recommended for detection of Ser 83 phosphorylated Vimentin of human origin by WB and ELISA
Modification
Phosphoralated
Modification Notes
Phosphorylation of Vimentin on specific amino acid residues, such as Ser 83 and Ser 71, induces disassembly of Vimentin intermediate filaments in vivo and in vitro. Binding of 14-3-3 depends on Vimentin phosphorylation and requires the phosphopeptide binding domain of 14-3-3, which is an amino terminal head domain consisting of amino acids 1-96. Phosphorylated Vimentin sequesters 14-3-3 and limits its availability to other target proteins, which can affect intracellular signaling processes that require 14-3-3. The amino-terminal domain of Vimentin is the target site for several protein kinases, including Rho kinase and PKC. The disruption of subcellular compartmentalization of interphase cells leads to PKC-mediated phosphorylation of Vimentin. Thus, targeting of activated PKC, coupled with the reorganization of intracellular membranes which contain phospholipids essential for activation, leads to the mitosis-specific phosphorylation of Vimentin.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPELISA
WB:1:500~1:2000 IP:1:100~1:500 Notes:Optimal dilutions/concentrations should be determined by the researcher.
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
recommended for detection of Ser 83 phosphorylated Vimentin of human origin by WB and ELISA
Tissue Specificity
recommended for detection of Ser 83 phosphorylated Vimentin of human origin by WB and ELISA