Chromatography, short for “chromatographic analysis”, is a method for the separation and determination of multi-component mixtures based on the different physical properties of each component.
Through cooperation with Bestchrom (Shanghai) Biosciences Co., Ltd, Jean Standard Biological Technology Co. Ltd provides customers with quality products and services, including gel filtration media, ion exchange media, hydrophobic interaction media, affinity chromatography media, etc.
Gel filtration media:
Gel filtration is a type of chromatography method to separate substances based on the size and shape of biomolecules. The gel filtration medium has a porous network structure. The smaller the biomolecules, the deeper they go into the medium, and the longer they stay in the medium, and the longer they stay in the medium. The aperture of each medium has a certain range, so the key to the selection of gel filtration media is the appropriate separation range, followed by the mechanical properties and magnification.
Features of Gel Filtration Chromatography:
—Non-adsorption method, easy operation, only one buffer solution required.
Classification and Characteristics of Gel Filtration Chromatography:
—Group Separation (desalination/buffer exchange); The sample volume can reach 30% of the column volume.
—Fine Separation (aggregate removal, separation of proteins of different molecular weights); Sample volume of 0.5-4%, column bed height is higher than 60cm.
(Sephadex Gel Filter Media)
|Bestarose Fast Flow series||Bestarose 4 Fast Flow|
|Bestarose 6 Fast Flow|
|Chromdex prep grade series||Chromdex 30 prep grade|
|Chromdex 75 prep grade|
|Chromdex 200 prep grade|
|Bestarose/Bestarose CL series
(Agarose gel medium)
|Bestarose CL 4B|
|Bestarose CL 6B|
Ion exchange chromatography:
Ion exchange chromatography (ION-exchange) is a type of chromatography technique to separate different biomolecules based on the difference of charge properties and quantities. As most biomolecules are with acidic groups, or basic groups, and can change the charge properties and quantities by adjusting the pH of buffer. After the biomolecules bond with anion exchange media or cation exchange media with the opposite charge, by changing the ionic strength or pH in the mobile phase, those with weak binding force will be eluted first and those with strong binding force will be eluted later, thus achieving the purpose of separation and purification.
Features of Ion Exchange Chromatography:
—Good controllability, high selectivity, high load, high recovery, good physical and chemical stability, simple in situ cleaning
Classification and Characteristics of Ion Exchange Media:
—Composed of the base frame and the functional group, the ion exchange medium is divided into cation exchange and anion exchange according to the charge properties of the functional group, and is classified into strong ion exchange group and weak ion exchange group according to its electric strength in the solution.
—The type and density of the ion-exchange group determine the selectivity and load of the medium. The properties of the base frame determine the resolution and mechanical properties of the medium.
|Bestarose Fast Flow(Strong ion)||Q Bestarose Fast Flow|
|SP Bestarose Fast Flow|
|Bestarose Fast Flow(Weak ion)||DEAE Bestarose Fast Flow|
|CM Bestarose Fast Flow|
|Bestarose XL IEX||Q Bestarose XL|
|SP Bestarose XL|
|Bestarose High Performance||Q Bestarose High Performance|
|SP Bestarose High Performance|
|Diamond MMC||Diamond MMC|
|MMC Bestarose 6FF|
|Diamond Mix-A||Diamond Mix-A/Diamond MIX-A Mustang XL|
|Diamond Mustang||Diamond Q Mustang/Diamond Q Mustang XL|
|Diamond SP Mustang/Diamond SP Mustang XL|
|Diamond MMC Mustang||Diamond MIX-A Mustang/Diamond MMC Mustang|
|Bestdex||CM Bestdex C-25/DEAE Bestdex A-50|
|Bestarose XL Big Beads IEX||Q Bestarose XL Big Beads|
|SP Bestarose XL Big Beads|
|Bestarose BB||SP Bestarose BB/Q Bestarose BB|
hydrophobic interaction media:
Hydrophobic interaction chromatography is a commonly used method to separate biomacromolecules such as proteins or peptides according to the difference in the hydrophobicity of molecular surface. The key to the selection of hydrophobic chromatography media lies in the appropriate hydrophobic ligands. If the protein is with strong hydrophobicity, then select a medium with weak hydrophobicity, and vice versa. A certain amount of salt (usually ammonium sulfate) should be added to the buffer to enhance the binding of protein to hydrophobic medium. If the protein itself is with strong hydrophobicity, there is no need to add too much salt. Hydrophobic media with smaller particles can be selected to improve the resolution.
