protein

Recombinant Human Apolipoprotein A-IV

MBS1002082

0.01 mg (E-Coli)

160 USD

Recombinant Protein

Recombinant Human Apolipoprotein A-IV

[Apolipoprotein A-IV]

[Apolipoprotein A4]

[Apolipoprotein A-IV; Apolipoprotein A4]

[APOA4]

[APOA4; Apo-AIV; ApoA-IV]

APOA4_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

[21-396aa; Full Length]

396

EVSADQVATVMWDYFSQLSNNAKEAVEHLQKSELTQQLN
ALFQDKLGEVNTYAGDLQKKLVPFATELHERLAKDSEKL
KEEIGKELEELRARLLPHANEVSQKIGDNLRELQQRLEP
YADQLRTQVNTQAEQLRRQLTPYAQRMERVLRENADSLQ
ASLRPHADELKAKIDQNVEELKGRLTPYADEFKVKIDQT
VEELRRSLAPYAQDTQEKLNHQLEGLTFQMKKNAEELKA
RISASAEELRQRLAPLAEDVRGNLRGNTEGLQKSLAELG
GHLDQQVEEFRRRVEPYGENFNKALVQQMEQLRQKLGPH
AGDVEGHLSFLEKDLRDKVNSFFSTFKEKESQDKTLSLP
ELEQQQEQQQEQQQEQVQMLAPLES

Greater than 90% as determined by SDS-PAGE.

Liquid containing glycerol

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Cardiovascular

May have a role in chylomicrons and VLDL secretion and catabolism. Required for efficient activation of lipoprotein lipase by ApoC-II; potent activator of LCAT. Apoa-IV is a major component of HDL and chylomicrons.

Structure, evolution, and tissue-specific synthesis of human apolipoprotein AIV.Karathanasis S.K., Yunis I.Biochemistry 25:3962-3970(1986) Structure, evolution, and polymorphisms of the human apolipoprotein A4 gene (APOA4) .Karathanasis S.K., Oettgen P., Haddad I.A., Antonarakis S.E.Proc. Natl. Acad. Sci. U.S.A. 83:8457-8461(1986) Structure and expression of the human apolipoprotein A-IV gene.Elshourbagy N.A., Walker D.W., Paik Y.K., Boguski M.S., Freeman M., Gordon J.I., Taylor J.M.J. Biol. Chem. 262:7973-7981(1987) The primary structure of human apolipoprotein A-IV.Yang C., Gu Z.W., Xiong W., Rosseneu M., Yang H.X., Lee B.M., Gotto A.M. Jr., Chan L.Biochim. Biophys. Acta 1002:231-237(1989) 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) Human chromosome 11 DNA sequence and analysis including novel gene identification.Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.Nature 440:497-500(2006) The nucleotide and derived amino acid sequence of human apolipoprotein A-IV mRNA and the close linkage of its gene to the genes of apolipoproteins A-I and C-III.Elshourbagy N.A., Walker D.W., Boguski M.S., Gordon J.I., Taylor J.M.J. Biol. Chem. 261:1998-2002(1986) Biosynthesis of human preapolipoprotein A-IV.Gordon J.I., Bisgaier C.L., Sims H.F., Sachdev O.P., Glickman R.M., Strauss A.W.J. Biol. Chem. 259:468-474(1984) Genetic polymorphism of apolipoprotein A-IV.Lohse P., Brewer H.B. Jr.Curr. Opin. Lipidol. 2:90-95(1991) Genetic polymorphism of human plasma apolipoprotein A-IV is due to nucleotide substitutions in the apolipoprotein A-IV gene.Lohse P., Kindt M.R., Rader D.J., Brewer H.B. Jr.J. Biol. Chem. 265:10061-10064(1990) Human plasma apolipoproteins A-IV-0 and A-IV-3. Molecular basis for two rare variants of apolipoprotein A-IV-1.Lohse P., Kindt M.R., Rader D.J., Brewer H.B. Jr.J. Biol. Chem. 265:12734-12739(1990) 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) The structure of dimeric apolipoprotein A-IV and its mechanism of self-association.Deng X., Morris J., Dressmen J., Tubb M.R., Tso P., Jerome W.G., Davidson W.S., Thompson T.B.Structure 20:767-779(2012) The mutation causing the common apolipoprotein A-IV polymorphism is a glutamine to histidine substitution of amino acid 360.Tenkanen H., Lukka M., Jauhiainen M., Metso J., Baumann M., Peltonen L., Ehnholm C.Arterioscler. Thromb. 11:851-856(1991) Three genetic variants of human plasma apolipoprotein A-IV apoA-IV-1(Thr-347-->Ser) , apoA-IV-0(Lys-167-->Glu,Gln-360-->His) , and apoA-IV-3(Glu-165-->Lys) .Lohse P., Kindt M.R., Rader D.J., Brewer H.B. Jr.J. Biol. Chem. 266:13513-13518(1991) ErratumLohse P., Kindt M.R., Rader D.J., Brewer H.B. Jr.J. Biol. Chem. 266:19866-19866(1991) Nonsynonymous polymorphic sites in the apolipoprotein (apo) A-IV gene are associated with changes in the concentration of apo B- and apo A-I-containing lipoproteins in a normal population.von Eckardstein A., Funke H., Schulte M., Erren M., Schulte H., Assmann G.Am. J. Hum. Genet. 50:1115-1128(1992) A novel polymorphism of apolipoprotein A-IV is the result of an asparagine to serine substitution at residue 127.Tenkanen H., Koskinen P., Metso J., Baumann M., Lukka M., Kauppinen-Makelin R., Kontula K., Taskinen M.R., Manttari M., Manninen V., Ehnholm C.Biochim. Biophys. Acta 1138:27-33(1992) Molecular basis of a unique African variant (A-IV 5) of human apolipoprotein A-IV and its significance in lipid metabolism.Kamboh M.I., Williams E.R., Law J.C., Aston C.E., Bunker C.H., Ferrell R.E., Pollitzer W.S.Genet. Epidemiol. 9:379-388(1992) Apolipoprotein A-IV polymorphism in the Hungarian population gene frequencies, effect on lipid levels, and sequence of two new variants.Menzel H.J., Dieplinger H., Sandholzer C., Karadi I., Utermann G., Csaszar A.Hum. Mutat. 5:58-65(1995) Two novel apolipoprotein A-IV variants in individuals with familial combined hyperlipidemia and diminished levels of lipoprotein lipase activity.Deeb S.S., Nevin D.N., Iwasaki L., Brunzell J.D.3.3.CO;2-T>Hum. Mutat. 8:319-325(1996) Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis.Halushka M.K., Fan J.-B., Bentley K., Hsie L., Shen N., Weder A., Cooper R., Lipshutz R., Chakravarti A.Nat. Genet. 22:239-247(1999) 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)

