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anti-Mouse (Murine) MASP1 Antikörper:
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Human Monoclonal MASP1 Primary Antibody für IA, IP - ABIN2191969
Schwaeble, Dahl, Thiel, Stover, Jensenius: The mannan-binding lectin-associated serine proteases (MASPs) and MAp19: four components of the lectin pathway activation complex encoded by two genes. in Immunobiology 2002
Show all 6 Pubmed References
Human Monoclonal MASP1 Primary Antibody für IA, IP - ABIN2191968
Hajela, Kojima, Ambrus, Wong, Moffatt, Ferluga, Hajela, Gál, Sim: The biological functions of MBL-associated serine proteases (MASPs). in Immunobiology 2002
Show all 5 Pubmed References
MBL (zeige MBL2 Antikörper)-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 (zeige CFH Antikörper)) and MASP-1/MASP-3 did not ameliorate either the plasma Complement C3 (zeige C3 Antikörper) (C3) activation or glomerular C3 accumulation in FH-deficient mice.
Within the mannose-binding lectin (zeige MBL2 Antikörper)/MASP complex, MASP-1 is the necessary complement component for thrombin (zeige F2 Antikörper)-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.
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 (zeige MASP2 Antikörper), 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 (zeige MASP2 Antikörper) 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 (zeige THBS1 Antikörper), GPLD1 (zeige GPLD1 Antikörper) and ApoA-IV (zeige APOA4 Antikörper), 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 (zeige COLEC10 Antikörper) 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
The exclusion of the MASP1 and COLEC11 (zeige COLEC11 Antikörper) 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 (zeige MASP2 Antikörper) 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.
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