Recombinant Human eEF1A1/EF-Tu protein (denatured) is a Human Full Length protein, in the 1 to 462 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
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- Pharmaceutical research 40:3011-30232023Preclinical Pharmacokinetics and Translational Pharmacokinetic/Pharmacodynamic Modeling of M8891, a Potent and Reversible Inhibitor of Methionine Aminopeptidase 2.Applications:Unspecified applicationReactive species:Unspecified reactive speciesFloriane Lignet,Manja Friese-Hamim,Frank Jaehrling,Samer El Bawab,Felix RohdichPubMed 37798538
Key facts
- Purity
- >90% SDS-PAGE
- Expression system
- Escherichia coli
- Tags
- Tag free
- Applications
- SDS-PAGE
- Biologically active
- No
Amino acid sequence
M G K E K T H I N I V V I G H V D S G K S T T T G H L I Y K C G G I D K R T I E K F E K E A A E M G K G S F K Y A W V L D K L K A E R E R G I T I D I S L W K F E T S K Y Y V T I I D A P G H R D F I K N M I T G T S Q A D C A V L I V A A G V G E F E A G I S K N G Q T R E H A L L A Y T L G V K Q L I V G V N K M D S T E P P Y S Q K R Y E E I V K E V S T Y I K K I G Y N P D T V A F V P I S G W N G D N M L E P S A N M P W F K G W K V T R K D G N A S G T T L L E A L D C I L P P T R P T D K P L R L P L Q D V Y K I G G I G T V P V G R V E T G V L K P G M V V T F A P V N V T T E V K S V E M H H E A L S E A L P G D N V G F N V K N V S V K D V R R G N V A G D S K N D P P M E A A G F T A Q V I I L N H P G Q I S A G Y A P V L D C H T A H I A C K F A E L K E K I D R R S G K K L E D G P K F L K S G D A A I V D M V P G K P M C V E S F S D Y P P L G R F A V R D M R Q T V A V G V I K A V D K K A A G A G K I T K S A Q K A Q K A K
Reactivity data
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application FuncS | Reactivity No | Dilution info - | Notes - |
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
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Target data
Function
Translation elongation factor that catalyzes the GTP-dependent binding of aminoacyl-tRNA (aa-tRNA) to the A-site of ribosomes during the elongation phase of protein synthesis (PubMed:26593721, PubMed:26651998, PubMed:36123449, PubMed:36264623, PubMed:36638793). Base pairing between the mRNA codon and the aa-tRNA anticodon promotes GTP hydrolysis, releasing the aa-tRNA from EEF1A1 and allowing its accommodation into the ribosome (PubMed:26593721, PubMed:26651998, PubMed:36123449, PubMed:36264623, PubMed:36638793). The growing protein chain is subsequently transferred from the P-site peptidyl tRNA to the A-site aa-tRNA, extending it by one amino acid through ribosome-catalyzed peptide bond formation (PubMed:26593721, PubMed:26651998, PubMed:36123449, PubMed:36264623). Also plays a role in the positive regulation of IFNG transcription in T-helper 1 cells as part of an IFNG promoter-binding complex with TXK and PARP1 (PubMed:17177976). (Microbial infection) Required for the translation of viral proteins and viral replication during human coronavirus SARS-CoV-2 infection.
