Cell Signaling Technology

Product Pathways - Cytoskeletal Signaling

Phospho-Vimentin (Ser83) Antibody #3878


No. Size Price
3878S 100 µl ( 10 western blots ) ¥4,050.00 现货查询 购买询价 防伪查询
3878T 20 µl ( 2 western blots ) ¥1,500.00 现货查询 购买询价 防伪查询
3878 carrier free & custom formulation / quantityemail request
Applications Dilution Species-Reactivity Sensitivity MW (kDa) Isotype
W 1:1000 Human,Mouse,Rat,Monkey, Endogenous 57 Rabbit

Species cross-reactivity is determined by western blot.

Applications Key: W=Western Blotting,

Specificity / Sensitivity

Phospho-Vimentin (Ser82) Antibody detects endogenous levels of vimentin only when phosphorylated at Ser82.

Phospho-Vimentin (Ser82) Antibody检测仅在Ser82位点磷酸化的内源性vimentin蛋白。

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser82 of human vimentin. Antibodies are purified by peptide affinity chromatography.


Western blot analysis of extracts from HeLa cells, untreated or phosphorylated in vitro by PLK, using Phospho-Vimentin (Ser82) Antibody (upper). β-Actin Antibody #4976 (lower) was used as a loading control.

使用Phospho-Vimentin (Ser82) Antibody (上图),免疫印迹(Western Blot)分析HeLa细胞中Phospho-Vimentin (Ser82)蛋白水平,细胞分为未处理和PLK激酶体外刺激。β-Actin Antibody #4967被使用作为内参照(下图)。


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). 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).

细胞骨架由三种细胞基质纤维组成:微丝(actin filaments)、中间纤维和微管。中间纤维的主要类型是有区别的,且它在特别的细胞中表达:细胞角蛋白(epithelial细胞)、胶质原纤维酸性蛋白 或GFAP(glial细胞)、desmin (skeletal、viscera和某种vascular smooth muscle 细胞)、波形蛋白(间充质来源)和神经纤维细丝(neurons)。GFAP和vimentin蛋白在星形胶质细胞瘤细胞中形成中间纤维,并且调节它们的活性和形状(1)。尤其,vimentin filaments在早期发育阶段出现,而GFAP filaments是分化的和成熟的大脑星形胶质细胞的特征。因此,GFAP普遍被用作来自星形胶质细胞颅内和椎管内肿瘤上升的标记物 (2)。Vimentin出现在恶性毒瘤中,但不出现癌中,因此相对于其它标记物该蛋白的表达被检测用于区别两种形式的肿瘤(3)。在外界刺激下,Vimentin的动力结构的改变和空间的重组有助于协调不同的信号通路(4)。在平滑肌细胞中血清素刺激下,vimentin蛋白在Ser56位点的磷酸化调节vimentin微丝的结构性布置(5,6)。在淋巴细胞的黏附和迁移期间,vimentin的重塑和其它中间纤维对穿过内皮是起着重要作用(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).


  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.
  12. Yamaguchi, T. et al. (2005) J Cell Biol 171, 431-436.
  13. Oguri, T. et al. (2006) Genes Cells 11, 531-540.

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