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<p>Antibodies serve as essential recognition elements in in vitro diagnostics (IVD), yet reliance on polyclonal antibodies (pAbs) introduces significant challenges related to batch-to-batch consistency. To address this, we employed a <i>de novo</i> sequencing platform, which identified 15 candidate monoclonal antibody (mAb) sequences. From these, four distinct mAb mixtures were formulated and evaluated. Using an immunoturbidimetric assay to quantify apolipoprotein A-I (ApoA-I) in 105 human serum samples, the performance of these mixtures was compared to that of a conventional pAb reagent. The four-mAb mixture demonstrated excellent correlation with the pAb assay (Passing-Bablok: y = 1.0536x-0.0748&#xa0;g/L; r<sup>2</sup> = 0.994). This optimized cocktail successfully replaced the pAb reagent, matching or exceeding its performance in key analytical parameters including linearity, sensitivity, and precision. Our work thus establishes a practical pathway for converting heterogeneous pAbs into defined, recombinant antibody reagents suitable for standardized IVD applications.</p>

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From polyclonal to monoclonal: de novo sequencing of goat antibodies for a standardized ApoA-I immunoturbidimetric assay

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年5月12日

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  • Lulai Xu,
  • Qitao Song,
  • Ming Zhu,
  • Wei Zhao,
  • Qiang Li,
  • Sai Li,
  • Bohong Li,
  • Linzhu Li,
  • Bin Ma,
  • Zhengzhong Song,
  • Xin Yang,
  • Yun Xie,
  • Weijing Yi,
  • Jing Wang

摘要

Antibodies serve as essential recognition elements in in vitro diagnostics (IVD), yet reliance on polyclonal antibodies (pAbs) introduces significant challenges related to batch-to-batch consistency. To address this, we employed a de novo sequencing platform, which identified 15 candidate monoclonal antibody (mAb) sequences. From these, four distinct mAb mixtures were formulated and evaluated. Using an immunoturbidimetric assay to quantify apolipoprotein A-I (ApoA-I) in 105 human serum samples, the performance of these mixtures was compared to that of a conventional pAb reagent. The four-mAb mixture demonstrated excellent correlation with the pAb assay (Passing-Bablok: y = 1.0536x-0.0748 g/L; r2 = 0.994). This optimized cocktail successfully replaced the pAb reagent, matching or exceeding its performance in key analytical parameters including linearity, sensitivity, and precision. Our work thus establishes a practical pathway for converting heterogeneous pAbs into defined, recombinant antibody reagents suitable for standardized IVD applications.