Alternative names
EEF1A, EF1A, LENG7, EEF1A1, Elongation factor 1-alpha 1, EF-1-alpha-1, Elongation factor Tu, Eukaryotic elongation factor 1 A-1, Leukocyte receptor cluster member 7, EF-Tu, eEF1A-1
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Recombinant Human eEF1A1/EF-Tu protein (denatured) is a Human Full Length protein, in the 1 to 462 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
Key facts
- Purity
- >90% SDS-PAGE
- Expression system
- Escherichia coli
- Tags
- Tag free
- Applications
- SDS-PAGE
- Biologically active
- No
- Accession
- P68104-1
- Animal free
- No
- Species
- Human
- Concentration
- Storage buffer
pH: 8
Constituents: 10% Glycerol (glycerin, glycerine), 2.4% Urea, 0.32% Tris HCl
Sequence info
Amino acid sequence
- M G K E K T H I N I V V I G H V D S G K S T T T G H L I Y K C G G I D K R T I E K F E K E A A E M G K G S F K Y A W V L D K L K A E R E R G I T I D I S L W K F E T S K Y Y V T I I D A P G H R D F I K N M I T G T S Q A D C A V L I V A A G V G E F E A G I S K N G Q T R E H A L L A Y T L G V K Q L I V G V N K M D S T E P P Y S Q K R Y E E I V K E V S T Y I K K I G Y N P D T V A F V P I S G W N G D N M L E P S A N M P W F K G W K V T R K D G N A S G T T L L E A L D C I L P P T R P T D K P L R L P L Q D V Y K I G G I G T V P V G R V E T G V L K P G M V V T F A P V N V T T E V K S V E M H H E A L S E A L P G D N V G F N V K N V S V K D V R R G N V A G D S K N D P P M E A A G F T A Q V I I L N H P G Q I S A G Y A P V L D C H T A H I A C K F A E L K E K I D R R S G K K L E D G P K F L K S G D A A I V D M V P G K P M C V E S F S D Y P P L G R F A V R D M R Q T V A V G V I K A V D K K A A G A G K I T K S A Q K A Q K A K
- Accession
- P68104
- Protein length
- Full Length
- Predicted molecular weight
- 50 kDa
- Amino acids
- 1 to 462
- Nature
- Recombinant
Specifications
- Form
- Liquid
General info
- Function
Translation elongation factor that catalyzes the GTP-dependent binding of aminoacyl-tRNA (aa-tRNA) to the A-site of ribosomes during the elongation phase of protein synthesis (PubMed:26593721, PubMed:26651998, PubMed:36123449, PubMed:36264623, PubMed:36638793). Base pairing between the mRNA codon and the aa-tRNA anticodon promotes GTP hydrolysis, releasing the aa-tRNA from EEF1A1 and allowing its accommodation into the ribosome (PubMed:26593721, PubMed:26651998, PubMed:36123449, PubMed:36264623, PubMed:36638793). The growing protein chain is subsequently transferred from the P-site peptidyl tRNA to the A-site aa-tRNA, extending it by one amino acid through ribosome-catalyzed peptide bond formation (PubMed:26593721, PubMed:26651998, PubMed:36123449, PubMed:36264623). Also plays a role in the positive regulation of IFNG transcription in T-helper 1 cells as part of an IFNG promoter-binding complex with TXK and PARP1 (PubMed:17177976).
- Sequence similarities
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily.
- Post-translational modifications
ISGylated.
- Subcellular localisation
- Nucleus, Nucleolus
Storage
- Shipped at conditions
- Blue Ice
- Appropriate short-term storage duration
- 1-2 weeks
- Appropriate short-term storage conditions
- +4°C
- Appropriate long-term storage conditions
- -20°C
- Aliquoting information
- Upon delivery aliquot
- Storage information
- Avoid freeze / thaw cycle
Supplementary info
- This supplementary information is collated from multiple sources and compiled automatically.
- Activity summary
EEF1A1 also known as EF-Tu in prokaryotes functions as an elongation factor in the process of protein synthesis. It facilitates the delivery of aminoacyl-tRNA to the ribosome during the elongation phase of translation. eEF1A1 exhibits a mass of approximately 50 kDa and shows high expression levels in various tissues particularly in the liver and neuronal tissues. It shares functional similarities with EF-G which plays a role in translocation during translation. Moreover eEF1A1 appears relevant in cellular processes beyond translation contributing to its importance across cellular functions.
- Biological function summary
EEF1A1 acts as an important component in the machinery of protein synthesis and takes part in the elongation factor complex. Within this complex eEF1A1 interacts with other molecules to ensure the accuracy and efficiency of codon-anticodon pairing on the ribosome. Additionally eEF1A1 associates with actin and participates in the cytoskeleton organization. This multifunctional currency of eEF1A1 suggests its involvement in diverse cellular processes beyond classic translation tasks.
- Pathways
The role of eEF1A1 in protein synthesis positions it within the larger context of the mTOR signaling pathway important for cellular growth proliferation and metabolism. Since its function bridges translation initiation and elongation it interacts with proteins like mTOR and S6K1. Within the MAPK pathway eEF1A1 shows interactions influencing cellular survival and apoptosis. These interactions connect eEF1A1 to essential regulatory mechanisms that maintain cellular homeostasis and adaptability.
- Associated diseases and disorders
EEF1A1 exhibits significant involvement in cancer and neurodegenerative diseases. Overexpression or mutation of eEF1A1 frequently associates with various cancers implicating its role in tumor progression and cell proliferation. Interactions with proteins such as p53 link eEF1A1 to pathways that influence tumor suppression and genomic stability. In neurodegenerative conditions like Alzheimer's disease altered eEF1A1 behavior and expression affect neuronal viability and tau protein interaction suggesting its potential contribution to the pathogenesis of these disorders.
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SDS-PAGE - Recombinant Human eEF1A1/EF-Tu protein (denatured) (ab177675)
15% SDS-PAGE analysis of ab177675 (3 μg).
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