Antibodies have been indispensable tools in molecular biology, biochemistry and medical research.
This paper reports on the use of Affimer proteins as research reagents. It shows that Affimer proteins represent complementary affinity reagents to antibodies for various molecular and cell biology applications.
An ultraefficient cap-exchange protocol (UCEP) that can convert hydrophobic quantum dots (QDs) into stable, biocompatible, and aggregation-free water-dispersed ones at a ligand:QD molar ratio (LQMR) as low as 500, some 20−200-fold less than most literature methods, has been developed.
Conventional immunoassays rely on antibodies that provide high affinity, specificity, and selectivity against a target analyte.
Selection methods are used to identify Affimers that recognise α-helix mimicking
To enable multiplexed protein analysis through the use of microarrays, reliable molecules capable of specifically binding to a protein of interest with high affinity are required. Further, this specificity and affinity must be retained upon immobilization to the microarray surface.
Biosensors with high sensitivity and short time-to-result that are capable of detecting biomarkers in body fluids such as serum are an important prerequisite for early diagnostics in modern healthcare provision.
The B-cell CLL/lymphoma-2 (Bcl-2) family of proteins are important regulators of the intrinsic pathway of apoptosis, and their interactions, driven by Bcl-2 homology (BH) domains, are of great interest in cancer research.
Adhirons (commercialised as Affimer reagents) are robust, well expressing, peptide display scaffold proteins, developed as an effective alternative to traditional antibody binding proteins for highly specific molecular recognition applications. Read More
The HIF-1α/p300 protein–protein interaction plays a key role in tumor metabolism and thus represents a high value target for anticancer drug-development.