Genome-wide identification of transcription factor (TF) binding sites is pivotal to our understanding of gene expression regulation. Although much progress has been made in the determination of potential binding regions of proteins by chromatin immunoprecipitation, this method has some inherent limitations regarding DNA enrichment efficiency and antibody necessity. Here, we report an alternativ...

We present the directed immobilization of recombinant antibody fragments as ligands for general immunoaffinity chromatography methods. It is based on fusion proteins of scFv fragments with several chitinbinding domains which can be immobilized directly from a crude bacterial lysate on inexpensive chitin beads for the purification of proteins without any gradient or detector. It has been used wi...

purification of parasitic antigens is a major activity in immunoparasitology because of its application in immunodiagnosis, vaccination analysis of immunopathology, preparation of monocolomal antibody and finding out the cross reactive antigens versus specific antigens of a parasite. in this survey f2 ultrafiltration excretory secretory antigens of ascaris lumbricoides and toxocara cati were se...

The purification of functional proteins is a critical pre-requisite for many experimental assays. Immunoaffinity chromatography, one of the fastest and most efficient purification procedures available, is often limited by elution conditions that disrupt structure and destroy enzymatic activity. To address this limitation, we developed polyol-responsive antibody mimetics, termed nanoCLAMPs, base...

background: the purity and correct folding of a recombinant protein is critical for any structural, biochemical and vaccine design studies. plasmodium vivax duffy binding protein-ii is a leading vaccine candidate for vivax malaria. in the present study, the purification process of recombinant dbp-ix (a variant form of pvdbp-ii) was optimized to achieve the highest yield and purity. moreover, na...

purification development for antibodies with affinity, hydrophobic-interaction, and ionexchange chromatography (1). Fahrner et al. discuss the importance of considering the optimal flow rate on protein A affinity chromatography and suggest that higher flow rates will reduce process time significantly without significantly affecting process capacity (2). Notwithstanding these good publications, ...

We have developed a rapid and sensitive thin film assay for in-process monitoring of target protein purification. This novel biosensor method provides rapid (5-min) visual evaluation of column purification fractions. The method can be used to monitor the efficiency of purification and potential loss of protein if the column binding capacity is exceeded. The eluted fractions containing the highe...

An anti-hapten IgG was covalently immobilized on glutaraldehyde-activated alginate-chitosan gel beads. The antibody immobilization efficiency was influenced by glutaraldehyde-bead reaction time, IgG concentration and pH. In addition, immobilization conditions such as glutaraldehyde and antibody concentrations influenced antibody hapten binding affinity. The immobilized IgG on the beads was stab...

Hens (White Leghorn) were immunized with different protein antigens and antibodies were isolated from eggs by PEG precipitation. To determine experimental conditions under which optimal antibody titers are reached the antigen dose and the mode of application were varied. Injecting the antigen three times every four weeks in the absence of adjuvant led to a phase like immune response. A plateau ...