Mutagenesis

Reliable Mutagenesis for Targeted Protein Engineering

In vitro site-directed mutagenesis is an invaluable technique for studying protein structure-function relationships, gene expression, and for carrying out vector modification. Over the past two decades, this critical technique has enabled researches to explore critical aspects of the role proteins play in cellular systems, and has enabled the field of protein engineering to emerge, as researchers develop novel protein structures for study and downstream application.

QuikChange Primer Design Program available for QuikChange users.

Agilent Technologies—and its Stratagene Products division—is a pioneer in the field of mutagenesis, with a deep heritage of innovation and reliability. Through an innovative portfolio of site-directed and random mutagenesis kits, Agilent helps researchers investigate—and publish on—protein structure and function. Agilent’s QuickChange site-directed mutagenesis kits enable multiple point mutations without subcloning, streamlining the mutagenesis process, while our GeneMorph kits deliver a balanced mutational spectrum.

For more than two decades, Agilent has developed mutagenesis tools that deliver results you can count on.

Figure
hOGG1 relocalisation to nuclear speckles is not dependent on the recognition of the lesion 8-oxoG. (A) Fpg- and T4-endoV-sensitive sites and single-strand breaks (ssb) were measured by alkaline elution in non-irradiated (NI) and UVA-irradiated cells. Bars represent the average of at least three determinations ± s.d. (B) HeLa cells were transiently transfected with the plasmids encoding hOGG1-GFP or the mutant proteins K249Q-GFP and F319A-GFP. Protein extracts were analysed by western blotting with an anti-hOGG1 antibody. (C) The same protein extracts were assayed for hOGG1 glycosylase activity. S and P indicate the substrate and the product, respectively. (D) Transiently transfected cells were UVA-irradiated and analysed under the confocal microscope. Both mutant proteins K249Q and F319A, as well as the wild-type hOGG1 (green), were able to re-localise into foci co-localising with SC35 (red). Bars, 4 µm.

Reference
UVA irradiation induces relocalisation of the DNA repair protein hOGG1 to nuclear speckles, J. Cell Sci., 120:23 - 32.