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The protein encoded by SCARB2 is a type III glycoprotein that is located primarily in limiting membranes of lysosomes and endosomes. Additionally we are shipping SCARB2 Antibodies (77) and SCARB2 Kits (11) and many more products for this protein.
Showing 10 out of 16 products:
This work describes a novel function for the Scarb2 receptor as an essential glycoprotein for notochord development.
Crystal structure of a LIMP-2 luminal domain dimer with bound cholesterol and phosphatidylcholine is described. Binding of these lipids alters LIMP-2 from functioning as a glucocerebrosidase-binding monomer toward a dimeric state that preferentially binds anionic phosphatidylserine over neutral phosphatidylcholine.
The binding of a monoclonal antibody to the apical region of SCARB2 blocks EV71 infection.
The findings identify SR-BII as a functional SAA (show SAA1 Proteins) receptor that mediates SAA (show SAA1 Proteins) uptake and contributes to its proinflammatory signaling via the MAPK (show MAPK1 Proteins)-mediated signaling pathways.
In this paper we provide an updated overview of the clinical and genetic features of SCARB2-related PME (show CSTB Proteins) and on the functions of the LIMP2 protein [review]
neutrophils are able to drive a macrophage activation that would regulate the increase in LIMP-2 expression during the early phase of Cer (show CBLN1 Proteins)-induced acute pancreatitis
Findings suggested that STX1B (show STX1B Proteins) rs4889603, FAM47E rs6812193 and SCARB2 rs6825004 do not confer a significant risk for Parkinson's disease
LIMPII was increased greater than twofold in urinary microvesicles obtained from patients with idiopathic membranous nephropathy compared to microvesicles of patients with idiopathic focal segmental glomerulosclerosis and normal controls.
hSR-BII (show CACNA1E Proteins), and to a lesser extent hSR-BI, significantly increase LPS (show IRF6 Proteins)-induced inflammation and contribute to LPS (show IRF6 Proteins)-induced tissue injury in the liver and kidney, two major organs susceptible to LPS (show IRF6 Proteins) toxicity.
Although hrGCase cellular uptake is independent of LIMP-2, its trafficking to the lysosomes is mediated by this receptor.
SNCA and SCARB2 loci are also associated with dementia with Lewy bodies, after a study-wise Bonferroni correction, although these have a different association profile than the associations reported for the same loci in Parkinson's.
LIMP-2 facilitates transport of phospholipids into murine fibroblasts, with a strong substrate preference for phosphatidylserine.
AP-3 (show AP3B1 Proteins)-dependent LB targeting is facilitated by protein/protein interaction between LIMP-2/SCARB2 and PRDX6 (show PRDX6 Proteins) in vitro and in vivo
Heterologous expression of the luminal domain of LIMP-2 in wild-type cells.
In LIMP-2-deficient brains a significant reduction in GC activity led to lipid storage, disturbed autophagic/lysosomal function, and alpha-synuclein accumulation.
absence of Limp-2 reduces inflammation in experimental crescentic glomerulonephritis with decreased macrophage and T-cell infiltration in the kidney.
Limp-2 deficiency leads to a minor increase in circulating renin (show REN Proteins). Limp-2, however, is not required for acute or chronic stimulation of renin (show REN Proteins) release.
The SR-BII is involved in cholesterol ester uptake for steroidogenesis and spermatogenesis in the testis.
The residues between 144 and 151 are critical for SCARB2 binding to VP1 of EV71 and seven residues from the human receptor could convert murine SCARB2, an otherwise inefficient receptor, to an efficient receptor for EV71 viral infection.
The data suggest that tubular proteinuria in Limp-2(-/-) mice is due to failure of endosomes containing reabsorbed proteins to fuse with lysosomes in the proximal tubule of the kidney. Failure of proteolysis is a novel mechanism for tubular proteinuria.
The protein encoded by this gene is a type III glycoprotein that is located primarily in limiting membranes of lysosomes and endosomes. Earlier studies in mice and rat suggested that this protein may participate in membrane transportation and the reorganization of endosomal/lysosomal compartment. The protein deficiency in mice was reported to impair cell membrane transport processes and cause pelvic junction obstruction, deafness, and peripheral neuropathy. Further studies in human showed that this protein is a ubiquitously expressed protein and that it is involved in the pathogenesis of HFMD (hand, foot, and mouth disease) caused by enterovirus-71 and possibly by coxsackievirus A16. Mutations in this gene caused an autosomal recessive progressive myoclonic epilepsy-4 (EPM4), also known as action myoclonus-renal failure syndrome (AMRF). Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
CD36 antigen (collagen type I receptor, thrombospondin receptor)-like 2
, CD36 antigen-like 2
, lysosome membrane protein 2
, scavenger receptor class B, member 2
, lysosome membrane protein 2-like
, putative lysosomal integral membrane protein II
, 85 kDa lysosomal membrane sialoglycoprotein
, 85 kDa lysosomal sialoglycoprotein scavenger receptor class B, member 2
, CD36 antigen (collagen type I receptor, thrombospondin receptor)-like 2 (lysosomal integral membrane protein II)
, LIMP II
, lysosome membrane protein II