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APOA1 protein :: Apolipoprotein A1 Protein

Catalog #    MBS173020 APOA1 protein
Unit / Price
0.1 mg  /  $140 +1 FREE 8GB USB
0.5 mg  /  $275 +1 FREE 8GB USB
1 mg  /  $360 +1 FREE 8GB USB
3 mg  /  $600 +1 FREE 8GB USB
 Go to:     Product Names    Product Info    Accession #s    Product Desc    Diseases/Tissues/Pathways    Applications    References 
 Product Name   

Apolipoprotein A1 (APOA1), Protein

 Also Known As   

Apolipoprotein A1 Human Serum

 Product Synonym Names    Lipoproteins A1; apo A1; Apolipoprotein A1 (APO A1), Human Serum - >=96% (SDS-PAGE)
 Product Gene Name   

APOA1 protein

[Similar Products]
 OMIM    phenotype 604091
 Purity/Purification    >= 96% (SDS-PAGE)
 Form/Format    0.2 micron filtered solution in 50mM tris, 150mM Sodium chloride, 1mg/ml sodium azide, and 1mg/ml disodium EDTA, pH 7.4
 Source    Human Serum
 UNSPSC Code    51131909
 Protein    0.9mg/ml (BCA)
 Preservatives    Sodium Azide
 pH    7.4
 Note    Product is soluble in aqueous buffers at low concentrations (<50ug/ml), but due to amphipathic nature, it will self-associate into oligomers at high concentrations in the absence of chaotropes (urea, guanine hydrochloride)
 Preparation and Storage    At -20 degree C
 Other Notes for APOA1 protein    Small volumes of APOA1 protein may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice.
 Searchable Terms for APOA1 purchase    anti-APOA1 cost; Buy APOA1 protein, Apolipoprotein A1 Protein (MBS173020) product datasheet at MyBioSource, Proteins; Proteins; Antigens; Standards/controls; Native Proteins; Apolipoprotein A1 (apo A1); 335; APOA1_HUMAN; APOA1 protein price; protein for APOA1

Product Description specifically for APOA1 protein

   Custom preparations, technical support, bulk quantities and aliquoting available.

Single polypeptide chain in 245 amino acids with high alpha-helical content, major structurual component of high density lipoproteins, cofactor for lecthin:cholesterol acyltransferase, levels in general are inversely related to risk of coronary artery disease in humans.

Human APO A1 is isolated by ultracentrifugation, delipidated and ion-exchange chromatography and is soluble in aqueous buffers at low concentrations (<50ug/mL) but due to amphipathic nature, APO A1 will self-associate into oligomers at high concentrations in the absence of chaotrupes (urea, guanidine hydrochloride).

Apo-AI comprises ~70% of the protein moiety in HDL. It is a single polypeptide chain consisting of 245 amino acids with glutamic acid as the C-terminal residue and aspartic acid as the N-terminal residue. The molecular mass is reported to be 28.3 kDa. The protein is made up of one major isoform (pI 5.6) and two minor isoforms (pI 5.53 and 5.46). Apo-AI shows a high content of -helix structure. The amphipathic regions in the -helix structure seem to be responsible for lipid binding capacity. In aqueous solution, Apo-AI shows self-association with minor conformation change. Apo-AI activates lecithin-cholesterol (LCAT) acyltransferase, which is responsible for cholesterol esterification in plasma.

Apo-AI levels in normal plasma are 90-130 mg/dL. Apo-AI levels may be inversely related to the risk of coronary disease.
 Product Categories/Family for APOA1 protein    Proteins; Antigens; Standards/controls; Native Proteins; Apolipoprotein A1 (apo A1)
NCBI/Uniprot data below describe general gene information for APOA1. It may not necessarily be applicable to this product.
 NCBI GI #    4557321
 NCBI GeneID    335
 NCBI Accession #    NP_000030.1 [Other Products]
 NCBI GenBank Nucleotide #    NM_000039.1 [Other Products]
 UniProt Secondary Accession #    Q6LDN9; Q6Q785; Q9UCS8; Q9UCT8; A8K866 [Other Products]
 UniProt Related Accession #    P02647 [Other Products]
 Molecular Weight    28.3 kDa [Similar Products]
 NCBI Official Full Name    apolipoprotein A-I preproprotein
 NCBI Official Synonym Full Names    apolipoprotein A-I
 NCBI Official Symbol    APOA1 [Similar Products]
 NCBI Protein Information    apolipoprotein A-I; apo-AI
 UniProt Protein Name    Apolipoprotein A-I
 UniProt Synonym Protein Names   

