Ni-IDA Agarose Resins

CAT.NO	UNIT	PRICE
		$70.00

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Description	Affinity chromatography is a method of separating biochemical mixtures based on highly specific molecular interactions. The Ni-IDA agarose is developed for the purification of proteins with an affinity tag of six consecutive histidine residues. This histidine-metal ion interaction makes one-step purification possible for proteins from any expression system, under native or denaturing conditions. The His-tag sequence binds to Ni²⁺ cations, which are immobilized onto a solid support using iminodiacetic acid groups (IDA). Impurities are removed and the purified His-tagged proteins can be eluted by imidazole or a reduced pH solution. Special Features One-step easy purification protocol from crude lysate to >95% pure protein. Purification under native or denaturing conditions. Ready-to-use for any scale of purification. Protein binding capacity: approx. 20-40 μmol Ni²⁺/ml gel. Economical value. Can be used for successive cycles. Resins and columns formats suitable for batch and gravity purification.
SKU	10011749
Resin Type	Nickel
Applications	Purification of His-tagged proteins. Antibody purification. Assays involving protein-protein and protein-DNA interactions. Structural and functional investigation of proteins.
Description	Affinity chromatography is a method of separating biochemical mixtures based on highly specific molecular interactions. The Ni-IDA agarose is developed for the purification of proteins with an affinity tag of six consecutive histidine residues. This histidine-metal ion interaction makes one-step purification possible for proteins from any expression system, under native or denaturing conditions. The His-tag sequence binds to Ni²⁺ cations, which are immobilized onto a solid support using iminodiacetic acid groups (IDA). Impurities are removed and the purified His-tagged proteins can be eluted by imidazole or a reduced pH solution. Special Features One-step easy purification protocol from crude lysate to >95% pure protein. Purification under native or denaturing conditions. Ready-to-use for any scale of purification. Protein binding capacity: approx. 20-40 μmol Ni²⁺/ml gel. Economical value. Can be used for successive cycles. Resins and columns formats suitable for batch and gravity purification.
SKU	G250
Applications	Purification of His-tagged proteins. Antibody purification. Assays involving protein-protein and protein-DNA interactions. Structural and functional investigation of proteins.
Unit quantity	5.0 ml
Description	Affinity chromatography is a method of separating biochemical mixtures based on highly specific molecular interactions. The Ni-IDA agarose is developed for the purification of proteins with an affinity tag of six consecutive histidine residues. This histidine-metal ion interaction makes one-step purification possible for proteins from any expression system, under native or denaturing conditions. The His-tag sequence binds to Ni²⁺ cations, which are immobilized onto a solid support using iminodiacetic acid groups (IDA). Impurities are removed and the purified His-tagged proteins can be eluted by imidazole or a reduced pH solution. Special Features One-step easy purification protocol from crude lysate to >95% pure protein. Purification under native or denaturing conditions. Ready-to-use for any scale of purification. Protein binding capacity: approx. 20-40 μmol Ni²⁺/ml gel. Economical value. Can be used for successive cycles. Resins and columns formats suitable for batch and gravity purification.
SKU	G251
Applications	Purification of His-tagged proteins. Antibody purification. Assays involving protein-protein and protein-DNA interactions. Structural and functional investigation of proteins.
Unit quantity	25 ml
Description	Affinity chromatography is a method of separating biochemical mixtures based on highly specific molecular interactions. The Ni-IDA agarose is developed for the purification of proteins with an affinity tag of six consecutive histidine residues. This histidine-metal ion interaction makes one-step purification possible for proteins from any expression system, under native or denaturing conditions. The His-tag sequence binds to Ni²⁺ cations, which are immobilized onto a solid support using iminodiacetic acid groups (IDA). Impurities are removed and the purified His-tagged proteins can be eluted by imidazole or a reduced pH solution. Special Features One-step easy purification protocol from crude lysate to >95% pure protein. Purification under native or denaturing conditions. Ready-to-use for any scale of purification. Protein binding capacity: approx. 20-40 μmol Ni²⁺/ml gel. Economical value. Can be used for successive cycles. Resins and columns formats suitable for batch and gravity purification.
SKU	G253
Applications	Purification of His-tagged proteins. Antibody purification. Assays involving protein-protein and protein-DNA interactions. Structural and functional investigation of proteins.
Unit quantity	100 ml

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References

Kim , BY et al. "Corneal Dystrophy-associated R124H Mutation Disrupts TGFBI Interaction with Periostin and Causes Mislocalization to the Lysosome" J Biol Chem 284 (29):19580-19591 (2009). DOI: 10.1074/jbc.M109.013607. Application: Protein Isolation Assays.
How, KY et al. "Whole genome sequencing enables the characterization of BurI, a LuxI homologue of Burkholderia cepacia strain GG4" PeerJ : (2015). DOI: 10.7717/peerj.1117. Application: Protein Purification.