Structures of bacterial immunoglobulin-binding domains and their complexes with immunoglobulins
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Real-time monitoring of papain digestion of antibodies immobilized with various strategies by optical interferometry
2023, International Journal of Biological MacromoleculesReal-time kinetics and affinity analysis of the interaction between protein A and immunoglobulins G derived from different species on silica colloidal crystal films
2022, Colloids and Surfaces B: BiointerfacesReshaping nanobodies for affinity purification on protein a
2020, New BiotechnologyCitation Excerpt :Alternative purification methods are being explored, such as purification on Staphylococcus aureus Protein A (SpA) [12]. SpA comprises five homologous domains, each folding into three alpha-helices [13]. Due to its ability to interact with human immunoglobulins (Ig) in a non-antigen specific manner, SpA is widely used as a biochemical research tool or as an affinity reagent for isolation of recombinant Ig [14–16].
Engineering of Protein A for improved purification of antibodies and Fc-fused proteins
2020, Approaches to the Purification, Analysis and Characterization of Antibody-Based TherapeuticsSelf-assembled protein nanocarrier for intracellular delivery of antibody
2017, Journal of Controlled ReleaseCitation Excerpt :We sought to explore its utility as a vehicle for cytosolic delivery of antibodies by fusing Protein A domain B (SPAB) to Hex spaced by four repeats of a flexible glycine-serine linker (Supplementary Fig. S1). SPAB has nanomolar binding affinity to the Fc region of IgG and its subclasses from various mammalian species [22]. Hexahistidine (H6) was terminally appended to function as a potential endosomolytic motif in addition to an affinity tag for nickel–NTA purification.