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Mouse Anti-EEF2 Recombinant Antibody (CAP663) (CBMAB-AP1987LY)

Summary

Host Animal
Mouse
Specificity
Human, Mouse, Rat
Clone
CAP663
Antibody Isotype
IgG
Application
ELISA, WB

Basic Information

Immunogen
Purified recombinant human EEF2 protein fragments expressed in E.coli.
Specificity
Human, Mouse, Rat
Antibody Isotype
IgG
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
Eukaryotic Translation Elongation Factor 2
Introduction
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, Jul 2008]
Entrez Gene ID
Human1938
Mouse13629
Rat29565
UniProt ID
HumanP13639
MouseP58252
RatP05197
Alternative Names
Eukaryotic Translation Elongation Factor 2; Polypeptidyl-TRNA Translocase; EF-2; EF2; Elongation Factor 2; EEF-2; SCA26;
Research Area
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.
Biological Process
Aging Source: Ensembl
Cellular response to brain-derived neurotrophic factor stimulus Source: Ensembl
Glial cell proliferation Source: Ensembl
Hematopoietic progenitor cell differentiation Source: Ensembl
Positive regulation of cytoplasmic translation Source: Ensembl
Positive regulation of translation Source: UniProtKB
Response to drug Source: Ensembl
Response to endoplasmic reticulum stress Source: Ensembl
Response to estradiol Source: Ensembl
Response to ethanol Source: Ensembl
Response to folic acid Source: Ensembl
Response to hydrogen peroxide Source: Ensembl
Response to ischemia Source: Ensembl
Skeletal muscle cell differentiation Source: Ensembl
Skeletal muscle contraction Source: Ensembl
Translational elongation Source: GO_Central
Cellular Location
Nucleus; Cytoplasm. Phosphorylation by CSK promotes cleavage and SUMOylation-dependent nuclear translocation of the C-terminal cleavage product.
Involvement in disease
Spinocerebellar ataxia 26 (SCA26):
A form of spinocerebellar ataxia, a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord.
PTM
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.

Liu, S., Matsui, T. S., Kang, N., & Deguchi, S. (2022). Analysis of senescence-responsive stress fiber proteome reveals reorganization of stress fibers mediated by elongation factor eEF2 in HFF-1 cells. Molecular biology of the cell, 33(1), ar10.

Ma, T. (2021). Roles of eukaryotic elongation factor 2 kinase (eEF2K) in neuronal plasticity, cognition, and Alzheimer disease. Journal of Neurochemistry.

Beretta, S., Gritti, L., Verpelli, C., & Sala, C. (2020). Eukaryotic elongation factor 2 kinase a pharmacological target to regulate protein translation dysfunction in neurological diseases. Neuroscience, 445, 42-49.

Suzuki, K., & Monteggia, L. M. (2020). The role of eEF2 kinase in the rapid antidepressant actions of ketamine. Advances in Pharmacology, 89, 79-99.

Mönkemeyer, L., Klaips, C. L., Balchin, D., Körner, R., Hartl, F. U., & Bracher, A. (2019). Chaperone function of Hgh1 in the biogenesis of eukaryotic elongation factor 2. Molecular cell, 74(1), 88-100.

Kameshima, S., Okada, M., & Yamawaki, H. (2019). Eukaryotic elongation factor 2 (eEF2) kinase/eEF2 plays protective roles against glucose deprivation-induced cell death in H9c2 cardiomyoblasts. Apoptosis, 24(3), 359-368.

Vasamsetti, B. M. K., Liu, Z., Park, Y. S., & Cho, N. J. (2019). Muscarinic acetylcholine receptors regulate the dephosphorylation of eukaryotic translation elongation factor 2 in SNU-407 colon cancer cells. Biochemical and biophysical research communications, 516(2), 424-429.

Susorov, D., Zakharov, N., Shuvalova, E., Ivanov, A., Egorova, T., Shuvalov, A., ... & Alkalaeva, E. (2018). Eukaryotic translation elongation factor 2 (eEF2) catalyzes reverse translocation of the eukaryotic ribosome. Journal of Biological Chemistry, 293(14), 5220-5229.

Shi, N., Chen, X., Liu, R., Wang, D., Su, M., Wang, Q., ... & Gu, H. (2018). Eukaryotic elongation factors 2 promotes tumor cell proliferation and correlates with poor prognosis in ovarian cancer. Tissue and Cell, 53, 53-60.

Zhang, X., Hu, L., Du, M., Wei, X., Zhang, J., Hui, Y., ... & Hou, J. (2018). Eukaryotic elongation factor 2 (eEF2) is a potential biomarker of prostate cancer. Pathology & Oncology Research, 24(4), 885-890.

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For research use only. Not intended for any clinical use.

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