Protino Technology

Protino Ni-NTA – Purification of polyhistidine (His)-tagged proteins

Features

• Highest protein yield and high purity
• 6 % beaded agarose (crosslinked), precharged with Ni²⁺
• Ready to use and cost saving

Protino Ni-NTA principle

Binding

Interaction between the His-tag of the recombinant protein and immobilized Ni²⁺ ions

Elution

Elution with imidazole (structure analogon of histidine, replacement reaction)
Two binding sites for His-tag

Protino Ni-TED – Purification of polyhistidine (His)-tagged proteins

Features

• Highest purity of isolated protein
• Macroporous silica with immobilized Ni²⁺
• Dry material for fast and easy handling

Protino Ni-TED principle

Binding

Interaction between the His-tag of the recombinant protein and immobilized Ni²⁺ ions

Elution

Elution with imidazole (structure analogon of histidine, replacement reaction)
One binding site for His-tag

Protino Ni-IDA – Purification of polyhistidine (His)-tagged proteins

Features

• High protein yield and high purity
• Macroporous silica with immobilized Ni²⁺
• Storage at room temperature

Protino Ni-IDA principle

Binding

Interaction between the His-tag of the recombinant protein and immobilized Ni²⁺ ions

Elution

Elution with imidazole (structure analogon of histidine, replacement reaction)
Three binding sites for His-tag

Protino Glutathione Agarose – Purification of Glutathione‑S‑transferase (GST)-tagged proteins

Features

• Highest performance and cost saving, equivalent to Glutathione Sepharose™ 4B
• 4 % beaded agarose with immobilized glutathione
• Suitable for small proteins, large protein complexes, proteins with low expression rates

Protino Glutathione Agarose 4B principle

Binding

Interaction between the GST-tag of the recombinant protein and immobilized glutathione

Elution

Elution with free glutathione (substrate of Glutathione-S-transferase)

 

 

 

 

 

 

 

 

For more detailed information and documents, click here.