, 81-93.
  3. Leader, M. et al. (1987) Histopathology 11, 63-72.
  4. Helfand, B.T. et al. (2004) J. Cell Sci. 117, 133-141.
  5. Tang, D.D. et al. (2005) Biochem. J. 388, 773-783.
  6. Fomina, I.G. et al. (1990) Klin. Med. (Mosk.) 68, 125-127.
  7. Nieminen, M. et al. (2006) Nat. Cell Biol. 8, 156-162.

Application References

Have you published research involving the use of our products? If so we'd love to hear about it. Please let us know!

Companion Products

For Research Use Only. Not For Use In Diagnostic Procedures.

Products