Protein chromatography columns are prepacked or self-packed devices containing a stationary phase (resin/media) used to separate and purify proteins based on specific biochemical properties such as affinity, charge, size, or hydrophobicity..

- Affinity Chromatography Columns

-Ion Exchange Chromatography Columns

- Size Exclusion Chromatography Columns

- Hydrophobic Interaction Chromatography Columns

Affinity chromatography is a widely used technique that immobilizes specific ligands on the solid phase to separate single components from complex solutions by exploiting the specific binding between biomolecules and ligands..

- Tag Protein Affinity Chromatography Ni Resin

- Antibody Purification Chromatography Resin

- IMAC Affinity Purification Chromatography Resin

- Chelating Beads Affinity Purification Chromatography Resin

- Heparin Beads Affinity Purification Chromatography Resin

Ion exchange chromatography is the most commonly used method for the separation and purification of biological macromolecules, which separates proteins based on their different charges under specific pH conditions. Ion exchange chromatography media with agarose gel as the matrix, retain the excellent hydrophilicity and pore structure of natural polysaccharide compounds, ensuring good compatibility with bioactive macromolecules..

- Anion Chromatography Resin

- Cation Chromatography Resin

- Styrene and divinylbenzene polymer particles

- Quaternary amine group Chromatography Resin

- Highly crosslinked agarose Chromatography Resin

Pre Packed Column - We provide pre packed purification columns for your research or analysis.

Resins - We have all pack sizes.

Gel filtration chromatography, also known as size exclusion chromatography, separates and purifies sample components based on differences in their physical sizes as the liquid flows through the resins. In this process, larger molecules eluting from resins first and smaller molecules eluting later..

- Agarose Gel Filtration Resin

- Dextran Gel Filtration Resin

- Highly cross-linked agarose and dextran

- Dextran gel

- Desalting Columns

Hydrophobic interaction chromatography (HIC) separates proteins based on the hydrophobicity of their surfaces by utilizing the interactions between proteins and hydrophobic groups. The hydrophobic chromatography media use highly cross-linked agarose gel as the matrix and ligands such as Phenyl and Butyl, which have strong hydrophobicity and high loading capacity, making them particularly suitable for the separation and purification of proteins, enzymes, polysaccharides, nucleic acids, and plasmids..

- HIC resin using Phenyl as its ligands

- HIC resin using low concentration of Phenyl as its ligands

- HIC resin using Cross-linked agarose

- Highly cross-linked agarose

A buffer, by definition, helps a solution to resist changes in pH when small quantities of acid or base are added to it. Protein purification protocols utilize various buffers to aid in stabilization at each step of the process..

- Buffering agent; Tris (pH 7 TO 8),HEPES (pH 7.4), phosphate buffer (pH 7.2)

- Salt;NaCl (100–500 mM), KCl

- Reducing agent; DTT (1–10 mM), β-mercaptoethanol (1–5 mM), TCEP

- Detergent;Triton X-100 (0.1–1%), Tween-20, CHAPS

- Protease inhibitors; PMSF, EDTA-free protease inhibitor

- Imidazole (10–500 mM)

Protein purification reagents are chemicals, enzymes, buffers, and materials used to isolate, concentrate, and stabilize proteins from complex biological mixtures while preserving their structure and biological activity..