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Ion-Exclusion IC Columns

Ideal for separation of aliphatic organic acids and alcohols in complex samples, and for monitoring trace levels of borate in high-purity water.

Hydroxide-Selective Anion-Exchange Columns

Use these high-capacity, high-resolution columns for inorganic anions, oxyhalides including bromate, organic acids, haloacetic acids, and multivalent anions in complex matrices.

Reprospher

Your workhorse
Reprospher media are based on a 100 A ultrapure silica and are fully scalable from UPLC (1.9 µm particles) to preparative and process scale applications.
Among the offered phases there are some unique selectivities such as a wide range of aromatic specialty phases, phases with polar selectivities and unique phases for achiral SFC.

ReproSil XR

Premium performance at exceptional value
An allround and fully scalable spherical Silica from 1.5 to 15 µm with an extra high purity.
The metal content is less than 100 ppb.
The silica impresses with its very narrow pore size distribution this make 99 % of the surface accessible for the separation.
The uniform bonded phase coverage translates to symmetrical peaks for acids/bases, and predictable reversed phase selectivity.
Because of its very low metal content it also impressed with a high pH stability.

ReproSil Saphir

Alternative to Luna C18. A low metal content spherical silica media scalable from sub-2-micron to 10 µm particles with high carbon load for small molecules and peptides and wide pore ion exchange media for protein and enzyme analysis and purification.

ReproSil-Pur

Specifically designed for pharmaceutical and biotechnical separations.
A robust modern and all-purpose ultra-high purity spherical silica media scalable from UPLC to prep.
Various pore sizes are available to cover applications for small molecules up to biomolecules.
State-of-the-art surface modification technologies are employed for normal and reversed phase media including shape selective, high carbon load as well as water wettable alkyl phases.

Normal phase and hydrophilic interaction liquid chromatography (HILIC)

Normal phase and hydrophilic interaction liquid chromatography (HILIC) are primarily used to separate polar and hydrophilic compounds. In reversed phase mode very polar compounds are often not sufficiently retained in low percent organic, or even in 100% aqueous mobile phase. The order of elution in normal phase is opposite that found in reversed phase for the same mixture of compounds. Although non-polar organic mobile phases and a silica stationary phase were used traditionally in normal phase LC, today most separations are performed with aqueous-organic mobile phases and a more polar-bonded stationary phase. This mode of HPLC is now commonly referred to as HILIC, hydrophilic interaction liquid chromatography.

Reversed Phase Chromatography (RPLC or RPC)

Reversed Phase Chromatography (RPLC or RPC) is the most efficient of all biomolecule separation techniques. It has been the technique of choice for the analysis of small molar mass compounds in both the pharmaceutical and chemical industries, as well as in biomedical research, since the late 1970s. More recently, RPC has become the accepted tool for the separation of peptides, proteins and other biopolymers, making it largely responsible for the widespread popularity of HPLC as a chromatographic technique.

Affinity Chromatography (AFC)

Affinity Chromatography (AFC) offers the greatest potential specificity and selectivity for the isolation or purification of biomolecules. Almost all biological molecules can be purified on the basis of a specific interaction between their chemical or biological structure and a suitable affinity ligand.

In AFC, the target molecule is specifically and reversibly adsorbed by a complementary ligand and immobilized on a matrix. Examples of a complementary ligand include an inhibitor, substrate analog or cofactor, or an antibody which specifically recognizes the target molecule. The selectivity is often based on spatial recognition, a ‘lock-and-key’ mechanism.

The adsorbed molecule is subsequently eluted either by competitive displacement or a conformation change through a shift in pH or ionic strength. Typical molecular pairs are antigens and antibodies, enzymes and coenzymes, and sugars with lectins.

Purification of several thousand-fold may be obtained due to the high selectivity of the affinity interactions. Although affinity chromatography is not specific, in that no enzyme interacts with only one substrate, it is the most selective method for separating proteins.

Hydrophobic interaction chromatography (HIC)

Hydrophobic interaction chromatography (HIC) is based on non-polar interactions that are induced by high salt mobile phases. Stationary phases are similar to reversed phase chromatography (RPC) but the density of functional groups is lower. A weakly non-polar stationary phase is used with an aqueous mobile phase containing a high concentration of a chaotropic salt.

The technique is mainly applied to the separation of proteins, which are eluted by decreasing the salt concentration or by adding a low percentage of organic solvent. Although also based on hydrophobic interactions, selectivity in HIC separations is distinctly different from that in reversed phase chromatography. Despite the lower peak capacity in HIC compared to RPC, HIC has the advantage that the mobile phase conditions (primarily aqueous) do not usually disrupt higher-order protein structures.

HIC is used in the biopharmaceutical industry for the analysis of antibody drug conjugates (ADCs) or to determine the aggregate content of monoclonal antibodies.

Ion Exchange Chromatography (IEC)

Ion Exchange Chromatography (IEC) is a technique based on the difference in the strength of the interaction between a sample ion and an oppositely charged functional group on the support. The sample ion competes for the functional group with a counter ion that has been added to the mobile phase as a salt. Elution is most often accomplished by increasing the salt concentration over time.