EEF2 Antibody | Affinity Biosciences

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Figure 1: Western blot analysis using EEF2 mouse mAb against HepG2 (1), Hela (2), HEK293 (3) and A431 (4) cell lysate.

Product:	EEF2 Antibody
Catalog:	BF0405
Description:	Mouse monoclonal antibody to EEF2
Application:	WB IHC IF/ICC ELISA
Reactivity:	Human, Mouse
Mol.Wt.:	95kDa; 95kD(Calculated).
Uniprot:	P13639
RRID:	AB_2833901

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Product Info

Source:

Mouse

Application:

ELISA 1:10000, WB 1:500-1:2000, IHC 1:200-1:1000, IF/ICC 1:200-1:1000
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:

Human,Mouse

Clonality:

Monoclonal [AFB1877]

Specificity:

EEF2 antibody detects endogenous levels of total EEF2.

RRID:

AB_2833901
Cite Format: Affinity Biosciences Cat# BF0405, RRID:AB_2833901.

Conjugate:

Unconjugated.

Purification:

Affinity-chromatography.

Storage:

Mouse IgG1 in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.

Alias:

Fold/Unfold

EEF 2; Eef2; EF-2; EF2; EF2_HUMAN; Elongation factor 2; Eukaryotic translation elongation factor 2; Polypeptidyl tRNA translocase; SCA26;

Immunogens

Immunogen:

Purified recombinant fragment of human EEF2 expressed in E. Coli.

Uniprot:

P13639(EF2_HUMAN) >>Visit HPA database.

Gene(ID):

EEF2(1938)

Description:

This gene encodes a member of the GTP-binding translation elongation factor family. This protein is an essential factor for protein synthesis. It promotes the GTP-dependent translocation of the nascent protein chain from the A-site to the P-site of the ribosome. This protein is completely inactivated by EF-2 kinase phosporylation. (provided by RefSeq)

Sequence:

P13639 EF2_HUMAN:
Protein BLAST With
NCBI/
ExPASy/
Uniprot

MVNFTVDQIRAIMDKKANIRNMSVIAHVDHGKSTLTDSLVCKAGIIASARAGETRFTDTRKDEQERCITIKSTAISLFYELSENDLNFIKQSKDGAGFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKMDRALLELQLEPEELYQTFQRIVENVNVIISTYGEGESGPMGNIMIDPVLGTVGFGSGLHGWAFTLKQFAEMYVAKFAAKGEGQLGPAERAKKVEDMMKKLWGDRYFDPANGKFSKSATSPEGKKLPRTFCQLILDPIFKVFDAIMNFKKEETAKLIEKLDIKLDSEDKDKEGKPLLKAVMRRWLPAGDALLQMITIHLPSPVTAQKYRCELLYEGPPDDEAAMGIKSCDPKGPLMMYISKMVPTSDKGRFYAFGRVFSGLVSTGLKVRIMGPNYTPGKKEDLYLKPIQRTILMMGRYVEPIEDVPCGNIVGLVGVDQFLVKTGTITTFEHAHNMRVMKFSVSPVVRVAVEAKNPADLPKLVEGLKRLAKSDPMVQCIIEESGEHIIAGAGELHLEICLKDLEEDHACIPIKKSDPVVSYRETVSEESNVLCLSKSPNKHNRLYMKARPFPDGLAEDIDKGEVSARQELKQRARYLAEKYEWDVAEARKIWCFGPDGTGPNILTDITKGVQYLNEIKDSVVAGFQWATKEGALCEENMRGVRFDVHDVTLHADAIHRGGGQIIPTARRCLYASVLTAQPRLMEPIYLVEIQCPEQVVGGIYGVLNRKRGHVFEESQVAGTPMFVVKAYLPVNESFGFTADLRSNTGGQAFPQCVFDHWQILPGDPFDNSSRPSQVVAETRKRKGLKEGIPALDNFLDKL