Apolipoprotein A1Cleaved into the following 2 chains:Proapolipoprotein A-I; ProapoA-I; Truncated apolipoprotein A-IAlternative name(s):Apolipoprotein A-I(1-242)

 UniProt Gene Name    APOA1 [Similar Products]
 UniProt Synonym Gene Names    Apo-AI; ApoA-I; ProapoA-I [Similar Products]
 UniProt Entry Name    APOA1_HUMAN
 NCBI Summary for APOA1    This gene encodes apolipoprotein A-I, which is the major protein component of high density lipoprotein (HDL) in plasma. The protein promotes cholesterol efflux from tissues to the liver for excretion, and it is a cofactor for lecithin cholesterolacyltransferase (LCAT) which is responsible for the formation of most plasma cholesteryl esters. This gene is closely linked with two other apolipoprotein genes on chromosome 11. Defects in this gene are associated with HDL deficiencies, including Tangier disease, and with systemic non-neuropathic amyloidosis. [provided by RefSeq, Jul 2008]
 UniProt Comments for APOA1    APOA1: Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility. Interacts with APOA1BP and CLU. Component of a sperm activating protein complex (SPAP), consisting of APOA1, an immunoglobulin heavy chain, an immunoglobulin light chain and albumin. Interacts with NDRG1. Major protein of plasma HDL, also found in chylomicrons. Synthesized in the liver and small intestine. The oxidized form at Met-110 and Met-136 is increased in individuals with increased risk for coronary artery disease, such as in carrier of the eNOSa/b genotype and exposure to cigarette smoking. It is also present in increased levels in aortic lesions relative to native ApoA-I and increased levels are seen with increasing severity of disease. Belongs to the apolipoprotein A1/A4/E family.

Protein type: Endoplasmic reticulum; Lipid-binding; Motility/polarity/chemotaxis; Secreted, signal peptide; Secreted; Vesicle; Cell development/differentiation

Chromosomal Location of Human Ortholog: 11q23-q24

Cellular Component: extracellular space; chylomicron; cell surface; endoplasmic reticulum lumen; endocytic vesicle; early endosome; plasma membrane; extracellular region; cytoplasmic vesicle; nucleus; cytosol; vesicle

Molecular Function: identical protein binding; protein binding; enzyme binding; phospholipid transporter activity; lipase inhibitor activity; beta-amyloid binding; chemorepellent activity; cholesterol transporter activity; cholesterol binding; phospholipid binding; phosphatidylcholine binding; apolipoprotein A-I receptor binding; high-density lipoprotein binding; apolipoprotein receptor binding

Biological Process: phototransduction, visible light; negative chemotaxis; negative regulation of lipase activity; axon regeneration in the peripheral nervous system; negative regulation of interleukin-1 beta secretion; sequestering of lipid; regulation of cholesterol absorption; transforming growth factor beta receptor signaling pathway; positive regulation of stress fiber formation; response to drug; cholesterol metabolic process; platelet activation; organ regeneration; regulation of Cdc42 protein signal transduction; adrenal gland development; positive regulation of hydrolase activity; positive regulation of Rho protein signal transduction; lipoprotein metabolic process; positive regulation of transferase activity; vitamin transport; cholesterol biosynthetic process; negative regulation of cytokine secretion during immune response; cholesterol homeostasis; lipoprotein biosynthetic process; response to estrogen stimulus; peptidyl-methionine modification; phosphatidylcholine biosynthetic process; positive regulation of lipoprotein lipase activity; blood vessel endothelial cell migration; cellular lipid metabolic process; platelet degranulation; phospholipid efflux; retinoid metabolic process; transmembrane transport; response to nutrient; phospholipid homeostasis; integrin-mediated signaling pathway; receptor-mediated endocytosis; positive regulation of fatty acid biosynthetic process; regulation of protein amino acid phosphorylation; cholesterol transport; negative regulation of heterotypic cell-cell adhesion; protein stabilization; protein amino acid oxidation; neurite regeneration; cholesterol efflux; glucocorticoid metabolic process; G-protein coupled receptor protein signaling pathway; reverse cholesterol transport; endothelial cell proliferation; negative regulation of inflammatory response; blood coagulation

