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Human MASP1 ELISA Kit for Sandwich ELISA - ABIN415090
Radu, Hu, Jiang, Bok: Bisretinoid-mediated complement activation on retinal pigment epithelial cells is dependent on complement factor H haplotype. in The Journal of biological chemistry 2014
Show all 2 references for ABIN415090
study provides conclusive evidence that an intact complement LP is essential to initiate CAIA, and that MAp44 may be an appropriate treatment for inflammatory arthritis.
Data indicate that co-deficiency of factor H (FH (show CFH ELISA Kits)) and MASP-1/MASP-3 did not ameliorate either the plasma Complement C3 (show C3 ELISA Kits) (C3) activation or glomerular C3 accumulation in FH-deficient mice.
Within the mannose-binding lectin (show MBL2 ELISA Kits)/MASP complex, MASP-1 is the necessary complement component for thrombin (show F2 ELISA Kits)-like activity in vitro.
We conclude that MASP-1 does not require binding to mannose binding lectins or ficolins to activate the alternative pathway of complement
we investigated the mechanism of MASP-3 activation and its substrate using the recombinant mouse MASP-3 (rMASP-3) and several different types of MASP-deficient mice
Our studies demonstrate for the first time, to our knowledge, the absolute requirement for the activity of MASP-1 protein in autoimmune-associated inflammatory tissue injury
MASP-1 converted pro-Df to the active form in vitro, although the activation mechanism of pro-Df by MASP-1 is still unclear. Thus, it is clear that MASP-1 is an essential protease of both the lectin and alternative complement pathways.
MASP-1 contributes to the activation of the lectin pathway, probably through the activation of MASP-2 (show MASP2 ELISA Kits).
The exclusion of the MASP1 and COLEC11 (show COLEC11 ELISA Kits) Loci in two individuals from different consanguineous families and the absence of mutations in four further individuals sequenced for both genes raises the possibility that that there is further genetic heterogeneity of 3MC syndrome
Plasma MASP-1 concentration at the early stage of Kawasaki disease is predictive of length of time of recovery from coronary artery lesions.
MASP-1 and MASP-2 (show MASP2 ELISA Kits) are activated during blood clotting. This activation is triggered by activated platelets and by the generation of fibrin during thrombotic reactions in vitro and in vivo, and may represent a novel activation/amplification mechanism in thromboinflammation.
described for the first time a detailed model of prothrombin (show F2 ELISA Kits) activation by MASP-1
Fusion of MAP-1 with FH domains represents a novel therapeutic approach for selective targeting upstream and central complement activation at sites of inflammation
The levels of MASP-1 and MASP-1/C1-INH complexes are reduced in HAE patients compared with controls. Both MASP-1 and MASP-1/C1-INH complexes are related to the degree of complement C4 consumption
Polymorphisms in MASP1 and MASP2 (show MASP2 ELISA Kits) genes are associated with the susceptibility or protection to infectious diseases. (Review)
Because MASP-1 and MASP-2 (show MASP2 ELISA Kits) have been shown to interact directly with blood coagulation, elevated levels of these proteins may play a role in the enhanced thrombotic environment and consequent vascular complications in diabetes.
MASP-1 cleaves prothrombin (show F2 ELISA Kits) and identified its cleavage sites, suggesting that MASP-1 gives rise to an alternative active form of thrombin (show F2 ELISA Kits) by cleaving at the cleavage site R393.
MASP-1 may activate neutrophils indirectly via endothelial cells.
This gene encodes a serine protease that functions as a component of the lectin pathway of complement activation. The complement pathway plays an essential role in the innate and adaptive immune response. The encoded protein is synthesized as a zymogen and is activated when it complexes with the pathogen recognition molecules of lectin pathway, the mannose-binding lectin and the ficolins. This protein is not directly involved in complement activation but may play a role as an amplifier of complement activation by cleaving complement C2 or by activating another complement serine protease, MASP-2. The encoded protein is also able to cleave fibrinogen and factor XIII and may may be involved in coagulation. A splice variant of this gene which lacks the serine protease domain functions as an inhibitor of the complement pathway. Alternate splicing results in multiple transcript variants.
, complement factor MASP-3
, complement-activating component of Ra-reactive factor
, mannan-binding lectin serine protease 1
, mannose-binding lectin-associated serine protease 1
, mannose-binding protein-associated serine protease
, ra-reactive factor serine protease p100
, serine protease 5
, Ra-reactive factor serine protease p100