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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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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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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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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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O.07M Sodium Chloride 1% BSA pH 7.2 Background: The Complement System is a plasma-based protein cascade, which functions as a highly regulated and effective immune barrier in the presence or absence of antibody. It is comprised of four main protein pathways that regulate and influence each other. The classical pathway (CP), so called


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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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The results demonstrate extensive binding of C3 and C4 to both collagen and elastin fibers within the adventitia in both ApoE(−/−) and C57Bl/6J control mice, as well as the presence of C3 and C4 within perivascular adipose tissue.. The aortas were sectioned longitudinally and cross-sectionally to produce en face and transverse sections.


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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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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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Background Nanotechnology holds revolutionary potential in the field of agriculture, with zinc oxide nanoparticles (ZnO NPs) demonstrating advantages in promoting crop growth. Photosynthesis is a key process in the growth and quality formation of tea plants, and phyllosphere microorga.


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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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Labcorp test details for C4-binding Protein. In blood, PS exists in a free and bound state. Sixty percent to 70% of plasma protein S circulates complexed to C4b-binding protein (C4bBP), a 570 kilodalton complement system regulator. 6 The remaining protein S, called free PS, in molar excess to C4bBP, is the functionally active form of PS. Acquired protein S deficiency may be, theoretically, the.


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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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