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Mouse Anti-EIF5A (AA 66-154) Recombinant Antibody (CBFYE-0191) (CBMAB-E0434-FY)


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Summary

Host Animal
Mouse
Specificity
Human
Clone
CBFYE-0191
Antibody Isotype
IgG2a, κ
Application
ELISA, IF, WB

Basic Information

Immunogen
Partial recombinant from human EIF5A2 with GST tag MW of the GST tag alone is 26 KDa
Specificity
Human
Antibody Isotype
IgG2a, κ
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
Buffer
PBS, pH 7.2
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.
Epitope
AA 66-154

Target

Full Name
Eukaryotic Translation Initiation Factor 5A
Introduction
EIF5A (Eukaryotic Translation Initiation Factor 5A) is a Protein Coding gene. Diseases associated with EIF5A include Human Immunodeficiency Virus Type 1 and Retinitis Pigmentosa 14. Among its related pathways are Metabolism of proteins and Translation Factors. Gene Ontology (GO) annotations related to this gene include protein N-terminus binding. An important paralog of this gene is EIF5AL1.
Entrez Gene ID
1984
UniProt ID
P63241
Alternative Names
Eukaryotic Translation Initiation Factor 5A; Rev-Binding Factor; EIF-5A-1; EIF-5A1; EIF-5A; EIF-4D
Research Area
mRNA-binding protein involved in translation elongation. Has an important function at the level of mRNA turnover, probably acting downstream of decapping. Involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity. With syntenin SDCBP, functions as a regulator of p53/TP53 and p53/TP53-dependent apoptosis. Regulates also TNF-alpha-mediated apoptosis. Mediates effects of polyamines on neuronal process extension and survival. May play an important role in brain development and function, and in skeletal muscle stem cell differentiation. Also described as a cellular cofactor of human T-cell leukemia virus type I (HTLV-1) Rex protein and of human immunodeficiency virus type 1 (HIV-1) Rev protein, essential for mRNA export of retroviral transcripts.
Biological Process
Cellular response to virus Source: UniProtKB
mRNA transport Source: UniProtKB-KW
Positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator Source: UniProtKB
Positive regulation of transcription by RNA polymerase II Source: UniProtKB
Positive regulation of translational elongation Source: UniProtKB
Positive regulation of translational termination Source: InterPro
Protein transport Source: UniProtKB-KW
Tumor necrosis factor-mediated signaling pathway Source: UniProtKB
Cellular Location
Endoplasmic reticulum membrane; Nucleus; Nuclear pore complex; Cytoplasm. Hypusine modification promotes the nuclear export and cytoplasmic localization and there was a dynamic shift in the localization from predominantly cytoplasmic to primarily nuclear under apoptotic inducing conditions.
PTM
Acetylated. Deacetylated by SIRT2.
eIF-5A seems to be the only eukaryotic protein to have a hypusine residue which is a post-translational modification of a lysine by the addition of a butylamino group (from spermidine).
More Infomation

Barba-Aliaga, M., & Alepuz, P. (2022). Role of eIF5A in Mitochondrial Function. International Journal of Molecular Sciences, 23(3), 1284.

Li, H., Wu, B. K., Kanchwala, M., Cai, J., Wang, L., Xing, C., ... & Pan, D. (2022). YAP/TAZ drives cell proliferation and tumour growth via a polyamine–eIF5A hypusination–LSD1 axis. Nature cell biology, 24(3), 373-383.

Faundes, V., Jennings, M. D., Crilly, S., Legraie, S., Withers, S. E., Cuvertino, S., ... & Banka, S. (2021). Impaired eIF5A function causes a Mendelian disorder that is partially rescued in model systems by spermidine. Nature communications, 12(1), 1-13.

Park, M. H., Kar, R. K., Banka, S., Ziegler, A., & Chung, W. K. (2021). Post-translational formation of hypusine in eIF5A: Implications in human neurodevelopment. Amino acids, 1-15.

Bourourou, M., Gouix, E., Melis, N., Friard, J., Heurteaux, C., Tauc, M., & Blondeau, N. (2021). Inhibition of eIF5A hypusination pathway as a new pharmacological target for stroke therapy. Journal of Cerebral Blood Flow & Metabolism, 41(5), 1080-1090.

Cougnon, M., Carcy, R., Melis, N., Rubera, I., Duranton, C., Dumas, K., ... & Pisani, D. F. (2021). Inhibition of eIF5A hypusination reprogrammes metabolism and glucose handling in mouse kidney. Cell Death & Disease, 12(4), 1-14.

Coni, S., Serrao, S. M., Yurtsever, Z. N., Di Magno, L., Bordone, R., Bertani, C., ... & Canettieri, G. (2020). Blockade of EIF5A hypusination limits colorectal cancer growth by inhibiting MYC elongation. Cell death & disease, 11(12), 1-14.

Zhang, H., Alsaleh, G., Feltham, J., Sun, Y., Napolitano, G., Riffelmacher, T., ... & Simon, A. K. (2019). Polyamines control eIF5A hypusination, TFEB translation, and autophagy to reverse B cell senescence. Molecular cell, 76(1), 110-125.

Manjunath, H., Zhang, H., Rehfeld, F., Han, J., Chang, T. C., & Mendell, J. T. (2019). Suppression of ribosomal pausing by eIF5A is necessary to maintain the fidelity of start codon selection. Cell reports, 29(10), 3134-3146.

Turpaev, K. T. (2018). Translation factor eIF5A, modification with hypusine and role in regulation of gene expression. eIF5A as a target for pharmacological interventions. Biochemistry (Moscow), 83(8), 863-873.

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

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