Product nameAnti-MNK1 antibody
See all MNK1 primary antibodies
DescriptionRabbit polyclonal to MNK1
Tested applicationsSuitable for: WB, ELISAmore details
Species reactivityReacts with: Mouse, Human
Predicted to work with: Rat
Synthetic non-phosphopeptide derived from human MNK1 around the phosphorylation site of threonine 255 (L-T-TP-P-C).
- 3T3 cell extracts.
Storage instructionsShipped at 4°C. Store at -20°C. Stable for 12 months at -20°C.
Storage bufferpH: 7.40
Preservative: 0.02% Sodium azide
Constituents: PBS, 50% Glycerol, 0.87% Sodium chloride
Without Mg2+ and Ca2+
Concentration information loading...
PurityImmunogen affinity purified
Our Abpromise guarantee covers the use of ab79365 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|WB||1/500 - 1/1000. Detects a band of approximately 51 kDa (predicted molecular weight: 51 kDa).|
FunctionMay play a role in the response to environmental stress and cytokines. Appears to regulate transcription by phosphorylating EIF4E, thus increasing the affinity of this protein for the 7-methylguanosine-containing mRNA cap.
Sequence similaritiesBelongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family.
Contains 1 protein kinase domain.
modificationsDual phosphorylation of Thr-250 and Thr-255 activates the kinase. Phosphorylation of Thr-385 activates the kinase.
Cellular localizationCytoplasm and Cytoplasm. Nucleus.
- Information by UniProt
- MAP kinase interacting kinase 1 antibody
- MAP kinase interacting serine/threonine kinase 1 antibody
- MAP kinase signal integrating kinase 1 antibody
All lanes : Anti-MNK1 antibody (ab79365) at 1/500 dilution
Lane 1 : 3T3 cell extracts
Lane 2 : 3T3 cell extracts with immunising peptide at 10 µg
Lysates/proteins at 30 µg per lane.
Predicted band size: 51 kDa
Observed band size: 51 kDa
Additional bands at: 27 kDa. We are unsure as to the identity of these extra bands.
ab79365 has not yet been referenced specifically in any publications.