Disease: Hypoalphalipoproteinemia, Primary; Amyloidosis, Familial Visceral
 UniProt References for APOA1    1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis. NHLBI resequencing and genotyping service (RS&G) Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
2. Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."The MGC Project TeamGenome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain and Skeletal muscle. "Human plasma proapoA-I: isolation and amino-terminal sequence."Brewer H.B. Jr., Fairwell T., Kay L., Meng M., Ronan R., Law S., Light J.A.Biochem. Biophys. Res. Commun. 113:626-632(1983) [PubMed] [Europe PMC] [Abstract]. Cited for: PROTEIN SEQUENCE OF 19-27. "The primary structure of human plasma high density apolipoprotein glutamine I (ApoA-I). II. The amino acid sequence and alignment of cyanogen bromide fragments IV, III, and I."Baker H.N., Gotto A.M. Jr., Jackson R.L.J. Biol. Chem. 250:2725-2738(1975) [PubMed] [Europe PMC] [Abstract]. Cited for: PROTEIN SEQUENCE OF 25-267. "The amino acid sequence of human APOA-I, an apolipoprotein isolated from high density lipoproteins."Brewer H.B. Jr., Fairwell T., Larue A., Ronan R., Houser A., Bronzert T.J.Biochem. Biophys. Res. Commun. 80:623-630(1978) [PubMed] [Europe PMC] [Abstract]. Cited for: PROTEIN SEQUENCE OF 25-267. "Serum prostacyclin stabilizing factor is identical to apolipoprotein A-I (Apo A-I). A novel function of Apo A-I."Yui Y., Aoyama T., Morishita H., Takahashi M., Takatsu Y., Kawai C.J. Clin. Invest. 82:803-807(1988) [PubMed] [Europe PMC] [Abstract]. Cited for: PROTEIN SEQUENCE OF 25-56. "Identification of apolipoprotein A1 and immunoglobulin as components of a serum complex that mediates activation of human sperm motility."Aakerloef E., Joernvall H., Slotte H., Pousette A.Biochemistry 30:8986-8990(1991) [PubMed] [Europe PMC] [Abstract]. Cited for: PROTEIN SEQUENCE OF 25-50, FUNCTION, IDENTIFICATION IN THE SPAP COMPLEX. Tissue: Serum. "Apolipoprotein A-I binds to a family of bovine seminal plasma proteins."Manjunath P., Marcel Y.L., Uma J., Seidah N.G., Chretien M., Chapdelaine A.J. Biol. Chem. 264:16853-16857(1989) [PubMed] [Europe PMC] [Abstract]. Cited for: PROTEIN SEQUENCE OF 25-48. "Similarity of cruzin, an inhibitor of Trypanosoma cruzi neuraminidase, to high-density lipoprotein."Prioli R.P., Ordovas J.M., Rosenberg I., Schaeffer E.J., Pereira M.E.A.Science 238:1417-1419(1987) [PubMed] [Europe PMC] [Abstract]. Cited for: PROTEIN SEQUENCE OF 25-43. "The human myocardial two-dimensional gel protein database: update 1994."Corbett J.M., Wheeler C.H., Baker C.S., Yacoub M.H., Dunn M.J.Electrophoresis 15:1459-1465(1994) [PubMed] [Europe PMC] [Abstract]. Cited for: PROTEIN SEQUENCE OF 25-42. Tissue: Heart. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]. Cited for: PROTEIN SEQUENCE OF 25-34. Tissue: Platelet. "The apolipoprotein A-I binding protein of placenta and the SP-40,40 protein of human blood are different proteins which both bind to apolipoprotein A-I."Ehnholm C., Bozas S.E., Tenkanen H., Kirszbaum L., Metso J., Murphy B., Walker I.D.Biochim. Biophys. Acta 1086:255-260(1991) [PubMed] [Europe PMC] [Abstract]. Cited for: PROTEIN SEQUENCE OF 25-33, INTERACTION WITH APOA1BP AND