MASP antibody Polyclonal Antibodies Primary antibodies
- Known as:
- MASP (anti-) Polyclonal Antibodies Primary antibodies
- Catalog number:
- orb10144
- Product Quantity:
- 100
- Category:
- -
- Supplier:
- Biorb
- Gene target:
- MASP antibody Polyclonal Antibodies Primary antibodies
Related genes to: MASP antibody Polyclonal Antibodies Primary antibodies
- Gene:
- MASP1 NIH gene
- Name:
- mannan binding lectin serine peptidase 1
- Previous symbol:
- CRARF, PRSS5
- Synonyms:
- MASP
- Chromosome:
- 3q27.3
- Locus Type:
- gene with protein product
- Date approved:
- 1995-07-06
- Date modifiied:
- 2019-04-23
- Gene:
- MASP2 NIH gene
- Name:
- mannan binding lectin serine peptidase 2
- Previous symbol:
- MASP1P1
- Synonyms:
- -
- Chromosome:
- 1p36.22
- Locus Type:
- gene with protein product
- Date approved:
- 1998-12-17
- Date modifiied:
- 2019-04-23
Related products to: MASP antibody Polyclonal Antibodies Primary antibodies
Related articles to: MASP antibody Polyclonal Antibodies Primary antibodies
- SLE is a systemic autoimmune disease in which the complement system plays a key pathogenic role, yet the contribution of the lectin pathway remains unclear. Lectin pathway-dependent complement activation is initiated by pattern-recognition molecules complexed with mannose-binding lectin (MBL)-associated serine proteases (MASPs) and MBL-associated proteins (MAPs). Here, we combined biochemical and genetic analyses to explore associations between MASP/MAP proteins, SLE manifestations and autoantibody specificities. - Source: PubMed
Publication date: 2026/04/09
Lindelöf LinneaGarred PeterHong Mun-GwanWahl Vælum SashaHolten Petersen LotteLeonard DagSayadi AhmedOke VilijaNiewold Timothy BDiaz-Gallo Lina-MarcelaSaevarsdottir SaedisGunnarsson IvaSvenungsson ElisabetEriksson Oskar - Hepatitis B vaccination is the most effective strategy for preventing chronic hepatitis B virus (HBV) infection; however, interindividual variability in vaccine-induced antibody responses remains a significant challenge in the field. Innate immune components, particularly lectin complement pathway proteins such as mannose-binding lectin (MBL), mannose-associated serine protease 1 (MASP-1), and mannose-associated serine protease 2 (MASP-2), may contribute to this variability in outcomes. This study aimed to evaluate the association between serum MBL, MASP-1, and MASP-2 levels, birth weight, and humoral response to hepatitis B vaccination in infants. This single-center prospective observational study included 37 term infants who received hepatitis B vaccinations at birth, 1 month, and 6 months of age according to the national immunization schedule. Venous blood samples were collected at month 6, before, and month 7 after the 3rd vaccine dose. Serum MBL, MASP-1, MASP-2, and antiHB levels were measured using commercial ELISA and chemiluminescence assays. Data were analyzed using non-parametric statistical tests and Spearman's correlation analysis. AntiHB levels increased significantly following vaccination (median Pre-3rdVac: 125.8 mIU/mL; Post-3rdVac: 609.7 mIU/mL; < 0.001). MASP-1 concentrations also showed a significant Post-3rdVac increase (median Pre-3rdVac: 809.52 ng/mL; Post-3rdVac: 1133.93 ng/mL; = 0.019). Birth weight was positively correlated with both MASP-1 levels ( = 0.492, = 0.004) and changes in MASP-1 concentrations ( = 0.524, = 0.002) after the third dose. In addition, MASP-1 levels were positively associated with antiHB levels ( = 0.385, = 0.030) and Post-3rdVac antiHB titers ( = 0.493, = 0.004). In contrast, serum MBL and MASP-2 concentrations were not significantly associated with antiHB levels before or after vaccination. MASP-1, but not MBL or MASP-2, is associated with the magnitude of the antibody response to hepatitis B vaccination in infants. These findings suggest that specific components of the lectin pathway may influence vaccine-induced immunity, independent of MBL. Further large-scale studies incorporating genetic and functional analyses are warranted to clarify the mechanisms by which lectin pathway proteins shape hepatitis B vaccine response. - Source: PubMed
