Phospho-Vimentin (Ser83) (D5A2D) Rabbit mAb #12569
- WB
- IF
- F
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 57 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IF-Immunofluorescence
- F-Flow Cytometry
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunofluorescence (Immunocytochemistry) | 1:100 |
| Flow Cytometry (Fixed/Permeabilized) | 1:200 |
Storage
Protocol
Specificity / Sensitivity
Species Reactivity:
The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.
Species predicted to react based on 100% sequence homology:
Source / Purification
Background
During mitosis, CDK1 phosphorylates vimentin at Ser56. This phosphorylation provides a PLK binding site for vimentin-PLK interaction. PLK further phosphorylates vimentin at Ser83, 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).
CDK1 phosphorylates vimentin at Ser56 during mitosis, providing a PLK binding site for vimentin-PLK interaction. PLK further phosphorylates vimentin at Ser83, which might serve as a memory phosphorylation site and play a regulatory role in vimentin filament disassembly (8,9).
- Eng, L.F. et al. (2000) Neurochem Res 25, 1439-51.
- 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, 133-41.
- Tang, D.D. et al. (2005) Biochem J 388, 773-83.
- Fomina, I.G. et al. (1990) Klin Med (Mosk) 68, 125-7.
- Nieminen, M. et al. (2006) Nat Cell Biol 8, 156-62.
- Yamaguchi, T. et al. (2005) J Cell Biol 171, 431-6.
- Oguri, T. et al. (2006) Genes Cells 11, 531-40.
- Zhu, Q.S. et al. (2011) Oncogene 30, 457-70.
- Xue, G. and Hemmings, B.A. (2013) J Natl Cancer Inst 105, 393-404.
- Yamaguchi, T. et al. (2005) J Cell Biol 171, 431-6.
- Oguri, T. et al. (2006) Genes Cells 11, 531-40.
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