method

form:Solution (100× in ddH2O) , components:Sodium Fluoride,Sodium Orthovanadate,Imidazole etc. , specificity of inhibition:Acid Phosphatase, Alkaline phosphatase, PTPs, ATPases

form:2 Tube Solution (100×) , components:Each Tube has different components , specificity of inhibition:Each Tube has different specificity of inhibition

form:Solution (100× in DMSO) , components:(-)-p-Bromotetramisole oxalate, Cantharidin, Microcystin LR , specificity of inhibition:Alkaline phosphatases, Ser/Thr phosphatases, Acid and PP1 and PP2A

The streptavidin–biotin (SA-Biotin) system is known to have a very high affinity (Kd= 10^-15) and specificity, and is widely used in biochemical field.  TargetMol Mag Beads Streptavidin (2 μm) covalently connects SA to the beads surface through protein-protein coupling method. This enables efficient binding of biotinylated antibodies, nucleic acids, and proteins. The product combines superparamagnetic advantages with unique features including uniform size and regular morphology, facilitating the rapid capture of target molecules and magnetic separation. This product can be used with automated equipment for high-throughput technology.

TargetMol His-tag Protein Purification Magrose 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 magnetic separation method, which greatly simplifies the purification process and improves the efficiency. The method is suitable for scientific research and industrial areas to facilitate the purification of his-tag protein. The His-tag protein purification beads, based on magnetic agarose microspheres, activate and couple iminodiacetic acid (IDA) or nitrilotriacetic acid (NTA). Then, they chelate Nickel and Cobalt ions respectively. 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 binding capacity of target proteins and non-specific adsorption. Nickel magnetic beads have a higher protein loading capacity but slightly lower purity (90%), while Cobalt magnetic beads have a slightly lower protein loading capacity but higher purity (95%). Users can select different types of His-tag protein purification beads based on different purposes.

TargetMol His-tag Protein Purification Magrose 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 magnetic separation method, which greatly simplifies the purification process and improves the efficiency. The method is suitable for scientific research and industrial areas to facilitate the purification of his-tag protein. The His-tag protein purification beads, based on magnetic agarose microspheres, activate and couple iminodiacetic acid (IDA) or nitrilotriacetic acid (NTA). Then, they chelate Nickel and Cobalt ions respectively. 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 binding capacity of target proteins and non-specific adsorption. Nickel magnetic beads have a higher protein loading capacity but slightly lower purity (90%), while Cobalt magnetic beads have a slightly lower protein loading capacity but higher purity (95%). Users can select different types of His-tag protein purification beads based on different purposes.

The Bicinchoninic acid (BCA) assay is a stable, sensitive and highly compatible method for the determination of protein concentration. It is commonly used for quantifying the total amount of proteins after extraction. The detection mechanism of BCA assay involves two reations. The first reation is based on the biruet reaction, in which the protein chelates with copper (II) ion in an alkaline environment and reduces the copper (II) to copper (I), forming a blue complex. The second reaction is the chelation of BCA with the cuprous ion, resulting in an intense purple color. The purple colored reaction product is formed by the chelation of two molecules of BCA with one cuprous ion. The complex exhibits a strong linear absorbance at 562 nm with increasing protein concentrations.

The streptavidin–biotin (SA-Biotin) system is known to have a very high affinity (Kd= 10^-15) and specificity, and is widely used in biochemical field.  TargetMol Mag Beads Streptavidin (5 μm) covalently connects SA to the beads surface through protein-protein coupling method. This enables efficient binding of biotinylated antibodies, nucleic acids, and proteins. The product combines superparamagnetic advantages with unique features including uniform size and regular morphology, facilitating the rapid capture of target molecules and magnetic separation. This product can be used with automated equipment for high-throughput technology.

The streptavidin–biotin (SA-Biotin) system is known to have a very high affinity (Kd= 10^-15) and specificity, and is widely used in biochemical field.  TargetMol Mag Beads Streptavidin (3 μm) covalently connects SA to the beads surface through protein-protein coupling method. This enables efficient binding of biotinylated antibodies, nucleic acids, and proteins. The product combines superparamagnetic advantages with unique features including uniform size and regular morphology, facilitating the rapid capture of target molecules and magnetic separation. This product can be used with automated equipment for high-throughput technology.

The streptavidin–biotin (SA-Biotin) system is known to have a very high affinity (Kd= 10^-15) and specificity, and is widely used in biochemical field.  TargetMol Mag Beads Streptavidin (300 nm), Sterile covalently connects SA to the beads surface through protein-protein coupling method. This enables efficient binding of biotinylated antibodies, nucleic acids, and proteins. The product combines superparamagnetic advantages with unique features including uniform size and regular morphology, facilitating the rapid capture of target molecules and magnetic separation. This product can be used with automated equipment for high-throughput technology.

TargetMol His-tag Protein Purification Magrose 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 magnetic separation method, which greatly simplifies the purification process and improves the efficiency. The method is suitable for scientific research and industrial areas to facilitate the purification of his-tag protein. The His-tag protein purification beads, based on magnetic agarose microspheres, activate and couple iminodiacetic acid (IDA) or nitrilotriacetic acid (NTA). Then, they chelate Nickel and Cobalt ions respectively. 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 binding capacity of target proteins and non-specific adsorption. Nickel magnetic beads have a higher protein loading capacity but slightly lower purity (90%), while Cobalt magnetic beads have a slightly lower protein loading capacity but higher purity (95%). Users can select different types of His-tag protein purification beads based on different purposes.

The streptavidin–biotin (SA-Biotin) system is known to have a very high affinity (Kd= 10^-15) and specificity, and is widely used in biochemical field.  TargetMol Mag Beads Streptavidin (2.8 μm) covalently connects SA to the beads surface through protein-protein coupling method. This enables efficient binding of biotinylated antibodies, nucleic acids, and proteins. The product combines superparamagnetic advantages with unique features including uniform size and regular morphology, facilitating the rapid capture of target molecules and magnetic separation. This product can be used with automated equipment for high-throughput technology.

The streptavidin–biotin (SA-Biotin) system is known to have a very high affinity (Kd= 10^-15) and specificity, and is widely used in biochemical field.  TargetMol Mag Beads Streptavidin (1 μm) covalently connects SA to the beads surface through protein-protein coupling method. This enables efficient binding of biotinylated antibodies, nucleic acids, and proteins. The product combines superparamagnetic advantages with unique features including uniform size and regular morphology, facilitating the rapid capture of target molecules and magnetic separation. This product can be used with automated equipment for high-throughput technology.