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AB177675

Recombinant Human eEF1A1/EF-Tu protein (denatured) (Tag Free)

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(2 Publications)

Recombinant Human eEF1A1/EF-Tu protein (denatured) (Tag Free) is a Human Full Length protein, in the 1 to 462 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE.

View 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

1 Images
SDS-PAGE - Recombinant Human eEF1A1/EF-Tu protein (denatured) (Tag Free) (AB177675)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human eEF1A1/EF-Tu protein (denatured) (Tag Free) (AB177675)

15% SDS-PAGE analysis of ab177675 (3 μg).

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

Tag free

Applications

SDS-PAGE

applications

Biologically active

No

Accession

P68104

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 10% Glycerol (glycerin, glycerine), 2.4% Urea, 0.32% Tris HCl

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "FuncS": { "reactivity":"TESTED_AND_DOES_NOT_REACT", "dilution-info":"", "notes":"<p></p>" }, "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEPPYSQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKGWKVTRKDGNASGTTLLEALDCILPPTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVRRGNVAGDSKNDPPMEAAGFTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAAIVDMVPGKPMCVESFSDYPPLGRFAVRDMRQTVAVGVIKAVDKKAAGAGKITKSAQKAQKAK","proteinLength":"Full Length","predictedMolecularWeight":"50 kDa","actualMolecularWeight":null,"aminoAcidEnd":462,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P68104","tags":[]}]
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Properties and storage information

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
False
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

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.

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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Specifications

Form

Liquid

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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).. (Microbial infection) Required for the translation of viral proteins and viral replication during human coronavirus SARS-CoV-2 infection.

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.. Phosphorylated by TXK (PubMed:17177976). Phosphorylation by PASK increases translation efficiency (PubMed:17595531). Phosphorylated by ROCK2 (PubMed:26497934). Phosphorylation by TGFBR1 inhibits translation elongation (PubMed:20832312).. Trimethylated at Lys-79 by EEF1AKMT1 (PubMed:26545399). Methylated at Lys-165 by EEF1AKMT3, methylation by EEF1AKMT3 is dynamic as well as inducible by stress conditions, such as ER-stress, and plays a regulatory role on mRNA translation (PubMed:28108655). Trimethylated at Lys-318 by EEF1AKMT2 (PubMed:25144183). Mono-, di-, and trimethylated at Lys-36 by EEF1AKMT4; trimethylated form is predominant. Methylation by EEF1AKMT4 contributes to the fine-tuning of translation rates for a subset of tRNAs (PubMed:28520920). Trimethylated at Gly-2 by METTL13 (PubMed:30143613). Mono- and dimethylated at Lys-55 by METTL13; dimethylated form is predominant (PubMed:30143613, PubMed:30612740).. Ubiquitinated at Lys-385 by RNF14 in response to ribosome collisions (ribosome stalling), leading to its degradation by the proteasome and rescue of stalled ribosomes.

Subcellular localisation

Nucleus

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Product protocols

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Target data

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.
See full target information EEF1A1
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Publications (2)

Recent publications for all applications. Explore the full list and refine your search

Molecular cancer therapeutics 23:159-173 PubMed37940144

2023

Novel Methionine Aminopeptidase 2 Inhibitor M8891 Synergizes with VEGF Receptor Inhibitors to Inhibit Tumor Growth of Renal Cell Carcinoma Models.

Applications

Unspecified application

Species

Unspecified reactive species

Manja Friese-Hamim,Maria J Ortiz Ruiz,Olga Bogatyrova,Marina Keil,Felix Rohdich,Beatrix Blume,Birgitta Leuthner,Frank Czauderna,Diane Hahn,Julia Jabs,Frank Jaehrling,Timo Heinrich,Roland Kellner,Katherine Chan,Amy H Y Tong,Dirk Wienke,Jason Moffat,Andree Blaukat,Frank T Zenke

Pharmaceutical research 40:3011-3023 PubMed37798538

2023

Preclinical Pharmacokinetics and Translational Pharmacokinetic/Pharmacodynamic Modeling of M8891, a Potent and Reversible Inhibitor of Methionine Aminopeptidase 2.

Applications

Unspecified application

Species

Unspecified reactive species

Floriane Lignet,Manja Friese-Hamim,Frank Jaehrling,Samer El Bawab,Felix Rohdich
View all publications
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