PTMs - P13639 As Substrate

P13639

Site	PTM Type	Enzyme	Source
R10	Methylation		Uniprot
K15	Ubiquitination		Uniprot
S23	Phosphorylation		Uniprot
K32	Ubiquitination		Uniprot
S38	Phosphorylation		Uniprot
C41	S-Nitrosylation		Uniprot
K42	Acetylation		Uniprot
K42	Ubiquitination		Uniprot
S48	Phosphorylation		Uniprot
R50	Methylation		Uniprot
T54	Phosphorylation	O00418 (EEF2K)	Uniprot
T57	Phosphorylation	O00418 (EEF2K)	Uniprot
T59	Phosphorylation	O00418 (EEF2K)	Uniprot
C67	S-Nitrosylation		Uniprot
S72	Phosphorylation		Uniprot
T73	Phosphorylation		Uniprot
S76	Phosphorylation		Uniprot
Y79	Phosphorylation		Uniprot
K90	Ubiquitination		Uniprot
K93	Ubiquitination		Uniprot
K152	Ubiquitination		Uniprot
K159	Ubiquitination		Uniprot
Y175	Phosphorylation		Uniprot
T177	Phosphorylation		Uniprot
S197	Phosphorylation		Uniprot
K235	Acetylation		Uniprot
K235	Ubiquitination		Uniprot
K239	Acetylation		Uniprot
K239	Sumoylation		Uniprot
K239	Ubiquitination		Uniprot
K251	Ubiquitination		Uniprot
K252	Acetylation		Uniprot
K252	Ubiquitination		Uniprot
K258	Acetylation		Uniprot
K259	Ubiquitination		Uniprot
R264	Methylation		Uniprot
Y265	Phosphorylation		Uniprot
K272	Acetylation		Uniprot
K272	Methylation		Uniprot
K272	Ubiquitination		Uniprot
S274	Phosphorylation		Uniprot
K275	Acetylation		Uniprot
K275	Ubiquitination		Uniprot
K283	Ubiquitination		Uniprot
T288	Phosphorylation		Uniprot
C290	S-Nitrosylation		Uniprot
K308	Acetylation		Uniprot
K308	Ubiquitination		Uniprot
K314	Acetylation		Uniprot
K314	Ubiquitination		Uniprot
K318	Acetylation		Uniprot
K318	Ubiquitination		Uniprot
K322	Acetylation		Uniprot
K322	Sumoylation		Uniprot
K322	Ubiquitination		Uniprot
S325	Phosphorylation		Uniprot
K330	Ubiquitination		Uniprot
K333	Ubiquitination		Uniprot
K337	Acetylation		Uniprot
K337	Ubiquitination		Uniprot
T355	Phosphorylation		Uniprot
S360	Phosphorylation		Uniprot
K366	Acetylation		Uniprot
K366	Ubiquitination		Uniprot
C369	S-Nitrosylation		Uniprot
Y373	Phosphorylation		Uniprot
K386	Ubiquitination		Uniprot
K391	Acetylation		Uniprot
K391	Ubiquitination		Uniprot
S399	Phosphorylation		Uniprot
K400	Ubiquitination		Uniprot
T404	Phosphorylation		Uniprot
K407	Acetylation		Uniprot
K407	Methylation		Uniprot
K407	Ubiquitination		Uniprot
R409	Methylation		Uniprot
Y411	Phosphorylation		Uniprot
S418	Phosphorylation		Uniprot
K426	Acetylation		Uniprot
K426	Ubiquitination		Uniprot
R428	Methylation		Uniprot
Y434	Phosphorylation		Uniprot
T435	Phosphorylation	P24941 (CDK2)	Uniprot
K438	Acetylation		Uniprot
K438	Ubiquitination		Uniprot
K439	Acetylation		Uniprot
K439	Ubiquitination		Uniprot
Y443	Phosphorylation		Uniprot
K445	Acetylation		Uniprot
K445	Methylation		Uniprot
K445	Ubiquitination		Uniprot
T450	Phosphorylation		Uniprot
K481	Ubiquitination		Uniprot
R495	Methylation		Uniprot
K498	Acetylation		Uniprot
K498	Methylation		Uniprot
K498	Ubiquitination		Uniprot
S500	Phosphorylation		Uniprot
S502	Phosphorylation		Uniprot
K512	Ubiquitination		Uniprot
K519	Methylation		Uniprot
K519	Ubiquitination		Uniprot
K525	Methylation		Uniprot
K525	Ubiquitination		Uniprot
R526	Methylation		Uniprot
K529	Sumoylation		Uniprot
S530	Phosphorylation		Uniprot
S541	Phosphorylation		Uniprot
C567	S-Nitrosylation		Uniprot
K571	Ubiquitination		Uniprot
K572	Ubiquitination		Uniprot
Y579	Phosphorylation		Uniprot
T582	Phosphorylation		Uniprot
S584	Phosphorylation		Uniprot
S587	Phosphorylation		Uniprot
C591	S-Nitrosylation		Uniprot
S593	Phosphorylation		Uniprot
K594	Methylation		Uniprot
K594	Ubiquitination		Uniprot
S595	Phosphorylation	P24941 (CDK2)	Uniprot
K598	Ubiquitination		Uniprot
K605	Ubiquitination		Uniprot
K619	Ubiquitination		Uniprot
S623	Phosphorylation		Uniprot
K629	Ubiquitination		Uniprot
K638	Acetylation		Uniprot
K638	Methylation		Uniprot
K638	Ubiquitination		Uniprot
K648	Acetylation		Uniprot
K648	Ubiquitination		Uniprot
C651	S-Nitrosylation		Uniprot
K667	Ubiquitination		Uniprot
Y671	Phosphorylation		Uniprot
K676	Ubiquitination		Uniprot
S678	Phosphorylation		Uniprot
K688	Acetylation		Uniprot
K688	Ubiquitination		Uniprot
R698	Methylation		Uniprot
R716	Methylation		Uniprot
T724	Phosphorylation		Uniprot
R726	Methylation		Uniprot
C728	S-Nitrosylation		Uniprot
Y730	Phosphorylation		Uniprot
S732	Phosphorylation		Uniprot
R739	Methylation		Uniprot
Y745	Phosphorylation		Uniprot
Y760	Phosphorylation		Uniprot
K766	Ubiquitination		Uniprot
R767	Methylation		Uniprot
T779	Phosphorylation		Uniprot
S793	Phosphorylation		Uniprot
S802	Phosphorylation		Uniprot
K842	Ubiquitination		Uniprot
K845	Ubiquitination		Uniprot
K857	Acetylation		Uniprot
K857	Ubiquitination		Uniprot

Research Backgrounds

P13639_EF2_HUMAN

Function:

Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. 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. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.

PTMs:

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 Location:

Cytoplasm. Nucleus.
Note: Phosphorylation by CSK promotes cleavage and SUMOylation-dependent nuclear translocation of the C-terminal cleavage product.

Subunit Structure:

Component of the mRNA surveillance SURF complex, at least composed of ERF1, ERF3 (ERF3A or ERF3B), EEF2, UPF1/RENT1, SMG1, SMG8 and SMG9. Interacts with RBPMS2.

Family&Domains:

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

Research Fields

· Environmental Information Processing > Signal transduction > AMPK signaling pathway. (View pathway)

· Organismal Systems > Endocrine system > Oxytocin signaling pathway.

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EEF2 Antibody - #BF0405

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