MPs | Free Full-Text | A Cost-Effective Immobilization Method for MBP Fusion Proteins on Microtiter Plates Using a Gelatinized Starch–Agarose Mixture and Its Application for Convenient Protein–Protein Interaction Analysis
Magnetic nanoparticles for the affinity adsorption of maltose binding protein (MBP) fusion enzymes - Journal of Materials Chemistry (RSC Publishing)
A designed fusion tag for soluble expression and selective separation of extracellular domains of fibroblast growth factor receptors | Scientific Reports
Evaluation of Maltose Binding Protein-Tagged hATR Kinase Domain Catalytic Activity with p53 Ser-15 Phosphorylation | Biochemistry
Maltose-binding protein: a versatile platform for prototyping biosensing - ScienceDirect
NEBExpress® MBP Fusion and Purification System | NEB
Solved Maltose binding protein (MBP) is a protein that binds | Chegg.com
One-step affinity purification of fusion proteins with optimal monodispersity and biological activity: application to aggregation-prone HPV E6 proteins | Microbial Cell Factories | Full Text
Recombinant E. coli Maltose Binding Protein Protein (ABIN5853046)
Tagged Protein Purification | Cytiva
Frontiers | Fusion tags for protein solubility, purification and immunogenicity in Escherichia coli: the novel Fh8 system
Purification of fibroblast growth factor 1 (FGF1) by receptor affinity... | Download Scientific Diagram
The Ability to Enhance the Solubility of Its Fusion Partners Is an Intrinsic Property of Maltose-Binding Protein but Their Folding Is Either Spontaneous or Chaperone-Mediated | PLOS ONE
AB Vector - pAB-MBP™
Maltose Binding Protein Affinity Resin - Amintra (ab270538) | Abcam
Mutations in maltose-binding protein that alter affinity and solubility properties | Applied Microbiology and Biotechnology
Solved Maltose binding protein (MBP) is a protein that binds | Chegg.com
Amylose Resin | NEB
Prokaryotic soluble expression and purification of bioactive human fibroblast growth factor 21 using maltose-binding protein | Scientific Reports
One-step affinity purification of fusion proteins with optimal monodispersity and biological activity: application to aggregation-prone HPV E6 proteins | Microbial Cell Factories | Full Text
