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Arginylation-Specific Antibody Production Services

Creative Biolabs can offer the customers with highly affinity arginylation-specific antibody discovery and production services based on the excellent High-Affi™ technology. These antibodies are produced by optimized immunization with KLH-conjugated synthetic arginylation modified peptides and purified by affinity chromatography. They do not cross-react with unmodified peptides.

According to the conventional theory, Ate1 transfers Arg from tRNA onto the N-terminally exposed amino group of the acceptor protein, forming a peptide bond (circled on the bottom of the diagram). The Recent finding also demonstrates an example of Arg addition to the side chain of the Glu residue of neurotensin (circled on the side of the diagram). If mediated by Ate1, this reaction constitutes an additional or alternative mechanism of protein arginylation. Fig. 1 Summary of the arginylation reaction
(Saha S and Kashina A 2011)

The characteristics of arginylation

Protein arginylation was an originally discovered post-translational modification (PTM) which was found to be transferred Arg from arginyl tRNA onto existing proteins with the help of arginyltransferase (Arginine Transfer Enzyme 1, ATE1). Although protein arginylation was proved to be a tRNA-dependent modification, it did not require any other components of the translation machinery. It should be noted that this kind of modification is different from enzymes mediating post-translational glycylation, glutamylation, and tyrosination, which do not utilize aminoacyl-tRNA, described primarily for tubulin. Even more amazing, this ribosome-independent amino acid incorporation was only observed in prokaryotes using Leu and Phe and in eukaryotes using Arg. Therefore, protein arginylation is highly conserved in evolution.

The arginylation reaction

It has been found that Ate1 conduct the Arg-transfer reaction on its own, with no requiring of ATP or any other protein components besides the substrate. Recent studies showed that arginylation occurs not only on N-terminally exposed amino group but also on a mid-chain Glu residue in the formation of a peptide bond with the carboxy group of the added Arg.

The substrates of arginylation

Growing evidence demonstrates that a majority of proteins in different organisms, cell types, and subcellular fractions can take place post-translational arginylation. It has been proven that secreted proteins can be arginylated after the removal of signal peptides. It was also found that some regulatory peptides and hormones that exist in the plasma and extracellular liquids can serve as substrates in the arginylation reaction. In addition, other arginylated proteins have been identified in multiple studies including chromosomal proteins, ornithine decarboxylase, as well as some cytosol proteins in hepatocytes.

The functions and related diseases of arginylation

Evidence shows that knockout of Ate1 starting with Drosophila results in embryonic lethality. Recent work also demonstrated protein arginylation played an essential role in multiple physiological processes such as embryogenesis, stress and heat shock, aging, protein degradation, and regenerative processes. The dysfunctions of arginylation result in embryonic lethality, impaired angiogenesis, abnormal cardiac morphogenesis, mental retardation, and infertility.

Recent work also demonstrated protein arginylation played an essential role in multiple physiological processes such as embryogenesis, stress and heat shock, aging, protein degradation, and regenerative processes. Fig. 2 Major biological pathways regulated by arginylation. (Kashina A. 2014)

Although arginylation has been found to modify some proteins and play multiple functions in eukaryotes, site-specific functions have not been reported. Creative Biolabs has been working in the field of post-translational modification antibody discoveries for many years. You can find the most comprehensive and highest quality of antibodies in our companies.

Creative Biolabs can provide a comprehensive list of PTM-specific antibody production services of your choice.


References

  1. Saha S and Kashina A. (2011) “Posttranslational arginylation as a global biological regulator”. Dev Biol, 358(1): 1-8.
  2. Kashina A. (2014) “Protein arginylation, a global biological regulator that targets actin cytoskeleton and the muscle”. Anat Rec, 297(9): 1630-1636.



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