Interaction of C1q with Human Aggregated IgG Detection Protocol

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Interaction of C1q with Human Aggregated IgG Detection

Fig.1 Flow chart of the interaction of C1q with human aggregated IgG detection protocol. (Creative Biolabs)

Published Data

ELISA analysis of the interaction between rCfC1qDC and human heat-aggregated IgG. Fig.2 ELISA assessment of rCfC1qDC binding with human heat-aggregated IgG.¹

Proteins containing the C1q domain (C1qDC) are defined by their globular C1q (gC1q) domain, facilitating participation in a range of immune responses by interacting with various ligands. The recombinant CfC1qDC (rCfC1qDC) was shown to bind human heat-aggregated IgG in a dose-dependent manner, a process inhibited by LPS, as evidenced by changes in absorbance. This interaction suggests evolutionary insights into the complement system's classical pathway. Additionally, rCfC1qDC markedly enhanced scallop hemocytes' phagocytic activity, readily apparent through the intracellular presence of phagocytized E. coli under microscopy, underscoring rCfC1qDC's immunomodulatory potential.

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Reference

Wang, Leilei, et al. "A C1q domain containing protein from scallop Chlamys farreri serving as pattern recognition receptor with heat-aggregated IgG binding activity." (2012): e43289. Distributed under Open Access license CC BY 4.0, without modification.

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