CFP

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Properdin is a protein that in humans is encoded by the CFP (complement factor properdin) gene. Properdin and factor H are regulatory proteins in the alternative complement pathway. Properdin is an up-regulator, stabilizing the C3bBb complex, and factor H is the down-regulator, promoting proteolytic degradation of C3b. Factor H is primarily produced in the liver, whereas properdin is sourced in neutrophils, monocytes, T cells and bone marrow progenitor cell line. Properdin is plasma glycoprotein that activates the complement system of the innate immune system. It is found in plasma and primarily produced by leukocytes. This protein binds to bacterial cell walls and dying human cells to stabilize the C3 and C5-convertase enzyme complexes to form an attack complex that leads to the lysis of the cell. The complement system is made of plasma and membrane-bound proteins that go through the blood to get rid of pathogens and damaged cells. Activation of the complement system occurs via three pathways, the classical, lectin, and alternative pathways. Activation of the alternative pathway occurs in bacteria, yeast, and parasites and is stimulated by antibody-antigen complexes made of IgG or IgA. Properdin and factor H are important regulatory proteins of the alternative pathway, which is initiated by a conformational change in C3 cleaved at a single site by the serine protease C3 convertase.