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AB183170

Recombinant Human EEF2/Elongation factor 2 protein (denatured)

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Recombinant Human EEF2/Elongation factor 2 protein (denatured) is a Human Fragment protein, in the 574 to 858 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE.

View Alternative Names

EF2, EEF2, Elongation factor 2, EF-2

1 Images
SDS-PAGE - Recombinant Human EEF2/Elongation factor 2 protein (denatured) (AB183170)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human EEF2/Elongation factor 2 protein (denatured) (AB183170)

15% SDS-PAGE analysis of ab183170 (3μg).

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

P13639

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": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Product details

This product was previously labelled as EEF2
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Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMGSDPVVSYRETVSEESNVLCLSKSPNKHNRLYMKARPFPDGLAEDIDKGEVSARQELKQRARYLAEKYEWDVAEARKIWCFGPDGTGPNILTDITKGVQYLNEIKDSVVAGFQWATKEGALCEENMRGVRFDVHDVTLHADAIHRGGGQIIPTARRCLYASVLTAQPRLMEPIYLVEIQCPEQVVGGIYGVLNRKRGHVFEESQVAGTPMFVVKAYLPVNESFGFTADLRSNTGGQAFPQCVFDHWQILPGDPFDNSSRPSQVVAETRKRKGLKEGIPALDNFLDKL","proteinLength":"Fragment","predictedMolecularWeight":"34.3 kDa","actualMolecularWeight":null,"aminoAcidEnd":858,"aminoAcidStart":574,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P13639","tags":[{"tag":"His","terminus":"N-Terminus"}]}]
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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.

EEF2 or elongation factor 2 is an important protein in the process of translation during protein synthesis. It is also known by the names EF-2 and EF2. This protein facilitates the translocation step where it moves tRNA and mRNA from the A-site to the P-site on the ribosome. EEF2 has a molecular weight of approximately 95 kDa. The protein is ubiquitously expressed in various tissues and cells due to its fundamental role in protein synthesis making it essential for cellular activities.
Biological function summary

EEF2 functions as part of a larger ribosomal complex. It has an important role in ensuring the accuracy and efficiency of elongation during the translation process. This process is energy-dependent with EEF2 requiring GTP to catalyze the movement along the mRNA strand. The protein must undergo reversible phosphorylation which directly affects its activity. This post-translational modification of EEF2 is a significant modulation point influencing the rate of protein synthesis.

Pathways

EEF2 plays an integral role in the mTOR signaling pathway and the insulin signaling pathway. In the mTOR pathway EEF2 activity is regulated to control protein translation based on cellular energy status and nutrient availability. This pathway is important for cell growth and proliferation. EEF2 interacts with other proteins such as factor 2 and eEF2kinase which phosphorylates the protein thereby inhibiting its activity. In the insulin signaling pathway similar regulatory mechanisms impact EEF2’s role in translation.

EEF2 connects to cancer and neurodegenerative diseases. In cancer aberrant regulation of EEF2 can lead to uncontrolled protein synthesis promoting cell proliferation and tumor growth. Its interaction with mTOR and other signaling proteins like ribosomal proteins plays a role in this dysregulation. In neurodegenerative conditions such as Alzheimer’s disease impaired EEF2 activity results in decreased synaptic protein synthesis affecting neuronal function. Understanding EEF2’s regulation and dysregulation provides insight into its involvement in these diseases offering potential for therapeutic intervention.
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Specifications

Form

Liquid

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General info

Function

Catalyzes the GTP-dependent ribosomal translocation step during translation elongation (PubMed : 26593721). During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively (PubMed : 26593721). Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (PubMed : 26593721).

Sequence similarities

Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily.

Post-translational modifications

Phosphorylation by EF-2 kinase completely inactivates EF-2; it requires prior phosphorylation by CDK2 at Ser-595 during mitotic prometaphase. Phosphorylation by CSK promotes SUMOylation, proteolytic cleavage, and nuclear translocation if the C-terminal fragment.. Diphthamide is 2-[3-carboxyamido-3-(trimethyl-ammonio)propyl]histidine (By similarity).. (Microbial infection) Diphthamide can be ADP-ribosylated by diphtheria toxin and by Pseudomonas exotoxin A, thus arresting protein synthesis.. ISGylated.. Proteolytically processed at two sites following phosphorylation by CSK.. SUMOylated following phosphorylation by CSK, promotes proteolytic cleavage.

Subcellular localisation

Nucleus

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Product protocols

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Target data

Catalyzes the GTP-dependent ribosomal translocation step during translation elongation (PubMed : 26593721). During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively (PubMed : 26593721). Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (PubMed : 26593721).
See full target information EEF2
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