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Product Includes Quantity Applications Reactivity MW(kDa) Isotype
Phospho-Vimentin (Ser56) Antibody 3877 1 x 40 µl
H M R Mk 57 Rabbit 
Phospho-Vimentin (Ser83) Antibody 3878 1 x 40 µl
H M R Mk 57 Rabbit 
Anti-rabbit IgG, HRP-linked Antibody 7074 x 100 µl
All Goat 
Vimentin (D21H3) XP® Rabbit mAb 5741 1 x 40 µl
H M R Mk 57 Rabbit IgG

Product Description

The Vimentin Antibody Sampler Kit provides an economical means to detect total levels of vimentin, vimentin phosphorylated at Ser56, and vimentin phosphorylated at Ser82. The kit contains enough primary and secondary antibody to perform four western blot experiments.


Specificity / Sensitivity

The antibodies in the Vimentin Antibody Sampler Kit detect endogenous levels of total vimetin protein, vimentin only when phosphorylated at Ser56, and when phosporylated at Ser82, respectively.


Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ser56, or Ser82 of human vimentin, respectively. Antibodies are purified by Protein A and peptide affinity chromatography. Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Arg45 of human vimentin protein.

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).

During mitosis, CDK1 phosphorylates vimentin at Ser56. This phosphorylation provides a PLK binding site for vimentin-PLK interaction. PLK further phosphorylates vimentin at Ser82, which might serve as memory phosphorylation site and play a regulatory role in vimentin filament disassembly (8,9). Additionally, studies using various soft-tissue sarcoma cells have shown that phosphorylation of vimentin at Ser39 by Akt1 enhances cell migration and survival, suggesting that vimentin could be a potential target for soft-tissue sarcoma targeted therapy (10,11).


1.  Eng, L.F. et al. (2000) Neurochem Res 25, 1439-51.

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, 133-41.

5.  Tang, D.D. et al. (2005) Biochem J 388, 773-83.

6.  Fomina, I.G. et al. (1990) Klin Med (Mosk) 68, 125-7.

7.  Nieminen, M. et al. (2006) Nat Cell Biol 8, 156-62.

8.  Yamaguchi, T. et al. (2005) J Cell Biol 171, 431-6.

9.  Oguri, T. et al. (2006) Genes Cells 11, 531-40.

10.  Zhu, Q.S. et al. (2011) Oncogene 30, 457-70.

11.  Xue, G. and Hemmings, B.A. (2013) J Natl Cancer Inst 105, 393-404.


Entrez-Gene Id 7431
Swiss-Prot Acc. P08670


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