Preparation and characterization of novel IgG affinity resin coupling anti-Fc camelid single-domain antibodies

Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences

Volumn 983-984, Issue , 2015, Pages 26-31

  Tu, Zhui ^a   Xu, Yang ^a   Fu, Jinheng ^a,b   Huang, Zhibing ^a   Wang, Yao ^a   Liu, Bin ^b   Tao, Yong ^a  

^a NANCHANG UNIVERSITY   (China)

^b Shanxi Defcred Biotechnology Co Ltd   (China)

Author keywords

Affinity chromatography; Anti Fc; Purification of IgG; Single domain antibody

Indexed keywords

AFFINITY CHROMATOGRAPHY; CHAINS; ESCHERICHIA COLI; LIGANDS; PURIFICATION; RESINS;

AFFINITY PURIFICATION; ANTI-FC; BINDING CAPACITIES; HEAVY-CHAIN ANTIBODIES; HIGH THERMAL STABILITY; NACL CONCENTRATION; PHAGE DISPLAY LIBRARIES; SINGLE-DOMAIN ANTIBODIES;

ANTIBODIES;

BACTERIAL PROTEIN; BUFFER; CAMELID SINGLE DOMAIN ANTIBODY; FRAGMENT CRYSTALLIZABLE ANTIBODY; IMMUNOGLOBULIN G; NANOBODY; PROTEIN ANTIBODY; RESIN; SODIUM CHLORIDE; UNCLASSIFIED DRUG; FC RECEPTOR; PROTEIN BINDING; RECOMBINANT PROTEIN;

AFFINITY CHROMATOGRAPHY; ANTIBODY AFFINITY; ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; ENZYME LINKED IMMUNOSORBENT ASSAY; ESCHERICHIA COLI; EXPERIMENTAL RABBIT; HEAT TOLERANCE; HEAT TREATMENT; HUMAN; HYDROGEN BOND; IONIC STRENGTH; MOUSE; NONHUMAN; PH; PHAGE DISPLAY; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; THERMOSTABILITY; ANIMAL; CHEMISTRY; IMMUNOLOGY; ISOLATION AND PURIFICATION; METABOLISM; NEW WORLD CAMELID; PROCEDURES; PROTEIN STABILITY; SOLUBILITY; TEMPERATURE;

CAMELIDAE; ESCHERICHIA COLI; ORYCTOLAGUS CUNICULUS;

ANIMALS; BUFFERS; CAMELIDS, NEW WORLD; CHROMATOGRAPHY, AFFINITY; ELECTROPHORESIS, POLYACRYLAMIDE GEL; HYDROGEN-ION CONCENTRATION; IMMUNOGLOBULIN G; MICE; PROTEIN BINDING; PROTEIN STABILITY; RECEPTORS, FC; RECOMBINANT PROTEINS; RESINS, SYNTHETIC; SINGLE-DOMAIN ANTIBODIES; SOLUBILITY; TEMPERATURE;

EID: 84921326166     PISSN: 15700232     EISSN: 1873376X     Source Type: Journal    
DOI: 10.1016/j.jchromb.2014.12.031     Document Type: Article

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