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Source. Mouse. Specificity. This monoclonal antibody was raised against purified human C4. It is specific for an antigen expressed on the C4c domain of C4 and therefore reactive to C4 and all C4c-containing fragments of C4. Storage. Short term (30 days) 4˚C. Long term at or below -20˚C. Background.

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It was shown that the complement system is activated in IgA nephropathy via the both alternative and classical pathways. A study on the deposition of complement control proteins in renal tissues from patients with IgA nephropathy is described. Renal biopsy specimens were obtained from patients with IgA nephropathy and other glomerular diseases. These biopsy samples were stained with antisera.

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Recognition causes activation of proteolytic enzyme cascades, resulting in cleavage of the complement proteins C3, C4, and C5. Fragments of these proteins have important effector functions through binding to host cell receptors and pathogen surfaces ( 1 ). In the lectin pathway of complement, four pattern recognition molecules, mannan-binding.

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Source. Mouse. Specificity. This monoclonal antibody was raised against purified human C4. It is specific for an antigen expressed on the C4d domain of C4 and therefore reactive to C4 and all C4d-containing fragments of C4. Storage. Short term (30 days) 4˚C. Long term at or below -20˚C. Background.

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Of note, the levels of C4 in CTRL MRL mouse serum were 16-fold lower than those measured in wildtype CTRL B6 mice or in KO B6 mice ( P < 0.001). In CTRL MRL mice, the serum C4 levels rise four-fold from 3 weeks of age to 8 weeks of age and then remain unchanged until at least 20 weeks of age.

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The gamma-domain and the L chain constitute the catalytic site of C1s to activate C4 to C4b and can be replaced by newly coming C4. The catalytic site for C4 of C1s has been presumed to consist of a C4-binding domain and a proteolytic domain. A mAb to C1s, M81, blocked C4 activation and C4 binding to C1s. M81 recognized the H chain of C1s. Using M81 as a probe, we tried to define C4-binding.

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A, binding to the surface of a pathogen induces autoactivation of MBP·MASP-2, exposing accessory C4-binding sites on the MASP and leading to recruitment of C4. B, MASP-2 cleaves C4. Anaphylatoxin C4a is released, whereas interactions between the MASP and the C4b fragment lead to covalent attachment of C4b proximal to the activating lectin.

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Complement C4, a key molecule in the complement system that is one of chief constituents of innate immunity for immediate recognition and elimination of invading microbes, plays an essential role for the functions of both classical (CP) and lectin (LP) complement pathways. Complement C4 is the most polymorphic protein in complement system.

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Diagnosis is based on antigenic assays of total or free plasma protein S (free protein S is the form unbound to the protein S carrier molecule, C4-binding protein). Protein S activity can also be measured, but the assay is technically difficult and is associated with a high false-positive rate (10 to 15%) so more reproducible antigen assays are.

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Fusion proteins comprising this antigen fused to the oligomerization domain of the murine complement inhibitor C4-binding protein (C4bp) and a series of homologues have been produced. These C4bp domains acted as adjuvants for the fused antigen; the MSP1(19)-murine C4bp fusion protein induced protective immunity in BALB/c mice.

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A summary of statistics is provided in Table 1.All diffraction images are deposited in TARDIS (19) and are freely available online.An initial molecular replacement solution was found using the BALBES pipeline web service (20), which internally uses MOLREP (21) with the coordinates for activated C1s (Protein Data Bank code 1ELV, containing the CCP2-SP domains) as a search model and REFMAC5 (22.

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