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GE17-5319-01

HisTrap Fast Flow

GE Healthcare, 17-5319-01, pack of 5 × 1 mL

  •  NACRES NA.56

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Properties

Related Categories Affinity Chromatography, IMAC Matrices, Molecular Biology, Protein Chromatography, Proteomics 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 × 1 mL
mfr. no.   GE Healthcare, 17-5319-01
parameter   <20 mL/min flow rate
  42 psi
bed size   16 mm × 25 mm
bed volume   5 mL
column I.D.   16 mm
matrix   6% cross-linked agarose
particle size   45-165 μm
average diameter   90 μm
cleaning   2 - 14 (Ni2+-stripped medium.)
working range   3 - 12 (Ni2+-stripped medium.)
capacity   ~40 mg binding capacity(histidine-tagged protein)
suitability   suitable for bioprocess medium

Description

General description

HisTrap FF is a ready-to-use column, prepacked with precharged Ni Sepharose® 6 Fast Flow for preparative purification of histidine-tagged recombinant proteins by immobilized metal ion affinity chromatography (IMAC).

Ni Sepharose® 6 Fast Flow consists of 90 μm beads of highly cross-linked agarose, to which a chelating ligand has been immobilized. This chelating ligand is charged with Ni2+ ions, the first-choice metal ion for purifying most histidine-tagged proteins. The negligible leakage of Ni2+ ions from the matrix ensures reliable capture of histidine-tagged proteins in repeated IMAC purifications.

The high flow rates made possible by the Ni Sepharose® 6 Fast Flow matrix make HisTrap FF columns well suited for small scale-up. Capacity can be increased by connecting columns in series. HiTrap® IMAC FF is the product of choice when charging the medium with different metal ions for optimization of purification protocols.

Features and Benefits

• High binding capacity, approx. 40 mg/mL medium.
• Negligible leakage of Ni2+.
• Prepacked columns offer reliable and convenient time-saving purification of histidinetagged recombinant proteins.
• Compatible with a wide range of reducing agents, detergents, denaturants, and other additives.

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

HiTrap is a registered 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

Affinity Chromatography in a Purification Strategy (CIPP)

Chapter 9, Extracted from Affinity Chromatography Vol. 2: Tagged Proteins, GE Healthcare, 2016
Keywords: Affinity chromatography, Chromatography, Ion Exchange, Ligands, Pharmaceutical, Reversed-phase chromatography, Size-exclusion chromatography, Tagged proteins

Cell disruption and membrane preparation

Extracted from Purifying Challenging - Proteins Principles and Methods, GE Healthcare, 2007
Keywords: Cell disruption, Centrifugation, Chromatography, Degradations, Detergents, Phase transitions, Purification

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

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

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

Optimizing Purification of Histidine-Tagged Proteins

Chapter 4, Extracted from Affinity Chromatography Vol. 2: Tagged Proteins, GE Healthcare, 2016
Keywords: Affinity chromatography, Buffers, Cell disruption, Chromatography, Immobilization, Ion Exchange, PAGE, Purification, Separation, Sequencing, Size-exclusion chromatography, Tagged proteins

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

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 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 6 Fast Flow

Ni Sepharose 6 Fast Flow consists of 90 µm beads of highly cross-linked agarose, to which a chelating ligand has been immobilized and subsequently charged with Ni2+ ions. The ligand density of Ni Sep...
Keywords: Affinity chromatography, Buffers, Cell disruption, Chromatography, Filtration, Homogenization, Immobilization, Ligands, Sample preparations, Sonication, Tagged proteins

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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