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anti-Rat (Rattus) MBL2 Antibodies:
anti-Mouse (Murine) MBL2 Antibodies:
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Human Monoclonal MBL2 Primary Antibody for IHC (fro), IHC (p) - ABIN2192483
Ramos, Nisihara, Maestri, Bicalho, Carvalho, de Messias Reason: MBL serum concentration in women with HPV presenting CIN III lesions. in Human immunology 2012
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Human Monoclonal MBL2 Primary Antibody for ELISA, WB - ABIN2192485
Fiane, Videm, Lingaas, Heggelund, Nielsen, Geiran, Fung, Mollnes: Mechanism of complement activation and its role in the inflammatory response after thoracoabdominal aortic aneurysm repair. in Circulation 2003
Show all 3 Pubmed References
Human Monoclonal MBL2 Primary Antibody for ELISA, WB - ABIN2192486
Hein, Honoré, Skjoedt, Munthe-Fog, Hummelshøj, Garred: Functional analysis of Ficolin-3 mediated complement activation. in PLoS ONE 2010
Human Monoclonal MBL2 Primary Antibody for IP, ELISA - ABIN2192488
Skjoedt, Hummelshoj, Palarasah, Honore, Koch, Skjodt, Garred: A novel mannose-binding lectin/ficolin-associated protein is highly expressed in heart and skeletal muscle tissues and inhibits complement activation. in The Journal of biological chemistry 2010
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this study shows that MBL-C expression is induced in the gut (show GUSB Antibodies) in response to Candida albicans sensing and is required for intestinal homeostasis and host defense against Candida albicans
Targeted deletion of Mbl1/2 causes differential levels of inflammation-related gene sets at baseline and after exposure to ozone and significantly reduces pulmonary inflammation, thus indicating an important innate immunomodulatory role of the Mbl1/2 genes.
Human and murine data together indicate that SP-A, SP-D and MBL are synthesized in early gestational tissues, and may contribute to regulation of immune response at the feto-maternal interface during pregnancy.
These data show that modulation of MBL is involved in the protection against renal I/RI induced by dietary restriction, and suggest that the mechanisms of protection induced by dietary restriction and fasting may be different.
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 (show MASP2 Antibodies) and the complement receptors C3aR (show C3AR1 Antibodies) and C5aR (show C5AR1 Antibodies).
demonstrate that apolipoprotein E (Apoe (show APOE Antibodies)), mannose-binding lectin 2 (Mbl2), and parotid secretory protein (Psp (show BPIFA2 Antibodies)) are present at significantly different quantities in depleted plasma of diabetic NZO mice compared to non-diabetic controls
Data indicate that no change of mannan-binding lectin MBL-A during the study, however, mannan-binding lectin MBL-C concentration increased in median by 3.6-fold (2.9; 4.5-fold) during the study in the diabetic group.
These observations point to a previously unappreciated role for MBL in regulating host resistance and cardiac inflammation during infection with a major human pathogen.
MBL plays a key role in clearing influenza A virus and maintaining lung homeostasis.
Data show that genetically defined MBL-deficiency is associated with a better outcome after acute stroke.
These results indicated that polymorphisms in MBL2 gene may influence susceptibility, progression and prognosis of HBV-related liver diseases.
The article data indicate that rs11003125 in the MBL2 (Mannose Binding Lectin 2) gene was shown to be associated with a high prevalence of caries in our cohort, and 2 haplotypes are also involved in the increased susceptibility to dental caries.
the findings of the current study obtained on mother and children from Zambia evidence lack of association between MBL2 functional polymorphisms and HIV-1 mother-to-child transmission
Mannose-binding lectin levels are largely genetically determined. This relationship was preserved in children during critical illness, despite the effect of large-volume fluid administration on mannose-binding lectin levels. Mannose-binding lectin levels had no association with infection status at admission, or with progression from systemic inflammatory response syndrome to sepsis or septic shock.
Low MBL levels are associated with a higher risk for future cardiac events and cardiovascular events.
results showed that despite MBL2 gene polymorphisms being associated with the protein plasma levels, the polymorphisms were not enough to predict the development of heart disease, regardless of infection with both species of Chlamydia.
MBL2 polymorphisms are associated with higher incidence of development of coronary in-stent restenosis.
MBL2 gene exon1 polymorphisms are associated with increased risk of high-risk HPV infection and cervical cancer development among Caucasians (Meta-Analysis)
In a large cohort of VLBWI MBL2 deficiency had no major impact on infection risk unless children were born between 32 0/7 and 36 6/7 weeks of gestation
The results suggest that the mutations in exon 1 of the MBL2 gene do not contribute directly to the clinical and laboratory features of HCV and HBV infections, but further studies should be performed to confirm whether the wild AA genotype has indirect effect on disease progression.
MBL2 polymorphisms were associated with some disease groups and with the presence of some etiologic agents
MBL1 was also found to be expressed in the lung, testis and brain, whereas low expression of MBL2 was detected in the testis and kidney.
Single nucleotide polymorphisms in MBL2 at exon 1 were detected using polymerase chain reaction single-strand conformation polymorphism analysis and DNA sequencing techniques in 825 Chinese Holstein cows.
the relationship between the variants of the bovine MBL2 gene and milk production traits, mastitis, serum MBL-C levels and hemolytic complement activity in both classical pathway (CH50) and alternative pathway (ACH50) in Chinese Holstein cattle
This gene encodes the soluble mannose-binding lectin or mannose-binding protein found in serum. The protein encoded belongs to the collectin family and is an important element in the innate immune system. The protein recognizes mannose and N-acetylglucosamine on many microorganisms, and is capable of activating the classical complement pathway. Deficiencies of this gene have been associated with susceptibility to autoimmune and infectious diseases.
mannose-binding lectin (protein C) 2, soluble (opsonic defect)
, mannose-binding lectin 2, soluble
, mannose-binding protein C
, Mannose-binding protein C
, RA-reactive factor P28A subunit
, mannan-binding protein
, mannose binding lectin 2 (protein C)
, mannose-binding protein C (liver)
, ra-reactive factor polysaccharide-binding component p28A
, raRF p28A
, mannose binding lectin (C)
, mannose binding lectin, liver (C)
, mannan-binding lectin
, mannose-binding lectin 2, soluble (opsonic defect)
, soluble mannose-binding lectin
, 27 kDa mannan-binding protein monomeric subunit
, c-type lectin
, mannose binding lectin, liver (A)
, mannose-binding lectin 2