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Rabbit polyclonal to EEF2K (phospho S366)
This antibody detects endogenous levels of EEF2K only when phosphorylated at serine 366.
Predicted to work with:
A synthesized phosphopeptide derived from human EEF2K around the phosphorylation site of serine 366 (T-L-S
Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.
Preservative: 0.02% Sodium azide Constituents: 50% Glycerol, 0.87% Sodium chloride, PBS
Concentration information loading...
Immunogen affinity purified
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific phosphopeptide. The antibody against non-phosphopeptide was removed by chromatography using non-phosphopeptide corresponding to the phosphorylation site.
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in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
1/50 - 1/100.
1/300 - 1/1000. Detects a band of approximately 100 kDa (predicted molecular weight: 95 kDa).
Phosphorylates eukaryotic elongation factor-2. Binds calmodulin.
Belongs to the protein kinase superfamily. Alpha-type protein kinase family.
Contains 1 alpha-type protein kinase domain.
Information by UniProt
Calcium/calmodulin dependent eukaryotic elongation factor 2 antibody
Calcium/calmodulin dependent eukaryotic elongation factor 2 kinase antibody
Western blot - Anti-EEF2K (phospho S366) antibody (ab51227)
All lanes :
Anti-EEF2K (phospho S366) antibody (ab51227) at 1/300 dilution
Lane 1 :
Extracts of Hela cells treated with 10% serum for 15mins.
Lane 2 :
Extracts of Hela cells treated with 10% serum for 15mins and phosphopeptide.
Predicted band size:
Observed band size:
100 kDa (
why is the actual band size different from the predicted?
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-EEF2K (phospho S366) antibody (ab51227)
Immunohistochemical analysis of paraffin-embedded human breast carcinoma using ab51227 (right picture is blocked with the phospho peptide)
has not yet been referenced specifically in any publications.
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