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antibody form
IgG fraction of antiserum
species reactivity
human (Human IgG)
shipped in
wet ice
storage temp.
2-8°C
General description
A Protein Conformational Array (PCA) in a sandwich ELISA format where the plate is coated with a panel of antibodies raised against peptides derived from the full length protein sequence of Etanercept. Taken individually, each of these antibodies is strongly antigenic to the peptide sequence that was used in its production. However, when these peptides are incorporated into a full length correctly folded protein, the antigenicity of many of them is masked by the three dimensional structure of the protein and only a limited number of the antibodies respond. The result is a histogram which can be likened to a ‘fingerprint′ for correctly folded Etanercept. For an Enbrel Biosimilar, if the protein is correctly folded and glycosylated, the ‘fingerprint′ will match that of Etanercept. If it is not correctly folded, previously masked peptide sequences will be exposed and will be recognized by the antibody made to that exposed sequence. In this way, changes in the ‘fingerprint′ generated by the ELISA will point out differences between the Biosimilar and authentic Etanercept.
Application
For research use only. Not for use in diagnostic procedures.
Signal Word
Warning
Hazard Statements
Precautionary Statements
Hazard Classifications
Eye Irrit. 2 - Met. Corr. 1 - Skin Irrit. 2
Storage Class Code
8A - Combustible corrosive hazardous materials
WGK
WGK 1
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Monoclonal antibody higher order structure analysis by high throughput protein conformational array.
Yuanli Song et al.
mAbs, 10(3), 397-405 (2018-01-10)
The elucidation of antibody higher order structure (HOS) is critical in therapeutic antibody development. Since HOS determines the protein bioactivity and chemo-physical properties, this knowledge can help to ensure that the safety and efficacy attributes are not compromised. Protein conformational
Biosimilar mAb in-process Sample Higher Order Structure Analysis with Protein Conformational Array ELISA.
Michael Davies, Gan Wang, Jian Gong, Guofeng Fu and Xing Wang
Pharmaceut. Res., 1-11 (2016)
Xing Wang et al.
Frontiers in pharmacology, 4, 103-103 (2013-08-24)
Antibody arrays were developed to probe a monoclonal antibody's three-dimensional structure (3-D structure). Peptides with overlapping regions were designed to cover the whole mAb light chain and heavy chain, respectively, and used to generate polyclonal antibodies after the conjugation of
Soon Kwan Jung et al.
mAbs, 6(5), 1163-1177 (2014-12-18)
Remsima (infliximab) was recently approved as the world's first biosimilar monoclonal antibody (mAb) in both the European Union and Korea. To achieve this, extensive physicochemical characterization of Remsima in relation to Remicade was conducted in order to demonstrate the highly
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