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anti-Human Apolipoprotein C-II Antibodies:
anti-Rat (Rattus) Apolipoprotein C-II Antibodies:
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the apoc2 mutant zebrafish is a robust and versatile animal model to study hypertriglyceridemia.
The effect of apolipoprotein C2 K30D-D69K mutations on rod-like apolipoprotein C2 fibril formation.
Results from this exploratory analysis suggest that regulatory element methylation levels within the larger TOMM40-APOE-APOC2 gene region correlate with AD-related biomarkers and TOMM40 or APOE gene expression in AD.
Triglyceride-raising variant alleles of the APOC2 encoding apo C-II, associated with clinical Cardiovascular endpoints.
The results demonstrate the important role of both intra- and inter-subunit charge interactions in stabilizing apoC-II amyloid fibrils, a process that may be a key factor in determining the general ability of proteins to form amyloid fibrils.
The results highlight the importance of charge-pair interactions within the apoC-II fibril core
Conformational rearrangement of apoC-II at lipoprotein surfaces promotes interaction with LPL.
Large deletion in APOC2 caused by Alu-Alu homologous recombination is associated with with apolipoprotein C-II deficiency.
No APOC2 mutations were identified in a cohort of patients with diabetic lipemia.
Six apolipoproteins (APOA1, APOA2, APOB, APOC2, APOC3, and APOE) were able to differentiate bladder cancer from hernia. SAA4 was significantly increased in bladder cancer subgroups, whereas ProEGF was significantly decreased in bladder cancer subgroups.
STAT1 bound on multienhancer 2 cooperates with RXRalpha located on apoCII promoter and upregulates apoCII expression only in macrophages.
Mutations in GPIHBP1 are rare but the associated clinical phenotype of hypertriglyceridaemia is severe
These results support a predictive change in the ratio of plasma ApoCIII to ApoCII in pregnancies complicated by severe preeclampsia.
Substoichiometric concentrations of cyc[60-70] significantly delayed fibril formation by the fibrillogenic, linear peptides apoC-II[60-70] and apoC-II[56-76].
Activation of apoC-II fibrils by submicellar lipid (NBD-lyso-12-phosphocholine) is catalytic with release of monomer- and tetramer-bound lipid accompanying fibril elongation and growth.
variants in LPL, OASL and TOMM40/APOE-C1-C2-C4 genes are associated with multiple cardiovascular-related traits
Physiological shear flow conditions and conditions experienced during apoC-II manufacturing exert significant effects on apoC-II conformation, leading to protein misfolding, aggregation, and amyloid fibril formation.
Includes the observation of APOC4-APOC2 read-through transcription
Our structural model for apoC-II fibrils suggests that apoC-II monomers fold and self-assemble to form a stable cross-beta-scaffold containing relatively unstructured connecting loops.
This study examines the association between APOE/C1/C4/C2 gene cluster variation using tagging single nucleotide polymorphisms and plasma lipid concentration along with risk of coronary heart disease in a prospective cohort.
Results describe the functional role of the secondary structure in the lipoprotein lipase-binding portion of apolipoprotein CII.
A novel mouse model of apoC-II deficiency was created with an apoC-II peptide that reverses the hypertriglyceridemia.
Data show that apoC-II and LPL mRNAs correlate temporally and geographically with surfactant lipid synthesis in preparation for birth and suggest that fatty acid recruitment from the circulation by apoC-II-activated LPL is modulated by apoC-II secretion.
regulated expression of gene cluster in macrophages
TR4 can also regulate apolipoprotein E, C-I, and C-II gene expression via the TR4 response element within the hepatic control region
These results are compatible with a role for apolipoproteins in lipid metabolism and transport in the developing lung in association with the sex difference in surfactant lipid synthesis.
This gene encodes a lipid-binding protein belonging to the apolipoprotein gene family. The protein is secreted in plasma where it is a component of very low density lipoprotein. This protein activates the enzyme lipoprotein lipase, which hydrolyzes triglycerides and thus provides free fatty acids for cells. Mutations in this gene cause hyperlipoproteinemia type IB, characterized by hypertriglyceridemia, xanthomas, and increased risk of pancreatitis and early atherosclerosis. This gene is present in a cluster with other related apolipoprotein genes on chromosome 19. Naturally occurring read-through transcription exists between this gene and the neighboring upstream apolipoprotein C-IV (APOC4) gene.
, apolipoprotein C2