catalog number :
MBS968139
products type :
Recombinant Protein
products full name :
Recombinant Human Apolipoprotein C-III
products short name :
Apolipoprotein C-III
products name syn :
Apolipoprotein C3
other names :
apolipoprotein C-III; Apolipoprotein C-III; apolipoprotein C-III; apolipoprotein C-III; Apolipoprotein C3
products gene name :
APOC3
other gene names :
APOC3; APOC3; HALP2; APOCIII; Apo-CIII; ApoC-III
uniprot entry name :
APOC3_HUMAN
host :
E Coli or Yeast or Baculovirus or Mammalian Cell
sequence positions :
21-99
sequence :
SEAEDASLLSFMQGYMKHATKTAKDALSSVQESQVAQQA
RGWVTDGFSSLKDYWSTVKDKFSEFWDLDPEVRPTSAVA
A
purity :
Greater than 90% as determined by SDS-PAGE.
form :
Liquid containing glycerol; lyophilization may be available upon request.
storage stability :
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
products categories :
Metabolism
products description :
Component of triglyceride-rich very low density lipoproteins (VLDL) and high density lipoproteins (HDL) in plasma. Plays a multifaceted role in triglyceride homeostasis. Intracellularly, promotes hepatic very low density lipoprotein 1 (VLDL1) assembly and secretion; extracellularly, attenuates hydrolysis and clearance of triglyceride-rich lipoproteins (TRLs). Impairs the lipolysis of TRLs by inhibiting lipoprotein lipase and the hepatic uptake of TRLs by remnant receptors.
products references :
Isolation and sequence analysis of the human apolipoprotein CIII gene and the intergenic region between the apo AI and apo CIII genes.Protter A.A., Levy-Wilson B., Miller J., Bencen G., White T., Seilhamer J.J.DNA 3:449-456(1984)
Isolation and DNA sequence of full-length cDNA for human preapolipoprotein CIII.Levy-Wilson B., Appleby V., Protter A.A., Auperin D., Seilhamer J.J.DNA 3:359-364(1984)
Isolation and characterization of cDNA clones corresponding to two different human apoC-III alleles.Karathanasis S.K., Zannis V.I., Breslow J.L.J. Lipid Res. 26:451-456(1985)
Human apolipoproteins AI, AII, CII and CIII. cDNA sequences and mRNA abundance.Sharpe C.R., Sidoli A., Shelley C.S., Lucero M.A., Shoulders C.C., Baralle F.E.Nucleic Acids Res. 12:3917-3932(1984)
The effects of scale
variation in the APOA1/C3/A4/A5 gene cluster.Fullerton S.M., Buchanan A.V., Sonpar V.A., Taylor S.L., Smith J.D., Carlson C.S., Salomaa V., Stengaard J.H., Boerwinkle E., Clark A.G., Nickerson D.A., Weiss K.M.Hum. Genet. 115:36-56(2004)
Amino acid sequence of human plasma apolipoprotein C-III from normolipidemic subjects.Hospattankar A.V., Brewer H.B. Jr., Ronan R., Fairwell T.FEBS Lett. 197:67-73(1986)
The complete amino acid sequence of alanine apolipoprotein (apoC-3)
, and apolipoprotein from human plasma very low density lipoproteins.Brewer H.B. Jr., Shulman R., Herbert P., Ronan R., Wehrly K.J. Biol. Chem. 249:4975-4984(1974)
An ABC of apolipoprotein C-III
a clinically useful new cardiovascular risk factor?Chan D.C., Chen M.M., Ooi E.M., Watts G.F.Int. J. Clin. Pract. 62:799-809(2008)
Enrichment of glycopeptides for glycan structure and attachment site identification.Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., Larson G.Nat. Methods 6:809-811(2009)
Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011)
Apolipoprotein C-III and hepatic triglyceride-rich lipoprotein production.Yao Z., Wang Y.Curr. Opin. Lipidol. 23:206-212(2012)
Identification of new apolipoprotein-CIII glycoforms with ultrahigh resolution MALDI-FTICR mass spectrometry of human sera.Nicolardi S., van der Burgt Y.E., Dragan I., Hensbergen P.J., Deelder A.M.J. Proteome Res. 12:2260-2268(2013)
An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014)
Molecular cloning of a human apoC-III variant
Thr 74-->Ala 74 mutation prevents O-glycosylation.Maeda H., Hashimoto R.K., Oguro T., Hiraga S., Uzawa H.J. Lipid Res. 28:1405-1409(1987)
Apolipoprotein C-III(Lys-58-->Glu)
. Identification of an apolipoprotein C-III variant in a family with hyperalphalipoproteinemia.von Eckardstein A., Holz H., Sandkamp M., Weng W., Funke H., Assmann G.J. Clin. Invest. 87:1724-1731(1991)
ncbi acc num :
NP_000031.1
ncbi gb acc num :
NM_000040.1
ncbi pathways :
Chylomicron-mediated Lipid Transport Pathway (1270006); HDL-mediated Lipid Transport Pathway (1270007); Lipid Digestion, Mobilization, And Transport Pathway (1270002); Lipoprotein Metabolism Pathway (1270005); Metabolism Pathway (1269956); Metabolism Of Fat-soluble Vitamins Pathway (1339147); Metabolism Of Lipids And Lipoproteins Pathway (1270001); Metabolism Of Vitamins And Cofactors Pathway (1270144); PPAR Signaling Pathway (83042); PPAR Signaling Pathway (450)
ncbi summary :
Apolipoprotein C-III is a very low density lipoprotein (VLDL) protein. APOC3 inhibits lipoprotein lipase and hepatic lipase; it is thought to delay catabolism of triglyceride-rich particles. The APOA1, APOC3 and APOA4 genes are closely linked in both rat and human genomes. The A-I and A-IV genes are transcribed from the same strand, while the A-1 and C-III genes are convergently transcribed. An increase in apoC-III levels induces the development of hypertriglyceridemia. [provided by RefSeq, Jul 2008]
uniprot summary :
APOC3: Inhibits lipoprotein lipase and hepatic lipase and decreases the uptake of lymph chylomicrons by hepatic cells. This suggests that it delays the catabolism of triglyceride-rich particles. Defects in APOC3 are the cause of hyperalphalipoproteinemia type 2 (HALP2). HALP2 is a condition characterized by high levels of high density lipoprotein (HDL) and increased HDL cholesterol levels. Belongs to the apolipoprotein C3 family. Protein type: Secreted; Secreted, signal peptide; Lipid-binding. Chromosomal Location of Human Ortholog: 11q23.3. Cellular Component: chylomicron; early endosome; extracellular region; extracellular space. Molecular Function: cholesterol binding; enzyme regulator activity; lipase inhibitor activity; phospholipid binding. Biological Process: cholesterol efflux; cholesterol homeostasis; cholesterol metabolic process; fat-soluble vitamin metabolic process; G-protein coupled receptor protein signaling pathway; inflammatory response; lipoprotein metabolic process; lipoprotein transport; negative regulation of fatty acid biosynthetic process; negative regulation of lipid catabolic process; negative regulation of lipid metabolic process; negative regulation of lipoprotein lipase activity; negative regulation of receptor-mediated endocytosis; phospholipid efflux; phototransduction, visible light; regulation of Cdc42 protein signal transduction; response to peptide hormone stimulus; response to triglyceride; response to vitamin A; retinoid metabolic process; reverse cholesterol transport; triacylglycerol catabolic process; triacylglycerol metabolic process; triacylglycerol mobilization; vitamin metabolic process. Disease: Apolipoprotein C-iii Deficiency