Scientific Library

Ras and Rho family members are small G proteins involved in the regulation of actin-dependent cell processes such as motility, growth, and intracellular trafficking. Furthermore, dysfunctions of Ras and

Cell culture under oxygen controlled conditions: an improvement towards more predictive results

Oxygen concentration in tissues is a key factor for cell and organ survival. In normal conditions, partial

Actin can be stained in living and fixed cells to determine and follow the structure and function of the cytoskeleton. The actin cytoskeleton is a very dynamic and labile structure in the living cell,

In this post, I invite you to discover some state-of-the art methods to measure the activation of the most prominent small G proteins. In future posts, we'll

In my previous post Small GTPases: Measuring small G protein activation I looked at state-of the-art methods for measuring the activation of small G proteins, such as RhoA, Rac1, Cdc42, and the proto-oncogen

You suspect your protein binds to microtubules? That it might stabilize or destabilize these filamentous structures? Then this post is here to help you to find a meaningful assay to validate your assumption.

Recently, I issued a post about a method which allows measuring microtuble binding capabilities of proteins of interest. Today, I invite you to look at methods for

In this post, I'd like to take a look at the current understanding of tubulin PTMs, that include tyrosination/detyrosination, Δ2-tubulin formation, acetylation, phosphorylation, ubiquitination, glutamylation,

Today, I'd like to give you an overview about methods in actin research with validated R&D products and kits which will allow you to measure binding to actin and effects on the polymerisation dynamics

As is already known, multiple families of small GTPases (Ras, Arf and Rho families) make up the Ras GTPase superfamily. Due to their role as molecular switches in cell signalling (active GTP-bound state

This month, a new leap forward in gene editing has been published in Nature under the title 'Search-and-replace genome editing without double-strand breaks or donor DNA'. DOI: 10.1038/s41586-019-1711-4.