Monoclonal validated for Post-Translational Modification studies

Knowing the Human genome better has allowed major advancements in Personalised Medicine. Nowadays, we can know (if we want) the likelihood to develop a given disease and/or how we will react to different pharmacological treatments. Examples of this include diseases like breast cancer (for diagnosis or estimation of likelihood) and lung cancer (for response to treatment), to name just a few.

That said, our genotype does not have the last word. Research in the last couple of decades has shown the power of other regulatory mechanisms, that may enhance or diminish the effect that our genotype will have on our health. Starting from basic healthy life styles, to other more subtle mechanisms, our genotype defines us, but not completely. Above genetics, we have epigenetics… and everything at the protein level. This post will focus on Post-Translational Modifications (PTM), because, after all, it’s the proteins that are the final effectors of a given response to a treatment or to an environmental stimulus.

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Citrullination: Taking the Charge out of Arg

Protein citrullination (a.k.a. deimination) is a novel arginine-directed post-translational modification (PTM) that results in a permanent change in the targeted protein. PeptidylArginine Deiminases (PADs) mediate the calcium-dependent deimination of the guanidino group of Arginine side chains to form an ureido group and the non-standard amino acid citrulline.

Some biologically relevant proteins known to be citrullinated include Keratin, Filaggrin, Trichohyalin, Vimentin, Myelin Basic Protein (MBP), Histones, alpha-Enolase, Fibrinogen, Fibrins, Collagen type I and II, beta-Actin, and Tubulin 9-11… It is noteworthy that several of these proteins are part of the cytoskeleton and/or are structural in nature.


Citrullination of peptidyl-arginine by peptidylarginine deiminases (PADs).

In their October newsletter, Cytoskeleton Inc. presents an overview about the consequences of citrullination, especially referring to cytoskeleton proteins such as Vimentin.

Interested in this exciting new PTM mechanism?

Download your free copy of the review:
Citrullination: Taking the Charge out of Arg


SUMO and cellular cytoskeletal partners

In the August 2014 edition of their newsletter, Cytoskeleton Inc. bring us an overview of SUMO activation and deconjugation processes, together with their role on cytoskeletal proteins (actin, tubulin…).

For the record, SUMO (for Small Ubiquitin-like Modifiers) is a family of small proteins that is covalently attached to (or detached from) cellular proteins. Such post-translational modification (called SUMOylation) modulates cellular architecture and numerous activities, including response to stress, progression through the cell cycle, transport, mobility…

Interested in reading more about SUMOylation of cytoskeletal proteins?

Download your free copy of the review “SUMOylation: A Post-translational Modification Targeting  Cytoskeletal Protein“!

3 monoclonals to discriminate free Ubiquitin from linear and polyubiquitin chains

Ubiquitin (Ub) is an 8 kDa  highly conserved polypeptide, commonly expressed in eukaryotic cells. Ub is added to lysine residues of the target proteins. This post-translational modification (known as ubiquitination) is made through the sequential action of 3 enzymes (E1 Ub activating enzyme, E2 conjugating enzyme and E3 ligase).

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