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GE17-5248-02

HisTrap High Performance

GE Healthcare, 17-5248-02, pack of 5 × 5 mL

  •  NACRES NA.56

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Properties

Related Categories Additional Affinity Purification, Molecular Biology, Plant Biotechnology, Plant Proteomics, Protein Purification More...
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 5 × 5 mL
mfr. no.   GE Healthcare, 17-5248-02
parameter   4 ml/min (1 ml), 5 ml/min (5ml) flow rate (H2O at room temperature)
  42 psi (H2O at room temperature.)
bed size   16 mm × 25 mm
bed volume   5 mL
column I.D.   16 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)(H20 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).

HisTrap HP 1 mL and 5 mL 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.

HisTrap HP columns can also be used for the purification of tagged proteins containing shorter or longer polyhistidine tags, such as (histidine)4 or (histidine)10. The shorter (histidine)4 will bind more weakly and the longer (histidine)10 will bind more strongly compared with (histidine)6. This difference in binding strength can be used during purification; since (histidine)10 binds more strongly, a higher concentration of imidazole can be added to the lysed cells. This can facilitate the removal of contaminants that can otherwise be copurified with the tagged target protein.

The high stability and broad compatibility of Ni Sepharose® High Performance maintains biological activity and increases product yield, at the same time as it greatly expands the range of suitable operating conditions.

For convenient scaling up of histidine-tagged protein purification, use 20 mL HisPrep FF 16/10 columns. Ni Sepharose® 6 Fast Flow, the medium prepacked in HisTrap FF and HisPrep FF 16/10 columns, allows high flow rates, which facilitates scale-up of histidine-tagged protein purification.

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)

Analysis Note

To view the Certificate of Analysis for this product, please visit www.gelifesciences.com.

Legal Information

HisPrep is a trademark of Cytiva

HisTrap is a trademark of Cytiva

Sepharose is a registered trademark of Cytiva

Safety & Documentation

Safety Information

RIDADR 
UN1170 - class 3 - PG 3 - Ethanol, solution

Documents

Certificate of Analysis (COA)

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Protocols & Articles

Protocols

Characteristics of Ni Sepharose, Ni Sepharose excel, TALON Superflow, and Uncharged IMAC Sepharose Products

Appendix 1, Extracted from Affinity Chromatography Vol. 2: Tagged Proteins, GE Healthcare, 2016  
Keywords: Affinity chromatography, Buffers, Cell culture, Centrifugation, Chromatography, Detergents, Immobilization, Precipitation, Purification, Tagged proteins

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

Desalting/Buffer Exchange and Concentration for Affinity Chromatography of Tagged Proteins

Desalting at laboratory scale is a well-proven, simple, and very fast method that will rapidly remove low molecular weight contaminants at the same time as transferring the sample into the desired bu...
Keywords: Absorption, Addition reactions, Affinity chromatography, Buffers, Centrifugation, Chromatography, Detergents, Dialysis, Fractionation, Ion Exchange, PAGE, Precipitation, Sample preparations, Separation, Size-exclusion chromatography, Tagged proteins

Handling Inclusion Bodies

Recombinant proteins are most often expressed in the intracellular space, but expression can also be controlled so that the protein is secreted into the periplasmic space or out into the culture medi...
Keywords: Affinity chromatography, Buffers, Chromatography, Detergents, Dialysis, Enzyme activity, Fractionation, Gene expression, Immobilization, Mass spectrometry, Nuclear magnetic resonance spectroscopy, PAGE, Purification, Reversed-phase chromatography, Sample preparations, Separation, Size-exclusion chromatography, Solvents, Sonication, 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

Manual and Automated Purification

Chapter 2, Extracted from Affinity Chromatography Vol. 2: Tagged Proteins, GE Healthcare, 2016
Keywords: Affinity chromatography, Centrifugation, Chromatography, Gene expression, Tagged proteins

Non-volatile and Volatile Buffer Systems

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

Performing High-Throughput Screening Using His MultiTrap HP and His MultiTrap FF 96-Well filter Plates

His MultiTrap™ HP and His MultiTrap™ FF are prepacked, disposable 96-well filter plates for reproducible, high-throughput screening of histidine-tagged recombinant protein expression. Typical applicat...
Keywords: Affinity chromatography, Biochemistry, Buffers, Cell disruption, Centrifugation, Chromatography, Detergents, Dot blot, Gene expression, PAGE, Precipitation, Size-exclusion chromatography, Tagged proteins

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

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

Principles and Standard Conditions for Different Purification Techniques

Appendix 11, Extracted from Affinity Chromatography Vol. 2: Tagged Proteins, GE Healthcare, 2016
Keywords: Affinity chromatography, Chromatography, Detergents, Ion Exchange, Ligands, Precipitation, Reversed-phase chromatography, Separation, Size-exclusion chromatography, Solvents, Tagged proteins

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

Purification of Protein A-Tagged Proteins

Chapter 8, Extracted from Affinity Chromatography Vol. 2: Tagged Proteins, GE Healthcare, 2016
Keywords: Affinity chromatography, Chromatography, Fermentation, Gene expression, Growth factors, Ligands, Separation, Tagged proteins

Purification Using HisTrap HP and HisTrap FF

HisTrap HP and HisTrap FF are 1 ml and 5 ml HiTrap columns packed with Ni Sepharose High Performance or Ni Sepharose 6 Fast Flow, respectively. Sample application, washing,  and elution can be perfor...
Keywords: Affinity chromatography, Buffers, Chromatography, PAGE, Purification, Size-exclusion chromatography, Tagged proteins

Purification of Histidine-Tagged Recombinant Proteins Using Ni Sepharose High Performance

Ni Sepharose High Performance consists of highly cross-linked 6% agarose beads (34 µm) to which a chelating group has been immobilized and subsequently charged with Ni2+ ions. The chromatography medi...
Keywords: Affinity chromatography, Buffers, Cell disruption, Chromatography, Filtration, Homogenization, Immobilization, Purification, Sample preparations, Sonication, Tagged proteins

Purification using StrepTrap HP 1 ml and 5 ml

StrepTrap™ HP 1 ml and 5 ml columns are made of biocompatible polypropylene that does not interact with biomolecules (Figure 7.2). Prepacked StrepTrap™ HP columns provide fast, simple, and easy separ...
Keywords: Affinity chromatography, Buffers, Cell disruption, Chromatography, Homogenization, PAGE, Sample preparations, 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

Tag Removal by Enzymatic Cleavage

In most cases, functional tests can be performed using the intact histidine-tagged protein. If removal of the tag is necessary, then procedures similar to GST tag removal can be followed, that is, sp...
Keywords: Affinity chromatography, Cell disruption, Centrifugation, Chromatography, Digestions, PAGE, Purification, Separation, Size-exclusion chromatography, Sonication, Tagged proteins

Troubleshooting Guide for Affinity Chromatography of Tagged Proteins

The troubleshooting guide below addresses problems common to the majority of purification products discussed in this chapter, as well as problems specific to a particular method. In the latter case, th...
Keywords: Addition reactions, Affinity chromatography, Buffers, Cell culture, Cell disruption, Centrifugation, Chromatography, Detergents, Fermentation, PAGE, Precipitation, Protein biosynthesis, Size-exclusion chromatography, Sonication, Tagged proteins, Western blot

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