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The ficolin-3 (show FCN3 Proteins)/MASP-2 complex was significantly lower in the cardiac syndrome X patients compared to controls.
MASP-1 (show MASP1 Proteins) and MASP-2 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.
MBL2 (show MBL2 Proteins) and MASP2 deficiencies protect against the development of systemic inflammatory response after pediatric cardiac surgery.
Data show that the vector expressing mannose-binding lectin (show MBL2 Proteins) associated protein 19 (MAp19) has been prepared successfully, and can express the target protein (MAp19) in the eukaryotic cells (HeLa cells).
polymorphism of MASP-2 (rs6695096) gene was associated with susceptibility to tuberculosis.
Polymorphisms of mannose-binding lectin (show MBL2 Proteins) (rs7096206) and MASP-2 (rs2273346 and rs6695096) were associated with the susceptibility of tuberculosis, and there were gene-gene interactions among them.
Polymorphisms in MASP1 (show MASP1 Proteins) and MASP2 genes are associated with the susceptibility or protection to infectious diseases. (Review)
MASP2 gene polymorphisms and protein levels seem to play an important role in the development of rheumatic fever and establishment of rheumatic heart disease.
Because MASP-1 (show MASP1 Proteins) and MASP-2 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.
TFPI (show TFPI Proteins) inhibits lectin pathway of complement activation by direct interaction with MASP-2.
Mannan-binding lectin-associated serine protease 2 is critical for the development of renal ischemia reperfusion injury and mediates tissue injury in the absence of complement C4.
Gene targeting of mouse TDP-43 (show TARDBP Proteins) negatively affects Masp2 expression.
ALI in H5N1-infected mice was caused by excessive complement activation, as demonstrated by deposition of C3, C5b-9, and MBL-C in lung tissue, and by up-regulation of MBL-associated serine protease-2 and the complement receptors C3aR (show C3AR1 Proteins) and C5aR (show C5AR1 Proteins).
study corroborates the essential function of MASP-2 in the lectin pathway and highlights the importance of mannan-binding lectin-independent lectin pathway activation in the host defense against pneumococci
Targeting of mannan-binding lectin (show MBL2 Proteins)-associated serine protease-2 (show PRSS2 Proteins) confers protection from myocardial and gastrointestinal ischemia/reperfusion injury.
Recombinant protein of masp2 was made and purified.
MASP-2 is essential for the activation of C4 and sMAP plays a regulatory role in the activation of the lectin pathway.
MASP-1 (show MASP1 Proteins) contributes to the activation of the lectin pathway, probably through the activation of MASP-2.
The Ra-reactive factor (RARF) is a complement-dependent bactericidal factor that binds to the Ra and R2 polysaccharides expressed by certain enterobacteria. Alternate splicing of this gene results in two transcript variants encoding two RARF components that are involved in the mannan-binding lectin pathway of complement activation. The longer isoform is cleaved into two chains which form a heterodimer linked by a disulfide bond. The encoded proteins are members of the trypsin family of peptidases.
MBL-associated plasma protein of 19 kD
, MBL-associated serine protease 2
, mannan-binding lectin serine peptidase 1 pseudogene 1
, mannan-binding lectin serine protease 1 pseudogene 1
, mannan-binding lectin serine protease 2
, mannose-binding protein-associated serine protease 2
, small MBL-associated protein
, mannose binding lectin-associated serine protease-2