Beads & Microspheres

TargetMol Mag Beads NHS (30-150 μm) are modified with NHS groups on the surface to form stable peptide bonds with proteins and other molecules with primary amine groups for affinity purification of antibodies, antigens and other biomolecules. In contrast to traditional carboxyl and amino magnetic beads, magnetic beads with NHS groups on the surface do not require prior activation with EDC/NHS or glutaraldehyde. The biologic ligands containing primary amines can be covalently coupled to the beads by simply dissolving the biologic ligands in coupling buffer, and then mixing the proteins with the NHS beads for 1~2 h at room temperature. The bead coupling process must be carried out in a buffered solvent that does not contain any amines. The beads are separated from the solvent manually using a magnetic separation rack. Automated equipment is also available and is suitable for multi-sample screening.

TargetMol Protein A/G Immunomagnetic Beads enables Protein A/G to cover superparamagnetic microspheres with high density by utilizing bio-nano technology. Protein A/G Immunomagnetic Beads can be used for the immunoprecipitation (IP) of proteins, protein complexes, protein-nucleic acid complexes, and other antigens. This product is suitable for antigen samples derived from cell lysates, cell culture supernatants, serum, ascites, and other sources.

TargetMol Protein A Immunomagnetic Beads enables Protein A to cover superparamagnetic microspheres with high density by utilizing bio-nano technology. Protein A Immunomagnetic Beads can be used for the immunoprecipitation (IP) of proteins, protein complexes, protein-nucleic acid complexes, and other antigens. This product is suitable for antigen samples derived from cell lysates, cell culture supernatants, serum, ascites, and other sources.

TargetMol Magrose Beads Protein A (30-150 μm) are antibody purification beads that utilize bio-nanosurface technology to covalently encapsulate Protein A onto the surface of NHS-activated superparamagnetic microspheres in a high-density, targeted manner to form composite particles. TargetMol Magrose Beads Protein A (30-150 μm) have a large specific surface area, which dramatically reduces the time required for antibody adsorption. Antibody adsorption can be completed in less than 10 minutes and antibody purification in less than 30 minutes. The product is reusable. Users can choose the type of beads according to the source and subtype of the target antibody.

TargetMol Magrose Beads Protein A (10-30 μm) are antibody purification beads that utilize bio-nanosurface technology to covalently encapsulate Protein A onto the surface of NHS-activated superparamagnetic microspheres in a high-density, targeted manner to form composite particles. TargetMol Magrose Beads Protein A (10-30 μm) have a large specific surface area, which dramatically reduces the time required for antibody adsorption. Antibody adsorption can be completed in less than 10 minutes and antibody purification in less than 30 minutes. The product is reusable. Users can choose the type of beads according to the source and subtype of the target antibody.

TargetMol Magrose Beads Protein G (30-150 μm) are antibody purification beads that utilize bio-nanosurface technology to covalently encapsulate Protein A onto the surface of NHS-activated superparamagnetic microspheres in a high-density, targeted manner to form composite particles. TargetMol Magrose Beads Protein G (30-150 μm) have a large specific surface area, which dramatically reduces the time required for antibody adsorption. Antibody adsorption can be completed in less than 10 minutes and antibody purification in less than 30 minutes. The product is reusable. Users can choose the type of beads according to the source and subtype of the target antibody.

TargetMol His-tag Protein Purification Beads IDA-Nickel is a new type of superparamagnetic functional material designed for efficient and rapid purification of His-tag proteins. It can directly extract high-purity target proteins from biological samples in one step using the magnetic separation method, which greatly simplifies the purification process and improves efficiency. The method is suitable for scientific research and industrial areas to facilitate the purification of his-tag protein. Based on magnetic agarose microspheres, the His-tag protein purification beads activate and couple iminodiacetic acid (IDA) or nitrilotriacetic acid (NTA). Then, they chelate respectively nickel (Nickel) and cobalt (Cobalt) ions. IDA has a relatively strong binding affinity with His-tag proteins and has a higher loading capacity but lower specificity, while NTA has the opposite characteristics. Nickel and Cobalt ions have different properties at a binding capacity of target proteins and non-specif

TargetMol His-tag Protein Purification Beads IDA-Cobalt is a new type of superparamagnetic functional material designed for efficient and rapid purification of His-tag proteins. It can directly extract high-purity target proteins from biological samples in one step using the magnetic separation method, which greatly simplifies the purification process and improves efficiency. The method is suitable for scientific research and industrial areas to facilitate the purification of his-tag protein. Based on magnetic agarose microspheres, the His-tag protein purification beads activate and couple iminodiacetic acid (IDA) or nitrilotriacetic acid (NTA). Then, they chelate respectively nickel (Nickel) and cobalt (Cobalt) ions. IDA has a relatively strong binding affinity with His-tag proteins and has a higher loading capacity but lower specificity, while NTA has the opposite characteristics. Nickel and Cobalt ions have different properties at a binding capacity of target proteins and non-specif

TargetMol His-tag Protein Purification Beads NTA-Nickel is a new type of superparamagnetic functional material designed for efficient and rapid purification of His-tag proteins. It can directly extract high-purity target proteins from biological samples in one step using the magnetic separation method, which greatly simplifies the purification process and improves efficiency. The method is suitable for scientific research and industrial areas to facilitate the purification of his-tag protein. Based on magnetic agarose microspheres, the His-tag protein purification beads activate and couple iminodiacetic acid (IDA) or nitrilotriacetic acid (NTA). Then, they chelate respectively nickel (Nickel) and cobalt (Cobalt) ions. IDA has a relatively strong binding affinity with His-tag proteins and has a higher loading capacity but lower specificity, while NTA has the opposite characteristics. Nickel and Cobalt ions have different properties at a binding capacity of target proteins and non-specif