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Common damage-associated molecular patterns (DAMPs) were internalized through the class A scavenger receptors MSR1 (show MSR1 Proteins) and MARCO in vitro. In ischemic murine brain, DAMP (show AMPH Proteins) internalization was largely mediated by MSR1 (show MSR1 Proteins). Combined deficiency for Msr1 (show MSR1 Proteins) and Marco in infiltrating myeloid cells caused impaired clearance of DAMPs, more severe inflammation, and exacerbated neuronal injury in a murine model of ischemic stroke.
Increasing MARCO expression by targeting Nrf2 (show NFE2L2 Proteins) signaling or the Akt (show AKT1 Proteins)-TFEB (show TFEB Proteins)-MARCO pathway are promising strategies to improve bacterial clearance and survival in postinfluenza bacterial pneumonia.
free actin likely contributes to impaired host defense by blocking scavenger receptor binding of bacteria.
this study shows that Marco functions as co-receptor along with TLRs for HMGB1 (show HMGB1 Proteins) in M1-type inflammatory macrophages
MARCO Is Processed by either Macropinocytosis or Endocytosis-Autophagy Pathway
our data demonstrate that MARCO differentially affects TLR-induced DC activation and suggest targeting of MARCO could lead to different outcomes that depend on the inflammatory context encountered by dendritic cells.
Vaccinia virus bound directly to MARCO, and overexpression of MARCO increased susceptibility to vaccinia infection.
MARCO-/- dendritic cells demonstrated enhanced migratory capacity in response to CCL-21 (show CCL21 Proteins) in vitro.
herpes simplex virus type 1 binds to MARCO to enhance its capacity for disease.
results indicate that accumulation of SQSTM1 (show SQSTM1 Proteins) leads to increased activation of NFE2L2 (show NFE2L2 Proteins) and the subsequent increase in MARCO and MSR1 (show MSR1 Proteins)
These data suggest the SRCR domain of MARCO is the key domain in modulating ligand binding, enhancing downstream pro-inflammatory signaling and MARCO-mediated cellular adhesion.
Expression of MARCO declined progressively as hepatocellular carcinoma condition is aggravated.
MARCO single nucleotide polymorphisms rs12998782 increases risk to pulmonary tuberculosis in a Chinese Han population.
CD36 and MARCO are associated with the susceptibility of Chinese Han females to carotid atherosclerosis. Menopausal status may affect the association between gene polymorphisms and carotid atherosclerosis in the female Chinese Han population.
Increasing MARCO expression by targeting Nrf2 (show GABPA Proteins) signaling or the Akt (show AKT1 Proteins)-TFEB (show TFEB Proteins)-MARCO pathway are promising strategies to improve bacterial clearance and survival in postinfluenza bacterial pneumonia.
results suggest that MARCO polymorphisms may regulate phagocytosis of M. tuberculosis and susceptibility and severity of pulmonary tuberculosis
this paper shows that key gene of intermediate proinflammatory monocytes, such as MARCO, is expressed three- to fourfold more in juvenile idiopathic arthritis-enthesitis-related arthritis
this study shows that MARCO modulates inflammatory responses against Cryptococcus neoformans infection
this translational investigation identified gene candidates, including Marco, for host susceptibility to multiple phenotypes of RSV disease in mice that closely mimic human disease, and a polymorphism in human MARCO associated with increased risk of RSV disease severity in infants.
Identifying N-linked glycan moiety and motifs in the cysteine-rich domain critical for N-glycosylation and intracellular trafficking of SR-AI (show MSR1 Proteins) and MARCO.
The protein encoded by this gene is a member of the class A scavenger receptor family and is part of the innate antimicrobial immune system. The protein may bind both Gram-negative and Gram-positive bacteria via an extracellular, C-terminal, scavenger receptor cysteine-rich (SRCR) domain. In addition to short cytoplasmic and transmembrane domains, there is an extracellular spacer domain and a long, extracellular collagenous domain. The protein may form a trimeric molecule by the association of the collagenous domains of three identical polypeptide chains.
macrophage receptor MARCO
, scavenger receptor class A member 2
, scavenger receptor class A, member 2
, putative scavenger receptor MARCO