CLU. Lubec G., Vishwanath V., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB. Cited for: PROTEIN SEQUENCE OF 35-64; 70-101; 121-140; 165-173; 185-195 AND 240-263, IDENTIFICATION BY MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex. "Isolation and characterization of cDNA clones for human apolipoprotein A-I."Breslow J.L., Ross D., McPherson J., Williams H.W., Kurnit D., Nussbaum A.L., Karathanasis S.K., Zannis V.I.Proc. Natl. Acad. Sci. U.S.A. 79:6861-6865(1982) [PubMed] [Europe PMC] [Abstract]. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 118-267. "Human apolipoprotein A-I. Post-translational modification by fatty acid acylation."Hoeg J.M., Meng M.S., Ronan R., Fairwell T., Brewer H.B. Jr.J. Biol. Chem. 261:3911-3914(1986) [PubMed] [Europe PMC] [Abstract]. Cited for: PALMITOYLATION. "Intracellular and extracellular processing of human apolipoprotein A-I: secreted apolipoprotein A-I isoprotein 2 is a propeptide."Zannis V.I., Karathanasis S.K., Keutmann H.T., Goldberger G., Breslow J.L.Proc. Natl. Acad. Sci. U.S.A. 80:2574-2578(1983) [PubMed] [Europe PMC] [Abstract]. Cited for: PROTEOLYTIC PROCESSING. "The preferential site of non-enzymatic glycation of human apolipoprotein A-I in vivo."Calvo C., Ulloa N., Campos M., Verdugo C., Ayrault-Jarrier M.Clin. Chim. Acta 217:193-198(1993) [PubMed] [Europe PMC] [Abstract]. Cited for: GLYCATION AT LYS-263. "Cloning and characterization of a novel apolipoprotein A-I-binding protein, AI-BP, secreted by cells of the kidney proximal tubules in response to HDL or ApoA-I."Ritter M., Buechler C., Boettcher A., Barlage S., Schmitz-Madry A., Orso E., Bared S.M., Schmiedeknecht G., Baehr C.H., Fricker G., Schmitz G.Genomics 79:693-702(2002) [PubMed] [Europe PMC] [Abstract]. Cited for: INTERACTION WITH APOA1BP. "Characterization of specifically oxidized apolipoproteins in mildly oxidized high density lipoprotein."Pankhurst G., Wang X.L., Wilcken D.E., Baernthaler G., Panzenboeck U., Raftery M., Stocker R.J. Lipid Res. 44:349-355(2003) [PubMed] [Europe PMC] [Abstract]. Cited for: MASS SPECTROMETRY, OXIDATION AT MET-110 AND MET-136, TISSUE SPECIFICITY. "Novel mass spectrometric immunoassays for the rapid structural characterization of plasma apolipoproteins."Niederkofler E.E., Tubbs K.A., Kiernan U.A., Nedelkov D., Nelson R.W.J. Lipid Res. 44:630-639(2003) [PubMed] [Europe PMC] [Abstract]. Cited for: IDENTIFICATION BY MASS SPECTROMETRY. "NDRG1 interacts with APO A-I and A-II and is a functional candidate for the HDL-C QTL on 8q24."Hunter M., Angelicheva D., Tournev I., Ingley E., Chan D.C., Watts G.F., Kremensky I., Kalaydjieva L.Biochem. Biophys. Res. Commun. 332:982-992(2005) [PubMed] [Europe PMC] [Abstract]. Cited for: INTERACTION WITH NDRG1.
4. "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) [PubMed] [Europe PMC] [Abstract]. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. "Conformation of human serum apolipoprotein A-I(166-185) in the presence of sodium dodecyl sulfate or dodecylphosphocholine by 1H-NMR and CD. Evidence for specific peptide-SDS interactions."Wang G., Treleaven W.D., Cushley R.J.Biochim. Biophys. Acta 1301:174-184(1996) [PubMed] [Europe PMC] [Abstract]. Cited for: STRUCTURE BY NMR OF 190-209. "Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation."Borhani D.W., Rogers D.P., Engler J.A., Brouillette C.G.Proc. Natl. Acad. Sci. U.S.A. 94:12291-12296(1997) [PubMed] [Europe PMC] [Abstract]. Cited for: X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 67-267. "Autosomal dominant hypoalphalipoproteinemia due to a completely defective apolipoprotein A-I gene."Nakata K., Kobayashi K., Yanagi H., Shimakura Y., Tsuchiya S., Arinami T., Hamaguchi H.Biochem. Biophys. Res. Commun. 196:950-955(1993) [PubMed] [Europe PMC] [Abstract]. Cited for: DISEASE. "Apolipoprotein A-I Q[-2]X causing isolated apolipoprotein A-I deficiency in a family with analphalipoproteinemia."Ng D.S., Leiter L.A., Vezina C., Connelly P.W., Hegele R.A.J. Clin. Invest. 93:223-229(1994) [PubMed] [Europe PMC] [Abstract]. Cited for: DISEASE. "Apolipoprotein A-IMilano. Detection of normal A-I in affected subjects and evidence for a cysteine for arginine substitution in the variant A-I."Weisgraber K.H., Rall S.C. Jr., Bersot T.P., Mahley R.W., Franceschini G., Sirtori C.R.J. Biol. Chem. 258:2508-2513(1983) [PubMed] [Europe PMC] [Abstract]. Cited for: VARIANT MILANO CYS-197. "Tangier disease: defective recombination of a specific Tangier apolipoprotein A-I isoform (pro-apo A-I) with high density lipoproteins."Schmitz G., Assmann G., Rall S.C. Jr., Mahley R.W.Proc. Natl. Acad. Sci. U.S.A. 80:6081-6085(1983) [PubMed] [Europe PMC] [Abstract]. Cited for: VARIANT TANGIER. "Apolipoprotein A-IGiessen (Pro143-->Arg). A mutant that is defective in activating lecithin:cholesterol acyltransferase."Utermann G., Haas J., Steinmetz A., Paetzold R., Rall S.C. Jr., Weisgraber K.H., Mahley R.W.Eur. J. Biochem. 144:325-331(1984) [PubMed] [Europe PMC] [Abstract]. Cited for: VARIANT GIESSEN ARG-167. "Abnormal lecithin:cholesterol acyltransferase activation by a human apolipoprotein A-I variant in which a single lysine residue is deleted."Rall S.C. Jr., Weisgraber K.H., Mahley R.W., Ogawa Y., Fielding C.J., Utermann G., Haas J., Steinmetz A., Menzel H.J., Assmann G.J. Biol. Chem. 259:10063-10070(1984) [PubMed] [Europe PMC] [Abstract]. Cited for: VARIANT NORWAY LYS-160. "Variant apolipoprotein AI as a major constituent of a human hereditary amyloid."Nichols W.C., Dwulet F.E., Liepnieks J., Benson M.D.Biochem. Biophys. Res. Commun. 156:762-768(1988) [PubMed] [Europe PMC] [Abstract]. Cited for: PROTEIN SEQUENCE OF 25-107, VARIANT AMYL8 ARG-50. "A mutation in apolipoprotein A-I in the Iowa type of familial amyloidotic polyneuropathy."Nichols W.C., Gregg R.E., Brewer H.B. Jr., Benson M.D.Genomics 8:318-323(1990) [PubMed] [Europe PMC] [Abstract]. Cited for: VARIANT AMYL8 ARG-50. "Isolation and characterization of human apolipoprotein A-I Fukuoka (110 Glu-->Lys). A novel apolipoprotein variant."Takada Y., Sasaki J., Ogata S., Nakanishi T., Ikehara Y., Arakawa K.Biochim. Biophys. Acta 1043:169-176(1990) [PubMed] [Europe PMC] [Abstract]. Cited for: PROTEIN SEQUENCE OF 25-267, VARIANT FUKUOKA LYS-134. "Apolipoprotein AI mutation Arg-60 causes autosomal dominant amyloidosis."Soutar A.K., Hawkins P.N., Vigushin D.M., Tennent G.A., Booth S.E., Hutton T., Nguyen O., Totty N.F., Feest T.G., Hsuan J.J., Pepys M.B.Proc. Natl. Acad. Sci. U.S.A. 89:7389-7393(1992) [PubMed] [Europe PMC] [Abstract]. Cited for: PROTEIN SEQUENCE OF 25-112, VARIANT AMYL8 ARG-84. "Apolipoprotein A1 Baltimore (Arg-10-->Leu), a new ApoA1 variant."Ladias J.A.A., Kwiterovich P.O. Jr., Smith H.H., Karathanasis S.K., Antonarakis S.E.Hum. Genet. 