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Human Polyclonal EIF5A Primary Antibody for ELISA, WB - ABIN4307667
Koettnitz, Kappel, Baumruker, Hauber, Bevec: The genomic structure encoding human initiation factor eIF-5A. in Gene 1994
EIF5A protein level is increased during pancreatic ductal adenocarcinoma progression with the highest levels of expression observed in metastatic cell populations.Kras protein expression is controlled by a self-regulating feedforward mechanism mediated by eIF5A-PEAK1.
The study identifies eIF5A as a key requirement for autophagosome formation and demonstrates the importance of translation in mediating efficient autophagy. eIF5A is required for lipidation of LC3B and its paralogs and promotes autophagosome formation.
Silencing of the eIF5A-1 gene could induce the apoptosis of HPV 16 E6-infected cervical carcinoma cells.
EIF5A1 is a vital regulator of epithelial ovarian cancer proliferation and progression.
Molecular structure of the exportin Xpo4 in complex with RanGTP and the hypusine-containing translation factor eIF5A has been reported.
the depletion of eIF5A leads to endoplasmic reticulum stress, an unfolded protein response and up-regulation of chaperone expression in HeLa cells.
Findings indicate that eIF5A-PEAK1-YAP signaling contributes to PDAC development by regulating an STF program associated with increased tumorigenicity.
eIF5A1 isoform A has a role in mitochondrial function.
These results suggest that binding of eEF2 to the ribosome alters its conformation, resulting in a weakened affinity of eIF5A and impairment of this interplay compromises cell growth due to translation elongation defects.
eIF5A-2 protein was highly expressed in gastric cancer tissues
Upregulation of translation initiation factor 5a observed in thalassemia is a novel finding and plays a protective role toward cell survival under oxidative stress.
Our results suggest that functional, hypusinated eIF5A is necessary for HIF-1alpha expression during hypoxia and that eIF5A is an attractive target for cancer therapy.
findings also implicate the eIF5A/RhoA/ROCK module as a potential new therapeutic target to treat metastatic PDAC cells
eIF5A has been shown to regulate a number of gene products specifically, termed the eIF5A regulon, and its role in translating proline-rich sequences has recently been identified.
eIF5A proteins utilize PEAK1 as a downstream effector to drive pancreatic ductal adenocarcinoma (PDAC) pathogenesis.
Mature eIF5A (hypusinated form) is not involved in the autophagic pathway.
The findings that eIF5A and EF-P are important for specific cellular processes and play a role in the relief of ribosome stalling caused by specific amino acid sequences
Data suggest a regulatory mechanism for the pro-apoptotic protein eukaryotic translation initiation factor 5A1 (eIF5A1) in which its level is possibly modulated by NF-kappaB in lung cells.
Data indicate that the signal of EIF5A2, MYCN, and MCL1 genes is decreased in hydroxyurea (HU) and gemcitabine (GEM) treated UACC-1598 ovarian cancer cell line.
mature eIF5A controls a translational network of cancer-driving genes, termed the eIF5A regulon, at the levels of mRNA abundance and translation
our results provide the first genetic evidence that the hypusine modification in eIF-5A is crucial for homeostasis in mammals
knockout of either the eIF5A-1 gene (Eif5a) or of the deoxyhypusine synthase gene (Dhps) caused early embryonic lethality in mice, indicating the essential nature of both eIF5A-1 and deoxyhypusine synthase in mammalian development
These results point to a new functional role for eIF5A, relating it to embryogenesis, development, and cell differentiation.
a decrease in either active eIF5A or polyamines inhibits cell growth, indicating that eIF5A and polyamines are independently involved in cell growth
Results indicate that the N-terminal extension of the eukaryotic eIF5A contributes in signaling this protein to nuclear localization, despite of bearing no structural similarity with classical nuclear localization signals.
Eukaryotic initiation factor 5A (eIF5A) (eIF-4D, eIF-5A) stimulates ribosomal peptidyltransferase activity, transport of HIV-1-mRNAs and binds exportins 1 and 4. Contains hypusine at lys 50. Mouse EIF5A1 and EIF5A2 encode two isoforms: eIF5AI and eIF5AII.
The deduced bovine eIF5A protein is 100% identical to human Eif5A.
phosphorylation of Ser(2) plays a role in regulation of nucleocytoplasmic shuttling of eIF5A in plant cells
Results describe the identification and characterization of nero, the Drosophila melanogaster deoxyhypusine hydroxylase (DOHH) homologue, and indicate that nero and eIF5A are required for cell growth and affect autophagy and protein synthesis.
This gene encodes an elongation initiation factor, which participates in protein synthesis. The encoded protein also plays roles in mRNA metabolism, cell proliferation, and cell cycle control. This protein contains a modified lysine residue called hypusine, which appears to be necessary for its function. Alternatively spliced transcript variants have been described. Related pseudogenes exist on chromosomes 2, 5, and 19.
, eukaryotic initiation factor 5A
, eukaryotic translation initiation factor 5A-1
, rev-binding factor
, eukaryotic translation initiation factor 5A
, translation initiation factor 5A
, eukaryotic translation initiation factor 5a
, initiation factor 5a
, putative eukaryotic initiation factor 5a
, eukaryotic translation factor 5A
, eukaryotic initiatin factor 5A (3)
, eukaryotic translation initiation factor 5A L homeolog
, translation initiation factor eIF-5A