P06727

59.4kD

Apoliprotein (apo) A-IV gene contains 3 exons separated by two introns. A sequence polymorphism has been identified in the 3'UTR of the third exon. The primary translation product is a 396-residue preprotein which after proteolytic processing is secreted its primary site of synthesis, the intestine, in association with chylomicron particles. Although its precise function is not known, apo A-IV is a potent activator of lecithin-cholesterol acyltransferase in vitro. [provided by RefSeq, Jul 2008]

APOA4: May have a role in chylomicrons and VLDL secretion and catabolism. Required for efficient activation of lipoprotein lipase by ApoC-II; potent activator of LCAT. Apoa-IV is a major component of HDL and chylomicrons. Synthesized primarily in the intestine and secreted in plasma. Belongs to the apolipoprotein A1/A4/E family. Protein type: Lipid-binding; Secreted, signal peptide; Endoplasmic reticulum; Cell adhesion; Secreted. Chromosomal Location of Human Ortholog: 11q23. Cellular Component: cell surface; chylomicron; cytosol; early endosome; endoplasmic reticulum lumen; extracellular region; extracellular space. Molecular Function: antioxidant activity; cholesterol binding; cholesterol transporter activity; copper ion binding; lipid binding; lipid transporter activity; phosphatidylcholine binding; protein binding; protein homodimerization activity. Biological Process: cellular protein metabolic process; cholesterol biosynthetic process; cholesterol efflux; cholesterol homeostasis; cholesterol metabolic process; fat-soluble vitamin metabolic process; hydrogen peroxide catabolic process; innate immune response in mucosa; leukocyte adhesion; lipid homeostasis; lipid transport; lipoprotein metabolic process; multicellular organismal lipid catabolic process; neurite regeneration; phosphatidylcholine metabolic process; phospholipid efflux; phototransduction, visible light; positive regulation of fatty acid biosynthetic process; positive regulation of lipoprotein lipase activity; protein-lipid complex assembly; regulation of cholesterol absorption; regulation of cholesterol transport; removal of superoxide radicals; response to lipid hydroperoxide; retinoid metabolic process; reverse cholesterol transport; triacylglycerol catabolic process; vitamin metabolic process

0.01 mg (E-Coli)

160 USD

0.01 mg (Yeast)

175

0.05 mg (E-Coli)

200

0.05 mg (Yeast)

225

0.1 mg (E-Coli)

295

0.1 mg (Yeast)

355

0.2 mg (E-Coli)

480

0.2 mg (Yeast)

565

0.5 mg (E-Coli)

790

0.5 mg (Yeast)

925

1 mg (E-Coli)

1215

1 mg (Yeast)

1410