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Monkey Translation Elongation Factor Activity

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Translation is the process where amino acid residues are assembled into polypeptides on ribosomes. This process is generally divided into three stages: initiation, elongation and termination. During elongation, mRNA and tRNA pair at the two active sites (A and P sites) on the ribosome. A number of eukaryotic elongation factors (eEFs) are involved in this process in mammalian cells (1). eEF1A, also called elongation factor Tu (EF-Tu), binds GTP and interacts with amino acyl-tRNAs to promote recruitment of amino acyl-tRNAs to the A-site of the ribosome (1). After GTP hydrolysis, GDP-eEF1A leaves the ribosome and is later converted back to the GTP-eEF1A by eEF1B (1). Studies have shown that eEF1A is phosphorylated under certain conditions, indicating that its activity is regulated at the post-translational level (2,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Translation is the process where amino acid residues are assembled into polypeptides on ribosomes. This process is generally divided into three stages: initiation, elongation and termination. During elongation, mRNA and tRNA pair at the two active sites (A and P sites) on the ribosome. A number of eukaryotic elongation factors (eEFs) are involved in this process in mammalian cells (1). eEF1A, also called elongation factor Tu (EF-Tu), binds GTP and interacts with amino acyl-tRNAs to promote recruitment of amino acyl-tRNAs to the A-site of the ribosome (1). After GTP hydrolysis, GDP-eEF1A leaves the ribosome and is later converted back to the GTP-eEF1A by eEF1B (1). Studies have shown that eEF1A is phosphorylated under certain conditions, indicating that its activity is regulated at the post-translational level (2,3).

$303
100 µl
APPLICATIONS
REACTIVITY
Chicken, Hamster, Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Eukaryotic elongation factor 2 (eEF2) catalyzes the translocation of peptidyl-tRNA from the A site to the P site on the ribosome. It has been shown that phosphorylation of eEF2 at threonine 56 by eEF2 kinase inhibits its activity (1-4). eEF2 kinase is normally dependent on Ca2+ ions and calmodulin (5,6). eEF2 kinase can also be activated by PKA in response to elevated cAMP levels (7-9), which are generally increased in stress- or starvation-related conditions. A variety of treatments known to raise intracellular Ca2+ or cAMP levels have been shown to result in increased phosphorylation of eEF2, and thus to inhibit peptide-chain elongation. The inactive phosphorylated eEF2 can be converted to its active nonphosphorylated form by a protein phosphatase, most likely a form of protein phosphatase-2A (PP-2A). Insulin, which activates protein synthesis in a wide range of cell types, induces rapid dephosphorylation of eEF2 through mTOR signaling and may involve modulation of the activity of the PP-2A or the eEF2 kinase or both (10).

$260
100 µl
APPLICATIONS
REACTIVITY
D. melanogaster, Human, Monkey, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Eukaryotic elongation factor 2 (eEF2) catalyzes the translocation of peptidyl-tRNA from the A site to the P site on the ribosome. It has been shown that phosphorylation of eEF2 at threonine 56 by eEF2 kinase inhibits its activity (1-4). eEF2 kinase is normally dependent on Ca2+ ions and calmodulin (5,6). eEF2 kinase can also be activated by PKA in response to elevated cAMP levels (7-9), which are generally increased in stress- or starvation-related conditions. A variety of treatments known to raise intracellular Ca2+ or cAMP levels have been shown to result in increased phosphorylation of eEF2, and thus to inhibit peptide-chain elongation. The inactive phosphorylated eEF2 can be converted to its active nonphosphorylated form by a protein phosphatase, most likely a form of protein phosphatase-2A (PP-2A). Insulin, which activates protein synthesis in a wide range of cell types, induces rapid dephosphorylation of eEF2 through mTOR signaling and may involve modulation of the activity of the PP-2A or the eEF2 kinase or both (10).

$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Eukaryotic elongation factor 2 kinase (eEF2k) phosphorylates and inactivates eEF2, resulting in the inhibition of peptide-chain elongation (1). eEF2k is normally dependent on Ca2+ ions and calmodulin (2,3). It can be activated by PKA in response to elevated cAMP levels (4-6), which are generally increased in stress- or starvation-related conditions. eEF2k can also be regulated in response to a wide range of stimuli that promote cell growth and protein synthesis. This involves the phosphorylation of eEF2k by p90RSK and p70 S6 kinase at Ser366 or by SAPK4/p38delta at Ser359, leading to the inactivation of eEF2k (7,8), which facilitates the dephosphorylation of eEF2, and thus promotes translation.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: Eukaryotic elongation factor 2 kinase (eEF2k) phosphorylates and inactivates eEF2, resulting in the inhibition of peptide-chain elongation (1). eEF2k is normally dependent on Ca2+ ions and calmodulin (2,3). It can be activated by PKA in response to elevated cAMP levels (4-6), which are generally increased in stress- or starvation-related conditions. eEF2k can also be regulated in response to a wide range of stimuli that promote cell growth and protein synthesis. This involves the phosphorylation of eEF2k by p90RSK and p70 S6 kinase at Ser366 or by SAPK4/p38delta at Ser359, leading to the inactivation of eEF2k (7,8), which facilitates the dephosphorylation of eEF2, and thus promotes translation.