Anti-Phosphorylated Vimentin (Ser55) (Mouse) mAb

WB - 1-5 ug/mL (chemiluminescence detection system) ICC - 1 ug/mL ELISA - It is reported that this monoclonal antibody can be used for ELISA in the reference number 13).

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.

1 mg/ml

100 ug IgG in 100 ul volume of PBS containing 50% glycerol, pH 7.2. No preservative iscontained.

Human: 7431 Mouse: 22352 Rat: 81818

MPV55 peptide synthesis, including the Ser55 phosphorylation site of phosphorylation of Mausubimenchin (SLYSS-phosphoS55-PGGAYC-KLH)

This antibody reacts specifically with the phosphorylated MPV55 peptide but not the non-phosphorylated peptide. This antibody detects vimentin phosphorylated by cdc2 kinase and does not detect non-phosphorylated vimentin or phosphorylated vimentin by cAMP-dependent kinase, protein kinase C, or Ca2+-calmodulin-dependent protein kinase II on Western blotting.

1 year

This antibody was purified from mouse ascites fluid using protein A agarose. This hybridoma (clone 4A4) was established by fusion of mouse myeloma cell SP2/0-Ag14 with Balb/c mouse splenocyte immunized with the synthetic MPV55 phosphopeptide corresponding to mouse phosphorylated vimentin Ser55 (SLYSS-phosphoS55-PGGAYC-KLH).

vimentin