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Phosphorylation of the substrates was detected by Western blot analysis using phospho-specific antibodies.
In the current study, western blot analysis using phospho-specific antibodies confirmed that expression of p-PDGFR-β, p-PI3K and p-Akt were significantly decreased with the downregulation of uPAR and cathepsin B in both U251 and 5310 cells.
The amount of phosphorylated substrate was determined by western blot analysis using phospho-specific antibodies.
Functional activation of PI3K-PDK1-AKT pathwas was evaluated by western blot analysis, using phospho-specific antibodies.
Western blot analysis using phospho-specific anti-JAKs, STATs and MAPKs antibodies was performed with an ECL Western blotting kit (Amersham, Little Chalfont, UK).
To investigate whether IP3/IP3R pathway affects GJ permeability by mediating the Cx43 phosphorylation, the relative abundance of pS262, pS368, and pS279/282 was analyzed by western blot analysis using phospho-specific antibodies.
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were subject to immunoblot analysis using phospho-specific anti-GSK antibodies to detect translocated SopB-GSK.
The ability of VEGF to induce MAPK phosphorylation was assessed by immunoblot analysis using phospho-specific antibodies.
This indeed is what we observed by performing Western blot analysis using a phospho-specific antibody against MEK1 Ser-217/221 (which was not present on the Kinexus KPSS7.0 panel) (Figs 4C and 5A).
Western blot analysis using either the phospho-specific antibody (anti-phospho-Rh2b) or anti-GST antibody (as a loading control) confirmed Ser phosphorylation and the phosphorylation specificity of the anti-phospho-Rh2b antibody.
As previous studies had shown that PKC-dependent phosphoylation of the serin368 residue of Cx43 is associated with a functional change of Cx43 channels from the open to the closed state [37], [49], we next studied Cx43-serine368 phosphorylation status by Western blot analysis using a serin368 phospho-specific antibody for Cx43.
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