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EEF2K (Ser-359), Phosphospecific Antibody

CAT: 0498-bs-70469RSize: 100 µLDry Ice: NoHazardous: No
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CAT#:0498-bs-70469RSize:100 µL
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24/48H Stock Items & 2 to 6 Weeks non Stock Items.
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Background
Eukaryotic elongation factor 2 (eEF2) catalyzes the translocation of peptidyl-tRNA from the A site to the P site on the ribosome. eEF2 kinase (eEF2K) phosphorylates and inactivates eEF2, resulting in the inhibition of peptide-chain elongation. eEF2K is normally dependent on Ca2+ ions and calmodulin, and can be activated by PKA in response to elevated cAMP levels during cell stress- or starvation-related conditions. Regulation of eEF2K occurs through phosphorylation at multiple sites. Ser-78 phosphorylation is required for calmodulin binding and eEF2K activity, while phosphorylation of Ser-500 is required for Ca2+/calmodulin-independent kinase activity. Thr-348 is an autophosphorylation site that is required for kinase activity. Inhibitory phosphorylation may also regulate eEF2K, since phosphorylation at Ser-359 by SAPK4/p38δ causes inactivation of eEF2K. Thus, multisite phospho-regulation of eEF2K may be important for proper control of eEF2K activity and protein translation.
Synonyms
EEF-2, eEF-2K, CaMK-III, eukaryotic elongation factor
Swiss Prot
O00418
Modification Site
Ser-359
Host
Rabbit
Cross Reactivity
Human, Mouse, Rat
Target
EEF2K (Ser-359)
Clonality
Polyclonal
Isotype
IgG
Conjugation
Unconjugated
Source
Phospho-eEF2K (Ser-359) synthetic peptide (coupled to carrier protein) corresponds to amino acids surrounding Ser-359 in human eEF2K.
Applications
WB
Purification
Antigen Affinity purification
Dilution
WB (1:300-5000)
Buffer
PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol
Modification
Phosphorylation
Storage Conditions
Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C.
Specificity
The antibody detects a 105 kDa* protein corresponding to the molecular mass of eEF2K on SDS-PAGE immunoblots of human recombinant eEF2K autophosphorylated in the presence of Ca2+ and Calmodulin. This reactivity is removed after lambda phosphatase treatment. This sequence is well conserved in rat and mouse eEF2K, and has low homology to other proteins.