Publication date: 2026/01/20
Tapcı Ayşe EsraBulut İsmailTaşar SerçinKallimci ZeynepYetkin Kezban ÇavdarSevim MelihaSerin OğuzhanTaşar Medine AyşinŞenes MehmetAlioğlu Bülent - The historical discovery that thrombin activates Protease-Activated Receptor 4 (PAR4) has paved the way for several novel findings. Besides thrombin, the complement lectin pathway protease Mannose-Binding Lectin-Associated Serine Protease-1 (MASP-1) also binds to PAR4, albeit with lower affinity. Similar to thrombin, MASP-1 activates Ca²⁺ signaling pathways in endothelial cells. MASP-2, a homolog of MASP-1, plays an important role in complement activation; however, its direct interaction with PAR4 has not yet been elucidated. In this study, we performed structural investigations of thrombin, MASP-1, and MASP-2 to evaluate their binding affinities toward the PAR4 peptide. - Source: PubMed
Publication date: 2026/01/20
Saqib UzmaMadhuri MridulHajela SumatiSharma SadhanaHajela Krishnan - We apply mass photometry to measure the mass distributions of individual protein assemblies in native silk dopes from silkworms and spiders. In both systems, we find that protein dimers dominate, but with distinct stabilization mechanisms. In silkworm dope, ∼700 kDa protein particles are sensitive to treatment with dithiothreitol (DTT), forming a new ∼350 kDa species. These results are consistent with the reduction of disulfide-linked heavy-chain homodimers. In spider major ampullate (Ma) dope, ∼550 kDa protein particles dominate, consistent with MaSp1 homodimers and MaSp1-MaSp2 heterodimers. These MaSp dimers are resistant to DTT, indicating they are stabilized primarily through noncovalent interactions. Together, these results reveal fundamental differences in the molecular organization of prespun silk proteins between these systems, with potential implications for the spinning process and the mechanical properties of fibers. More broadly, our findings demonstrate that mass photometry is a powerful tool for characterizing silk protein multimerization and provide direction for future studies of higher-order assemblies under biologically relevant spinning conditions. - Source: PubMed
Publication date: 2025/10/27
Johnson Hannah RDhaliwal Herman KMakasarashvili NinoMalki JohnVasquez FernandoVillarreal DanielShapakidze LadoHolland Gregory PGarmann Rees F - Aristolochic acid I (AAI) activates the complement system, triggering inflammation and renal interstitial fibrosis (RIF). This study investigated the role of mannan-binding lectin serine protease 1 (MASP1) in AAI-induced RIF. Treating human proximal tubular (HK-2) cells with AAI (2.5, 5, 10 μM) increased inflammatory factors, fibrosis proteins, complement factor C3a, and MASP1/MASP2 expression. Similar increases occurred in AAI-treated (5 mg/kg) C57BL/6J mice. Inhibiting MASP1 using siRNA (siMASP1) or an inhibitor (C1INH, 100 μg/mL) in HK-2 cells reduced AAI-induced C3a elevation, complement activation, inflammation, MASP2, and fibrosis proteins. Correspondingly, in situ renal inhibition of MASP1 in mice using adeno-associated virus 9 (AAV9-siMASP1) suppressed complement activation, kidney inflammation, and RIF following AAI exposure. These results demonstrate that AAI promotes RIF by activating the MASP1-complement pathway, leading to C3a release and inflammation. This study elucidates a mechanism for AAI-induced RIF and suggests MASP1 inhibition as a potential therapeutic strategy against AAI toxicity. - Source: PubMed
Publication date: 2025/08/21
Wang ChenZhang HongWang JiaheWu HuiminYe JingZhang QiJiang BaopingChen LangqunWang YingCheng SiyuYing JiahuiXiang YujieCheng YiranZhang Liang