Anti-Phosphorylated Vimentin (Ser55) (Mouse) mAb

  • Applications
    • ELISA
    • ICC
    • WB
  • Target vimentin
  • Host Species Mouse
  • Species Reactivities Human, Mouse, Rat
  • Code # D076-3
  • Size 100 μg
  • Price
    $306.33
Specifications

Background

Vimentin is an intermediate filament protein distributed widely in the cytoplasm and is phosphorylated by several protein kinase in vitro. Ser55 residues on vimentin were reported to be one of the phosphorylation sites of vimentin at metaphase and were the phosphorylation sites for cdc2 kinase but not for cAMP-dependent protein kinase, protein kinase C, and Ca2+-calmodulin-dependent protein kinase II in vitro. Immunofluorescence and immunoelectron microscopy showed that vimentin Ser55 residues distributed in the entire cytoplasmic vimentin filament system are phosphorylated when the cells enter mitosis and de-phosphorylated in cytokinesis. The use of this antibody that specifically reacts with the phosphorylation site of vimentin Ser55 by cdc2 kinase enables estimation of a particular cdc2 kinase function.
  • Antibody Type:
    Monoclonal
  • Application:
    ELISA, ICC, WB
  • Clone Number:
    4A4
  • Concentration:
    1 mg/ml
  • Conjugate:
    Unlabeled
  • Description:
    Monoclonal antibody of 100 μg targeting vimentin for ELISA, ICC, WB.
  • Formulation:
    100 μg IgG in 100 μl volume of PBS containing 50% glycerol, pH 7.2. No preservative iscontained.
  • Gene ID (Human):
  • Gene ID (Mouse):
  • Gene ID (Rat):
  • Host Species:
    Mouse
  • Immunogen:
    MPV55 peptide synthesis, including the Ser55 phosphorylation site of phosphorylation of Mausubimenchin (SLYSS-phosphoS55-PGGAYC-KLH)
  • Isotype:
    IgG2b
  • Product Type:
    Antibody
  • Reactivity:
    This antibody reacts specifically withthe phosphorylated MPV55 peptide but not thenon-phosphorylated peptide. This antibody detectsvimentin phosphorylated by cdc2 kinase and does notdetect non-phosphorylated vimentin or phosphorylatedvimentin by cAMP
  • Research Area:
    Cell Biology
  • Short Description:
    Vimentin Monoclonal Antibody
  • Size:
    100 μg
  • Species Reactivity:
    Human, Mouse, Rat
  • Storage Temperature:
    -20°C
  • Target:
    vimentin
Citations
  1. Chang IA et al. Vimentin phosphorylation by Cdc2 in Schwann cell controls axon growth via β1-integrin activation. FASEB J. 26, 2401-13 (2012),
  2. Englund C et al. Pax6, Tbr2, and Tbr1 are expressed sequentially by radial glia, intermediate progenitor cells, and postmitotic neurons in developing neocortex. J Neurosci. 25, 247-51 (2005),
  3. Fourest-Lieuvin A et al. Microtubule regulation in mitosis: tubulin phosphorylation by the cyclin-dependent kinase Cdk1. Mol Biol Cell. 17, 1041-50 (2006),
  4. Malik S et al. Neurogenesis continues in the third trimester of pregnancy and is suppressed by premature birth. J Neurosci. 33, 411-23 (2013),
  5. Martínez-Cerdeño V et al. N-Myc and GCN5 regulate significantly overlapping transcriptional programs in neural stem cells. PLoS One 7, e39456 (2012),
  6. Minobe S et al. Rac is involved in the interkinetic nuclear migration of cortical progenitor cells. Neurosci Res. 63, 294-301 (2009),
  7. Miyata T et al. Asymmetric production of surface-dividing and non-surface-dividing cortical progenitor cells. Development. 131, 3133-45 (2004),
  8. Shitamukai A et al. Oblique radial glial divisions in the developing mouse neocortex induce self-renewing progenitors outside the germinal zone that resemble primate outer subventricular zone progenitors. J Neurosci. 31, 3683-95 (2011),
  9. Tatsumi Y et al. Deregulation of Cdt1 induces chromosomal damage without rereplication and leads to chromosomal instability. J Cell Sci. 119, 3128-40 (2006),
  10. Tsai J W et al. LIS1 RNA interference blocks neural stem cell division, morphogenesis, and motility at multiple stages. J Cell Biol. 170, 935-45 (2005),
  11. Tsujimura K et al. Visualization and function of vimentin phosphorylation by cdc2 kinase during mitosis. J Biol Chem. 269, 31097-106 (1994)
References
  1. Malik, S., et al., J. Neurosci. 33, 411-423 (2013) [IHC]
  2. Martínez-Cerdeño,V., et al., PLoS One 7, e39456 (2012)[IHC]
  3. Chang,I. A., et al., FASEB J. 26, 2401-2413 (2012)[WB, IC, IHC]
  4. Shitamukai,A., et al., J. Neurosci. 31, 3683-3695 (2011) [IHC]
  5. Minobe, S., et al., Neurosci. Res. 63, 294-301 (2009) [IHC]
  6. Tatsumi, Y., et al., J. Cell Sci. 119, 3128-3140 (2006) [WB]
  7. Fourest-Lieuvin, A., et al., Mol. Biol. Cell17, 1041-1050 (2006)[WB]
  8. Tsai, J. W., et al., J. Cell Biol. 170, 935-945 (2005) [IC]
  9. Englund, C., et al., J. Neurosci. 25, 247-251 (2005) [IHC]
  10. Miyata, T., et al., Development 131, 3133-3145 (2004) [IHC]
  11. Tsujimura, K., et al., J. Biol. Chem. 269, 31097-31106 (1994) [WB, IC, ELISA]