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Complement System

Complement System

The complement system is a group of approximately 20 plasma proteins that strengthen the body's defenses against infections through opsonization, inflammation, and cell lysis. Opsonization involves coating pathogens with complement proteins, making them more recognizable and facilitating phagocyte engulfment. Certain complement proteins induce inflammation that attracts immune cells to the site of infection. Cell lysis involves the destruction of pathogens through the formation of a...

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Updated: May 6, 2026

Isolation and Characterization Of Chimeric Human Fc-expressing Proteins Using Protein A Membrane Adsorbers And A Streamlined Workflow

Isolation and Characterization Of Chimeric Human Fc-expressing Proteins Using Protein A Membrane Adsorbers And A Streamlined Workflow

Published on: January 8, 2014

Purification, quantification, and functional analysis of Complement Factor H.

Bing-Bin Yu¹, Beryl E Moffatt, Marina Fedorova

¹Department of Biochemistry, University of Oxford, Oxford, UK.

Methods in Molecular Biology (Clifton, N.J.)

|November 13, 2013

Summary

This summary is machine-generated.

Complement Factor H (FH) regulates complement system activation. It can be purified using affinity chromatography and quantified via ELISA, with its activity measured by cofactor-dependent C3b cleavage.

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Last Updated: May 6, 2026

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Measuring the 50% Haemolytic Complement CH50 Activity of Serum

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Published on: March 29, 2010

Area of Science:

Biochemistry
Immunology

Background:

Complement Factor H (FH) is a key regulator of the complement system.
FH is an abundant plasma glycoprotein with crucial regulatory functions.

Purpose of the Study:

To describe methods for purifying and quantifying Complement Factor H (FH).
To outline assays for measuring FH activity.

Main Methods:

Affinity chromatography using monoclonal anti-FH antibodies, cardiolipin, or TNP-BSA for FH purification.
Sandwich ELISA for quantifying human FH protein concentration.
Assays measuring cofactor activity in complement factor I-mediated C3b cleavage.

Main Results:

Successful purification of human and vertebrate FH using various affinity ligands.
Quantification of human FH protein concentration is achievable via ELISA.
FH's cofactor activity in C3b cleavage by factor I can be measured.

Conclusions:

Complement Factor H (FH) can be effectively purified from various sources using affinity chromatography.
Standardized methods exist for quantifying FH protein and measuring its functional activity.