Factors affecting the hydrophobic effect:
(1)Type and Concentration of Salt
Some ions that form the salt in the buffer have a stabilizing effect on protein conformation, such as SO42-, which can improve the stability of protein structure, decrease the solubility of protein, have a salting out effect on protein, and enhance the hydrophobic effect between protein and ligand. Some ions have an un-stabilizing effect on protein conformation, such as Cl- and Ca2+, which can increase protein solubility, and these ions have a strong elution ability. The properties of salting out and salting in can be used as the basis for choosing the equilibrium and elution conditions of hydrophobic media.
In the process of hydrophobic chromatography, the temperature goes up, there are conformational changes in biomacromolecules, and the hydrophobic effect is enhanced, which helps to improve the separating degree of column chromatography. However, for bioactive substances, high temperature will cause denaturation and deactivation, so hydrophobic chromatography is often conducted under a normal temperature or low temperature. It is suggested that hydrophobic chromatography should be conducted under the condition of constant temperature to avoid the influence of temperature changes on the tomographic results.
The mobile phase of hydrophobic chromatography is usually a phosphate buffer with a neutral pH value. The interaction between protein and hydrophobic group decreases with the increase of pH, because the charge of acidic group of protein increases gradually with the increase of pH, and the hydrophilicity increases. However, the hydrophobicity of proteins is usually not changed by adjusting the pH of solution in hydrophobic chromatography.
High rigidity agarose base frame hydrophobic chromatography medium
|Diamond Phenyl（HS）/Diamond Phenyl（LS）|
High-resolution rigid agarose-based hydrophobic chromatography medium
|Diamond Phenyl Mustang|
|Diamond Octyl Mustang|
|Diamond Butyl Mustang|
Fast-flow agarose-based hydrophobic chromatography medium
|Phenyl Bestarose FF (HS)/
Phenyl Bestarose FF (LS)
|Butyl Bestarose 4 FF|
|Octyl Bestarose 4 FF|
|Butyl-S Bestarose FF|
|Bestarose High Performance||Butyl Bestarose HP|
|Phenyl Bestarose HP|
|Octyl Bestarose HP|
Affinity chromatography media:
Affinity chromatography is a method of chromatography to separate substances based on specific interactions between biomolecules, such as the binding of enzymes to substrates, receptors to ligands, antibodies to antigens, etc. Such bindings are both specific and reversible. Protein purification is achieved through this reversible binding and separation.
Features of Affinity Chromatography:
—High efficiency, speediness; High selectivity; High resolution; Over 90% purity can be achieved usually through one-step purification; High recovery rate
Composition of Affinity Medium:
—Base Frame：Inert materials coupled with ligands, such as Bestarose FF, Bestarose HP, etc.
—Connecting Arm：Reduce the steric-hindrance effect, greatly increase the adsorption efficiency of ligands and biomacromolecules to be separated;
—Ligands：Substances that interact specifically with a target molecule.
|Alkali-resistant antibody affinity medium||AT Protein A Diamond / AT Protein Diamond Plus|
|Antibody affinity media||Protein A Diamond / rProtein A Bestarose 4FF|
|Antibody affinity media||Protein G Bestarose 4FF|
|Nucleic acid affinity medium||Plasmid Cap Bestarose HP/Plasmid Cap Mustang|
|Thiophilic affinity medium||IgM Cap Mustang/IgY Cap Mustang|
|IgM Capture Bestarose FF/IgM Capture Bestarose HP|
|IgY Capture Bestarose HP|
|Metal chelating affinity media||Ni Bestarose HP/Ni Bestarose FF|
|Benzamidine affinity medium||Benzamidine Bestarose 4FF/Benzamidine Bestarose 6B|
|Glutathione Affinity Medium||GST Bestarose 4FF/GST Bestarose 4B|
|Blue Gum Affinity Medium||Blue Bestarose FF/Blue Bestarose HP|
|Diamond Blue/Diamond Blue Mustang|
|Heparin affinity medium||Heparin Bestarose HP/Heparin Bestarose FF|
|Endotoxin affinity medium||Endotoxin Cap Bestarose 4FF|
|Metal chelating affinity media||IMAC Bestarose HP/IMAC Bestarose FF|
|Chelating Bestarose FF|
|Pre-activated affinity media||CNBr-activiated Bestarose 4B/CNBr-activiated Bestarose 4FF|
|NHS-activiated Bestarose 4FF|
|Epoxy-activiated Bestarose 6B|
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