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    > 98 % by SDS-PAGE and HPLC analyses.

    Approximately 7.8 kDa, a single non-glycosylated polypeptide chain containing 68 amino acids.

    Escherichia coli

    100 μg, 500 μg, 5 μg
  • ActiveActive

    > 97 % by SDS-PAGE and HPLC analyses.

    Approximately 7.8 kDa, a single non-glycosylated polypeptide chain containing 69 amino acids.

    Escherichia coli

    100 μg, 5 μg, 500 μg
  • ActiveActive

    > 96 % by SDS-PAGE and HPLC analyses.

    Approximately 7.8 kDa, a single non-glycosylated polypeptide chain containing 69 amino acids.

    Escherichia coli

    5 μg, 100 μg, 500 μg
  • ActiveActive

    > 97 % by SDS-PAGE and HPLC analyses.

    Approximately 7.8 kDa protein containing 70 amino acid residues, including the four highly conserved cysteine residues present in CC chemokines.

    Escherichia coli

    500 μg, 5 μg, 100 μg
  • ActiveActive

    > 97 % by SDS-PAGE and HPLC analyses.

    Approximately 7.8 kDa protein containing 70 amino acid residues, including the four highly conserved cysteine residues present in CC chemokines.

    Escherichia coli

    5 μg, 100 μg, 500 μg
  • ActiveActive

    > 95 % by SDS-PAGE and HPLC analyses.

    Approximately 9.6 kDa, a single non-glycosylated polypeptide chain containing 82 amino acids.

    Escherichia coli

    500 μg, 100 μg
  • ActiveActive

    > 97 % by SDS-PAGE and HPLC analyses.

    Approximately 4.9 kDa, a single non-glycosylated polypeptide chain containing 43 amino acids.

    Escherichia coli

    500 μg, 100 μg
  • ActiveActive

    > 98 % by SDS-PAGE and HPLC analyses.

    Approximately 19.8 kDa, a single non-glycosylated polypeptide chain containing 176 amino acids.

    Escherichia coli

    500 μg, 5 μg, 100 μg
  • ActiveActive

    > 97 % by SDS-PAGE and HPLC analyses.

    Approximately 13.2 kDa, a homodimeric protein consisting of two 59 amino acid chains, which includes a 40-amino acid trefoil motif containing three conserved intramolecular disulfide bonds.

    Escherichia coli

    100 μg, 500 μg, 5 μg
  • ActiveActive

    > 97 % by SDS-PAGE and HPLC analyses.

    Approximately 13.2 kDa, a homodimer consisting of two 60 amino acid polypeptide chains, which includes a 40-amino acid trefoil motif containing three conserved intramolecular disulfide bonds.

    Escherichia coli

    100 μg, 500 μg, 5 μg

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