Product Pathways - Cytoskeletal Signaling
Vimentin (D21H3) XP® Rabbit mAb (PE Conjugate) #12020
|F||H M R Mk||Endogenous||57||Rabbit IgG|
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.
Specificity / Sensitivity
Vimentin (D21H3) XP® Rabbit mAb (PE Conjugate) detects endogenous levels of total vimentin protein.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Arg45 of human vimentin protein.
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometry analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated Vimentin (D21H3) XP® Rabbit mAb #5741.
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).
- Eng, L.F. et al. (2000) Neurochem. Res. 25, 1439-1451.
- Goebel, H.H. et al. (1987) Acta Histochem. Suppl. 34, 81-93.
- Leader, M. et al. (1987) Histopathology 11, 63-72.
- Helfand, B.T. et al. (2004) J. Cell Sci. 117, 133-141.
- Tang, D.D. et al. (2005) Biochem. J. 388, 773-783.
- Fomina, I.G. et al. (1990) Klin. Med. (Mosk.) 68, 125-127.
- Nieminen, M. et al. (2006) Nat. Cell Biol. 8, 156-162.
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For Research Use Only. Not For Use In Diagnostic Procedures.