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MBL (show MBL2 Proteins)-KO (Figure 1a) and MASP-1-KO (Figure 1b) mice are poor mobilizers in response to mobilizing agents compared with WT littermates
this study shows that inhibition of MASP-1/3 by gene silencing is sufficient to ameliorate collagen Ab-induced arthritis in mice
MASP-1 plasma levels were higher among patients with type 2 diabetes and diabetic mice
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 Proteins)) and MASP-1/MASP-3 did not ameliorate either the plasma Complement C3 (show C3 Proteins) (C3) activation or glomerular C3 accumulation in FH-deficient mice.
Within the mannose-binding lectin (show MBL2 Proteins)/MASP complex, MASP-1 is the necessary complement component for thrombin (show F2 Proteins)-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.
Studies results provide evidence that Crohn's disease patients have an impairment in mannose-binding lectin-mannose-associated serine protease functional activity and that this defect is associated with mannose-binding lectin 2 and NOD2 variants.
These results indicate that PLTP (show PLTP Proteins) and MASP-1 can serve as plasma biomarkers for the early diagnosis and treatment of Age-related macular degeneration , which is critical for preventing Age-related macular degeneration -related blindness.
MASP-3 is the exclusive pro-factor D activator in resting blood: the lectin and the alternative complement pathways are fundamentally linked.
a strong influence of MASP-1, complement activation and pathway-specific inhibition on coagulation in a microvascular flow system
The complement lectin pathway serine proteases, MASP-1 and MASP-2 (show MASP2 Proteins), can be associated with ischaemic stroke development risk and may participate in pathological events leading to post-ischaemic brain damage. Moreover rs3203210 and rs147270785 single nucleotide polymorphisms in the MASP1 and MASP2 (show MASP2 Proteins) genes, respectively, are strongly associated with ischaemic stroke.
Our finding suggests that complement MASP-1 can increase adhesion between neutrophils and endothelial cells in a direct fashion
Study discovered novel and independent associations of prediabetes and related traits with MASP1, and some evidence for associations with THBS1 (show THBS1 Proteins), GPLD1 (show GPLD1 Proteins) and ApoA-IV (show APOA4 Proteins), suggesting a role for these proteins in the pathophysiology of type 2 diabetes.
MASP-1 was not associated with adverse cardiovascular outcomes in diabetics.
high serum CL-L1 (show COLEC10 Proteins) concentration in critically ill children upon PICU admission is associated with an increased risk of infection and prolonged need of intensive care, and counteracts the protective effect of having a high MASP-3 concentration
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