84:439-445(1990) [PubMed] [Europe PMC] [Abstract]. Cited for: VARIANT BALTIMORE LEU-34. "Apolipoprotein A-I variants. Naturally occurring substitutions of proline residues affect plasma concentration of apolipoprotein A-I."von Eckardstein A., Funke H., Henke A., Altland K., Benninghoven A., Assmann G., Welp S., Roetrige A., Kock R.J. Clin. Invest. 84:1722-1730(1989) [PubMed] [Europe PMC] [Abstract]. Cited for: VARIANTS ARG-27; ARG-28 AND ARG-189. "Structural analysis of human apolipoprotein A-I variants. Amino acid substitutions are nonrandomly distributed throughout the apolipoprotein A-I primary structure."von Eckardstein A., Funke H., Walter M., Altland K., Benninghoven A., Assmann G.J. Biol. Chem. 265:8610-8617(1990) [PubMed] [Europe PMC] [Abstract]. Cited for: VARIANTS GLU-113; MET-131; GLY-163; VAL-171 AND LYS-222. "Characterization of two new human apolipoprotein A-I variants: apolipoprotein A-I Tsushima (Trp-108-->Arg) and A-I Hita (Ala-95-->Asp)."Araki K., Sasaki J., Matsunaga A., Takada Y., Moriyama K., Hidaka K., Arakawa K.Biochim. Biophys. Acta 1214:272-278(1994) [PubMed] [Europe PMC] [Abstract]. Cited for: VARIANTS HITA AND TSUSHIMA. "Familial nephropathic systemic amyloidosis caused by apolipoprotein AI variant Arg26."Vigushin D.M., Gough J., Allan D., Alguacil A., Penner B., Pettigrew N.M., Quinonez G., Bernstein K., Booth S.E., Booth D.R., Soutar A.K., Hawkins P.N., Pepys M.B.Q. J. Med. 87:149-154(1994) [PubMed] [Europe PMC] [Abstract]. Cited for: VARIANT AMYL8 ARG-50. "A novel homozygous missense mutation in the apo A-I gene with apo A-I deficiency."Huang W., Sasaki J., Matsunaga A., Nanimatsu H., Moriyama K., Han H., Kugi M., Koga T., Yamaguchi K., Arakawa K.Arterioscler. Thromb. Vasc. Biol. 18:389-396(1998) [PubMed] [Europe PMC] [Abstract]. Cited for: VARIANT AOITA GLU-180. "Apo A-I Zaragoza(L144R): a novel mutation in the apolipoprotein A-I gene associated with familial hypoalphalipoproteinemia."Recalde D., Cenarro A., Civeira F., Pocovi M.Hum. Mutat. 11:416-416(1998). Cited for: VARIANT ZARAGOZA ARG-168. "Association of extreme blood lipid profile phenotypic variation with 11 reverse cholesterol transport genes and 10 non-genetic cardiovascular disease risk factors."Morabia A., Cayanis E., Costanza M.C., Ross B.M., Flaherty M.S., Alvin G.B., Das K., Gilliam T.C.Hum. Mol. Genet. 12:2733-2743(2003) [PubMed] [Europe PMC] [Abstract]. Cited for: VARIANT ILE-92. "Quantitative detection of single amino acid polymorphisms by targeted proteomics."Su Z.D., Sun L., Yu D.X., Li R.X., Li H.X., Yu Z.J., Sheng Q.H., Lin X., Zeng R., Wu J.R.J. Mol. Cell Biol. 3:309-315(2011) [PubMed] [Europe PMC] [Abstract]. Cited for: VARIANT ILE-92, IDENTIFICATION BY MASS SPECTROMETRY.
 Research Articles on APOA1    1. ApoA-I Milano (R173C) variants are no different in protein stability or solubility to wild type protein.
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Products associated with APOA1 proteinPathways associated with APOA1 protein
