Anti-EIF5A Antibody Picoband® Fluoro550 Conjugated

Eukaryotic translation initiation factor 5A-1 is a protein that in humans is encoded by the EIF5A gene. Eukaryotic initiation factor 5A (eIF5A) is an mRNA-binding protein that is involved in translation elongation and plays an important role in promoting translation of polyproline motifs. The eIF5A (eIF5A1) and eIF5A2 genes encode the two vertebrate eIF5A isoforms. While eIF5A1 is expressed constitutively in all tissues, eIF5A2 is mainly expressed in gonads. eIF5A and eIF5A2 are the only identified proteins that contain the distinctive amino acid hypusine, which is generated posttranslationally from lysine through a highly conserved polyamine metabolism pathway. eIF5A function and hypusine modification are both essential for cell proliferation, as knock down of eIF5A expression or blocking eIF5A hypusine modification suppresses cancer cell proliferation. Interestingly, eIF5A is an identified component of a tumor suppressor network of the polyamine-hypusine axis. Co-suppression of both eIF5A and adenosylmethionine decarboxylase 1 (AMD1) promotes lymphomagenesis in mice, while heterozygous deletions of the corresponding AMD1 and eIF5A genes often occur together in human lymphomas.

Dual specificity mitogen-activated protein kinase kinase 4; MAP kinase kinase 4; MAPKK 4; JNK-activating kinase 1; MAPK/ERK kinase 4; MEK 4; SAPK/ERK kinase 1; SEK1; Stress-activated protein kinase kinase 1; SAPK kinase 1; SAPKK-1; SAPKK1; c-Jun N-terminal kinase kinase 1; JNKK; MAP2K4; JNKK1; MEK4; MKK4; PRKMK4; SEK1; SERK1; SKK1

Dual specificity protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. Essential component of the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. With MAP2K7/MKK7, is the one of the only known kinase to ly activate the stress-activated protein kinase/c-Jun N-terminal kinases MAPK8/JNK1, MAPK9/JNK2 and MAPK10/JNK3. MAP2K4/MKK4 and MAP2K7/MKK7 both activate the JNKs by phosphorylation, but they differ in their preference for the phosphorylation site in the Thr-Pro-Tyr motif. MAP2K4 shows preference for phosphorylation of the Tyr residue and MAP2K7/MKK7 for the Thr residue. The phosphorylation of the Thr residue by MAP2K7/MKK7 seems to be the prerequisite for JNK activation at least in response to proinflammatory cytokines, while other stimuli activate both MAP2K4/MKK4 and MAP2K7/MKK7 which synergistically phosphorylate JNKs. MAP2K4 is required for maintaining peripheral lymphoid homeostasis. The MKK/JNK signaling pathway is also involved in mitochondrial death signaling pathway, including the release cytochrome c, leading to apoptosis. Whereas MAP2K7/MKK7 exclusively activates JNKs, MAP2K4/MKK4 additionally activates the p38 MAPKs MAPK11, MAPK12, MAPK13 and MAPK14.

1. Doerfel, L. K., Wohlgemuth, I., Kothe, C., Peske, F., Urlaub, H., Rodnina, M. V. EF-P is essential for rapid synthesis of proteins containing consecutive proline residues. Science 339: 85-88, 2013. 2. Faundes, V., Jennings, M. D., Crilly, S., Legraie, S., Withers, S. E., Cuvertino, S., Davies, S. J., Douglas, A. G. L., Fry, A. E., Harrison, V., Amiel, J., Lehalle, D., and 12 others. Impaired eIF5A function causes a Mendelian disorder that is partially rescued in model systems by spermidine. Nature Commun. 12: 833, 2021. 3. Gutierrez, E., Shin, B.-S., Woolstenhulme, C. J., Kim, J.-R., Saini, P., Buskirk, A. R., Dever, T. E. eIF5A promotes translation of polyproline motifs. Molec. Cell 51: 35-45, 2013.