| Protino® technology and products |
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| Features |
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Protino® Ni-IDA
Purification of polyhistidine (His)-tagged
proteins |
Protino® Ni-TED
Purification of polyhistidine (His)-tagged
proteins |
| Technology |
Affinity chromatography
(IMAC, immobilized metal ion affinity chromatography) |
Affinity chromatography
(IMAC, immobilized metal ion affinity chromatography) |
| Material / backbone |
Macroporous silica with immobilized Ni2+ |
Macroporous silica with immobilized Ni2+ |
| Format |
Dry material |
Dry material |
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Dry bulk resin, for gravity-flow chromatography, batch binding, MPLC (e.g., FPLCTM) |
Dry bulk resin, for gravity-flow chromatography, batch binding, MPLC (e.g., FPLCTM) |
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Gravity-flow columns filled with dry Ni-IDA
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Gravity-flow columns filled with dry Ni-TED |
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96-well plates filled with dry Ni-IDA |
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| Procedure |
Principle: interaction between the His-tag
of the recombinant protein and immobilized Ni2+ ions
• Elution with imidazole (structure analogon
of histdine, replacement reaction)
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Principle: interaction between the His-tag of the recombinant protein and immobilized Ni2+ ions
• Elution with imidazole (structure analogon
of histdine, replacement reaction) |
| Features |
Dry material, fast and easy handling,
storage at room temperature
Protino® Ni-IDA
IDA (iminodiacetic acid) as chelating ligand
Three binding sites for the His-tag (—>)
High protein yield and high purity
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Dry material, fast and easy handling,
storage at room temperature
Protino® Ni-TED
TED (tris(carboxymethyl) ethylendiamin) as chelating ligand
One binding site for the His-tag (—>)
Highest purity of isolated proteins
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| Features (continued) |
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Protino® Ni-NTA
Purification of polyhistidine (His)-tagged
proteins |
Protino® Glutathione Agarose 4B
Purificatin of Glutathione-S-transferase (GST)-tagged proteins |
| Technology |
Affinity chromatography
(IMAC, Immobilized metal ion affinity chromatography) |
Affinity chromatography |
| Material / backbone |
6 % beaded agarose (cross-linked), precharged with Ni2+ |
4 % beaded agarose with immobilized glutathione |
| Bead site |
45-165 µm |
90 µm |
| Form |
50 % aqueous suspension containing
30 % ethanol |
75 % aqueous suspension containing
20 % ethanol |
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Bulk resin, for gravity-flow chromatography, batch binding, MPLC (e.g., FPLC™)
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Bulk resin, for gravity-flow chromatography, batch binding, MPLC (e.g., FPLC™)
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FPLC™ columns filled with Ni-NTA agarose |
FPLC™ columns filled with Glutathione Agarose 4B |
| Procedure |
Principle: interaction between the
His-tag of the recombinant protein
and immobilized Ni2+ ions
• Elution with imidazole (structure
analogon of histdine, replacement
reaction) |
Principle: interaction between the
GST-tag of the recombinant protein
and immobilized glutathione
• Elution with free glutathion (substrate
of Glutathione-S-transferase) |
| Features |
High binding affinity and high capacity
Ready-to-use and cost-saving
Protino® Ni-NTA
NTA (nitrilotriacetic acid) as chelating ligand
Two binding sites for the His-tag (—>)
Highest protein yield and high purity
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Highest performance and cost-saving,
equivalent to Glutathione Sepharose™ 4B
Suitable for small proteins, large protein complexes, proteins with low expression rates
Protino® Glutathione Agarose 4B
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