 Reference Product  PubMed Publications
 APOB protein  >482 publications with APOA1 and APOB
 ABCA1 protein  >130 publications with APOA1 and ABCA1
 APOC3 protein  >70 publications with APOA1 and APOC3
 CETP protein  >60 publications with APOA1 and CETP
 APOA2 protein  >40 publications with APOA1 and APOA2
 LCAT protein  >39 publications with APOA1 and LCAT
 ALB protein  >8 publications with APOA1 and ALB
 TTR protein  >7 publications with APOA1 and TTR
 FGA protein  >2 publications with APOA1 and FGA
 Products by Pathway  Pathway Diagram
 ABC-family Proteins Mediated Transport Pathway antibodies  ABC-family Proteins Mediated Transport Pathway Diagram
 ABCA Transporters In Lipid Homeostasis Pathway antibodies  ABCA Transporters In Lipid Homeostasis Pathway Diagram
 African Trypanosomiasis Pathway antibodies  African Trypanosomiasis Pathway Diagram
 African Trypanosomiasis Pathway antibodies  African Trypanosomiasis Pathway Diagram
 Amyloids Pathway antibodies  Amyloids Pathway Diagram
 Binding And Uptake Of Ligands By Scavenger Receptors Pathway antibodies  Binding And Uptake Of Ligands By Scavenger Receptors Pathway Diagram
 Chylomicron-mediated Lipid Transport Pathway antibodies  Chylomicron-mediated Lipid Transport Pathway Diagram
 Disease Pathway antibodies  Disease Pathway Diagram
 Diseases Associated With Visual Transduction Pathway antibodies  Diseases Associated With Visual Transduction Pathway Diagram
 FOXA2 And FOXA3 Transcription Factor Networks Pathway antibodies  FOXA2 And FOXA3 Transcription Factor Networks Pathway Diagram
Diseases associated with APOA1 proteinOrgans/Tissues associated with APOA1 protein
 Disease Name  Pubmed Publications
 Cardiovascular Diseases Antibodies  >442 publications with APOA1 and Cardiovascular Diseases
 Atherosclerosis Antibodies  >272 publications with APOA1 and Atherosclerosis
 Dyslipidemias Antibodies  >184 publications with APOA1 and Dyslipidemias
 Hyperlipidemias Antibodies  >125 publications with APOA1 and Hyperlipidemias
 Inflammation Antibodies  >107 publications with APOA1 and Inflammation
 Insulin Resistance Antibodies  >98 publications with APOA1 and Insulin Resistance
 Hypertension Antibodies  >77 publications with APOA1 and Hypertension
 Hypercholesterolemia Antibodies  >65 publications with APOA1 and Hypercholesterolemia
 Hypertriglyceridemia Antibodies  >58 publications with APOA1 and Hypertriglyceridemia
 Liver Diseases Antibodies  >52 publications with APOA1 and Liver Diseases
 Organ/Tissue Name  Pubmed Publications
 Blood Antibodies  >786 publications with APOA1 and Blood
 Liver Antibodies  >181 publications with APOA1 and Liver
 Heart Antibodies  >158 publications with APOA1 and Heart
 Muscle Antibodies  >34 publications with APOA1 and Muscle
 Brain Antibodies  >33 publications with APOA1 and Brain
 Lung Antibodies  >21 publications with APOA1 and Lung
 Ovary Antibodies  >15 publications with APOA1 and Ovary
 Intestine Antibodies  >15 publications with APOA1 and Intestine
 Pancreas Antibodies  >7 publications with APOA1 and Pancreas
 Embryonic Tissue Antibodies  >4 publications with APOA1 and Embryonic Tissue
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