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GE29-0510-21

HisTrap High Performance

GE Healthcare, 29-0510-21, pack of 1 mL

  •  NACRES NA.56

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Properties

Related Categories Additional Affinity Purification, Affinity Chromatography, IMAC Matrices, Molecular Biology, Plant Biotechnology,
shelf life   Please be aware this product may be shipped 90 days before the expiration date. For more information on the batch specific expiration date, please contact technical service.
packaging   pack of 1 mL
mfr. no.   GE Healthcare, 29-0510-21
availability   not available in North America
parameter   flow rate
  4 ml/min (1 ml), 5 ml/min (5ml) flow rate (H2O at room temperature)
  42 psi (H2O at room temperature.)
bed size   7 mm × 25 mm
bed volume   1 mL
column I.D.   7 mm
matrix   highly cross-linked 6% agarose
avg. part. size   34 μm
cleaning   2 - 14 (Ni2+-stripped medium.)
working range   3 - 12 (Ni2+-stripped medium)
capacity   ≥40 mg binding capacity (histidine-tagged protein/ml medium)(H2O at room temperature.)
  ≥40 mg binding capacity (histidine-tagged protein/ml medium)(Protein binding capacity is protein-to-protein dependent.)

Description

General description

HisTrap HP columns are prepacked with Ni Sepharose High Performance and designed for simple, high-resolution purification of histidine-tagged proteins by immobilized metal ion affinity chromatography (IMAC).

Application

HisTrap HP columns are designed for simple, one-step purification of histidine-tagged proteins. The columns are prepacked with Ni Sepharose High Performance, which has high binding capacity and low nickel ion leakage that ensures reliable capture of target protein in repeated IMAC purifications.

Features and Benefits

• High binding capacity, at least 40 mg/ml chromatography medium.
• Compatible with a wide range of reducing agents, detergents, denaturants, and other additives.
• Negligible Ni2+ leakage
• Simple manual operation with a syringe, pump, or chromatography system such as AKTA design

Storage and Stability

Store at 4 to 30 °C (20% Ethanol)

Legal Information

HisTrap is a trademark of Cytiva

Safety & Documentation

Safety Information

Signal word 
Warning
Hazard statements 
Precautionary statements 
RIDADR 
NA 1993 / PGIII

Documents

Certificate of Analysis (COA)

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Protocols & Articles

Protocols

Column packing and preparation for Ion Exchange Chromatography & Chromatafocusing

Appendix 3, extracted from Ion Exchange Chromatography & Chromatofocusing, GE Healthcare, 2007
Keywords: Antimicrobials, Chromatography, Gene expression, Ion Exchange, Purification, Separation

Conditioning Purified Membrane Proteins

Extracted from Purifying Challenging Proteins - Principles and Methods, GE Healthcare, 2007
Keywords: Buffers, Chromatography, Column chromatography, Detergents, Dialysis, Ion Exchange, Precipitation, Reversed-phase chromatography, Solvents, Tagged proteins

Ion Exchange Chromatography Troubleshooting

If only certain peaks are of interest in this well-resolved separation, it may be advantageous to transfer to a step elution in order to save time and buffer. The rest of this section focuses on prac...
Keywords: Absorption, Adsorption, Buffers, Chromatography, Detergents, Digestions, Ion Exchange, PAGE, Precipitation, Sample preparations, Separation, Solvents

Non-volatile and Volatile Buffer Systems

Appendix 2, extracted from Ion Exchange Chromatography & Chromatofocusing, GE Healthcare, 2007
Keywords: Chromatography, Ion Exchange

Performing a purification and on-column refolding of an insoluble histidine-tagged protein from a 100 ml E. coli culture using HisTrap FF 1 ml with ÄKTAprime plus

This procedure uses a HisTrap FF 1 ml column but can also be used with a HisTrap HP 1 ml or a HisTrap FF crude 1 ml column. The procedure uses ÄKTAprime plus but can also be run on other ÄKTA systems...
Keywords: Buffers, Chromatography, Fractionation, Sonication, Tagged proteins

Performing an isolation of recombinant protein complexes

For structural studies and for comprehensive functional studies of multiprotein complexes it is often necessary to isolate protein amounts in the mg range. As mentioned above, pulldown methods are of...
Keywords: Chromatography, Dialysis, Gene expression, Ion Exchange, Scintillation, Tagged proteins

Practical Considerations for IEX Separation

This section covers detailed aspects of each step in an IEX separation, together with practical hints and tips to improve resolution and overall performance. In practice a separation can be summarize...
Keywords: Absorption, Buffers, Cell culture, Chromatography, Detergents, Filtration, Ion Exchange, Nucleic acid denaturation, PAGE, Phase transitions, Precipitation, Sample preparations, Separation, Solvents

Purification of Membrane Proteins

Extracted from Purifying Challenging Proteins - Principles and Methods, GE Healthcare, 2007
Keywords: Adsorption, Buffers, Cell culture, Cell disruption, Characterizations, Chromatography, Degradations, Detergents, Filtration, Immobilization, Ion Exchange, Ligands, PAGE, Sample preparations, Separation, Sonication, Tagged proteins

Sample Preparation in Ion Exchange Chromatography

Appendix 1, extracted from Ion Exchange Chromatography & Chromatofocusing, GE Healthcare, 2007
Keywords: Absorption, Adsorption, Affinity chromatography, Amplification, Buffers, Cell culture, Centrifugation, Chromatography, Detergents, Dialysis, Electrophoresis, Filtration, Indicators, Ion Exchange, Nucleic acid denaturation, PAGE, Precipitation, Purification, Sample preparations, Separation

Selection of Purification Equipment

Appendix 4 extracted from Ion Exchange Chromatography & Chromatofocusing, GE Healthcare, 2007
Keywords: Chromatography, Ion Exchange, Purification, Separation

Sepharose High Performance: Purification with High Resolution

Use Sepharose High Performance media for purification of proteins, peptides or oligonucleotides.
Keywords: Buffers, Chromatography, Detergents, Filtration, High performance liquid chromatography, Ion Exchange, PAGE, Precipitation, Purification, Sample preparations, Separation, Solvents

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