PolyCAT A

  • for Cation-Exchange of Proteins
    Use PolyCAT A  for:

    • Protein variants involving deamidation, PEGylation, position of attachment, desialylation, etc. It is widely used by the biotechnology industry.
    • Hemoglobin variant analysis by clinical chemistry labs.
    • Proteins with pI above 6.0 (5.0 in special cases).
    • Monoclonal antibodies.
    •  

PolyETHYL A

  • for Hydrophobic Interaction Chromatography (HIC) of Proteins and Peptides
    Use these HIC materials for:

    • Multidimensional protein purification (suggested sequence: Ion-exchange – [add salt to collected fractions] – HIC).
    • Purification of polypeptides (e.g., venoms and glycopeptides).
    • Characterization of antibodies.
    • QC analysis of proteins differing in the polarity of a single residue or modified positional variants.

PolyHYDROXYETHYL A

  • for Hydrophilic Interaction and Size Exclusion HPLC
    Use PolyHYDROXYETHYL A for

    • Analysis of polar small molecules for metabolomics or analysis via HILIC-MS/MS of specific small molecules (amino acids; methotrexate) in plasma or crude extracts.
    • Peptide separations and mapping involving differences in polar groups (Ser-; glycopeptides; etc.).
    • Multidimensional purification of synthetic and natural peptides or fractionation of really complex digests.
    • HPLC of solutes that aren’t soluble in aqueous media (membrane proteins; phospholipids).
    • Eliminating detergents, lipids, and salts from a sample.
    • Oligonucleotides and their analogs.

    In the absence of organic solvent, PolyHYDROXYETHYL A  functions in the Size Exclusion Chromatography (SEC) mode.

PolySULFOETHYL A

  • for Cation-Exchange of Peptides
    Use PolySULFOETHYL A for

    • Multidimensional HPLC of peptide mixtures, such as tryptic digests in proteomics analyses (including iTRAQ® and ICAT®* reaction products).
    • Isolation of peptides from natural products.
    • QC and purification of synthetic peptides.
    • Selective isolation of disulfide-linked peptides, phosphopeptides and C-terminal fragments from tryptic digests.
    • Mapping of peptide digests (tryptic, V8, CNBr, etc.).

PolyMETHYL A

  • for Hydrophobic Interaction Chromatography (HIC) of Proteins and Peptides
    Use PolyMETHYL A for

    • Multidimensional protein purification (suggested sequence: Ion-exchange – [add salt to collected fractions] – HIC).
    • Purification of polypeptides (e.g., venoms and glycopeptides).
    • Characterization of antibodies.
    • QC analysis of proteins differing in the polarity of a single residue or modified positional variants.

PolyWAX LP

  • for Anion-Exchange of Proteins and Nucleic Acids
    Use PolyWAX LP for

    • Purification of acidic proteins and polypeptides from natural products.
    • Analysis and purification of oligonucleotides and their analogs as well as amplified PCR products.
    • In proteomics, predigest fractionation of intact proteins via mixed-bed ion-exchange.
    • Anion-exchange of small, acidic solutes.

PolyGLYCOPLEX A

for HILIC of Complex Carbohydrates

This neutral material has the unusually high capacity needed to retain complex carbohydrates in the HILIC mode. Columns can frequently be operated with just acetonitrile and water, although charged carbohydrates may require inclusion of some salt such as ammonium acetate. These conditions are convenient for isolation of carbohydrates or direct flow to a mass spectrometer. Selectivity is good for both native glycans and derivatives such as those with the 2-aminopyridine (PA-) fluorophore. Oligosaccharide mixtures can often be resolved isocratically, although gradients are recommended for especially varied samples. Sialylated and asialo- glycans can be resolved using the same running conditions. In some cases selectivity compares favorably with that of HPAEC with PAD detection, and both running conditions and equipment maintenance are far more convenient.

PolyPROPYL A

for Hydrophobic Interaction Chromatography (HIC) of Proteins and Peptides
Use PolyPROPYLA for

    • Multidimensional protein purification (suggested sequence: Ion-exchange – [add salt to collected fractions] – HIC).
    • Purification of polypeptides (e.g., venoms and glycopeptides).
    • Characterization of antibodies.
    • QC analysis of proteins differing in the polarity of a single residue or modified positional variants

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