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H-Ficolin, also known as Ficolin-3, Hakata antigen, heat-resistant β-2 macro glycoprotein, is one of the lectins involved in innate immunity in human serum. Ficolin-3 recognizes acetyl groups and binds to acetylated carbohydrates on the surface of pathogens to activate the complement system in an antibody-independent manner. In addition, studies have also shown that Ficolin-3 interacts with specific polysaccharide or lipopolysaccharide components of certain pathogenic microorganisms. The Ficolin-3 component in serum can form a complex with MASP and its truncated protein. Using this property, Ficolin-3 can be purified from serum as a complex. Here, we briefly summarize the protocol for assessing the complement activation function of the ficolin-3-dependent lectin pathway, and provide simple technical references for your related research.
Ficolin-3-Pathway of Complement Analysis Protocol
Fig 1. The flow of ficolin-3-pathway of complement analysis protocol. (Creative Biolabs)
Complement-related research can be very complicated, and Creative Biolabs uses comprehensive professional knowledge and advanced technology platforms to wisely select and carry out any related tests for you, and provide accurate and reliable test results and final interpretations. With our extremely flexible service options, you can entrust us with the entire research project and validation work, freeing up your time for other important work. We are also willing to accept the challenge to help you complete the critical and difficult experimental steps in the overall plan. The extremely high professionalism and comprehensive theoretical knowledge allow us to provide you with fast and reproducible results.
Published Data
Fig 2. Serum Ficolins and MBL binding to acBSA.1
A novel ELISA method was developed to detect Ficolin-3-mediated complement activation. In this study, scientists utilized acetylated bovine serum albumin (acBSA) as a solid-phase ligand to evaluate the binding of ficolin. Additionally, we assessed the activation of the complement system by monitoring the deposition of C4, C3, and the terminal complement complex (TCC). The result demonstrated that serum Ficolin-3 binds to acBSA in a calcium-dependent manner, and the deposition of serum C4, C3, and TCC on acBSA was found to be entirely dependent on Ficolin-3 at specific serum dilutions. Additionally, there was a strong correlation between the deposition of downstream complement components and serum Ficolin-3 concentrations in healthy donors. The proposed method is able to measure Ficolin-3-mediated complement activation, providing a potential method for diagnosing related functional and genetic defects.
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Reference
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Hein, Estrid, et al. "Functional analysis of Ficolin-3 mediated complement activation." PLoS One 5.11 (2010): e15443. Distributed under Open Access license CC BY 4.0, without modification.
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