GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, Gentaur another in time delivery

Apolipoprotein B-100 (Apo B-100) [Cleaved into: Apolipoprotein B-48 (Apo B-48)]

 APOB_RAT                Reviewed;        4743 AA.
Q7TMA5;
10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
01-OCT-2003, sequence version 1.
16-JAN-2019, entry version 119.
RecName: Full=Apolipoprotein B-100;
Short=Apo B-100;
Contains:
RecName: Full=Apolipoprotein B-48;
Short=Apo B-48;
Flags: Precursor;
Name=Apob; ORFNames=Aa1064, Ac1-060;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
Xu C.S., Li W.Q., Li Y.C., Wang G.P., Chai L.Q., Yuan J.Y., Yang K.J.,
Yan H.M., Chang C.F., Zhao L.F., Ma H., Wang L., Wang S.F., Han H.P.,
Shi J.B., Rahman S., Wang Q.N., Zhang J.B.;
"Liver regeneration after PH.";
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[2]
FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=632283;
Wu A.L., Windmueller H.G.;
"Identification of circulating apolipoproteins synthesized by rat
small intestine in vivo.";
J. Biol. Chem. 253:2525-2528(1978).
[3]
CHARACTERIZATION.
PubMed=6948299; DOI=10.1073/pnas.79.1.179;
Van't Hooft F.M., Hardman D.A., Kane J.P., Havel R.J.;
"Apolipoprotein B (B-48) of rat chylomicrons is not a precursor of the
apolipoprotein of low density lipoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 79:179-182(1982).
[4]
RNA EDITING.
PubMed=2911593; DOI=10.1073/pnas.86.2.500;
Tennyson G.E., Sabatos C.A., Higuchi K., Meglin N., Brewer H.B. Jr.;
"Expression of apolipoprotein B mRNAs encoding higher- and lower-
molecular weight isoproteins in rat liver and intestine.";
Proc. Natl. Acad. Sci. U.S.A. 86:500-504(1989).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2006, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Apolipoprotein B is a major protein constituent of
chylomicrons (apo B-48), LDL (apo B-100) and VLDL (apo B-100). Apo
B-100 functions as a recognition signal for the cellular binding
and internalization of LDL particles by the apoB/E receptor.
{ECO:0000269|PubMed:632283}.
-!- SUBUNIT: Interacts with PCSK9. Interacts with MTTP.
{ECO:0000250|UniProtKB:P04114}.
-!- INTERACTION:
P04639:Apoa1; NbExp=2; IntAct=EBI-15185298, EBI-2925493;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04114}.
Secreted {ECO:0000269|PubMed:632283}.
-!- TISSUE SPECIFICITY: Detected in intestine and liver (at protein
level). {ECO:0000269|PubMed:632283}.
-!- PTM: Palmitoylated; structural requirement for proper assembly of
the hydrophobic core of the lipoprotein particle. {ECO:0000250}.
-!- RNA EDITING: Modified_positions=2147 {ECO:0000269|PubMed:2911593};
Note=The stop codon (UAA) at position 2147 is created by RNA
editing. Apo B-48, derived from the fully edited RNA, is produced
only in the intestine and is found in chylomicrons. Apo B-48 is a
shortened form of apo B-100 which lacks the LDL-receptor region.
The unedited version (apo B-100) is produced by the liver and is
found in the VLDL and LDL.;
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AY318958; AAP85369.1; -; mRNA.
EMBL; AY321317; AAP86249.1; -; mRNA.
RefSeq; NP_062160.2; NM_019287.2.
UniGene; Rn.33815; -.
ProteinModelPortal; Q7TMA5; -.
SMR; Q7TMA5; -.
BioGrid; 248449; 1.
DIP; DIP-29910N; -.
IntAct; Q7TMA5; 1.
STRING; 10116.ENSRNOP00000039779; -.
CarbonylDB; Q7TMA5; -.
iPTMnet; Q7TMA5; -.
PhosphoSitePlus; Q7TMA5; -.
jPOST; Q7TMA5; -.
PaxDb; Q7TMA5; -.
PRIDE; Q7TMA5; -.
Ensembl; ENSRNOT00000046811; ENSRNOP00000039779; ENSRNOG00000005542.
GeneID; 54225; -.
KEGG; rno:54225; -.
CTD; 338; -.
RGD; 2129; Apob.
eggNOG; KOG0654; Eukaryota.
eggNOG; KOG4338; Eukaryota.
eggNOG; ENOG411104F; LUCA.
GeneTree; ENSGT00590000083139; -.
HOGENOM; HOG000034000; -.
HOVERGEN; HBG050546; -.
InParanoid; Q7TMA5; -.
KO; K14462; -.
OMA; WPVPEVY; -.
OrthoDB; 5350at2759; -.
PhylomeDB; Q7TMA5; -.
TreeFam; TF331316; -.
Reactome; R-RNO-202733; Cell surface interactions at the vascular wall.
Reactome; R-RNO-3000471; Scavenging by Class B Receptors.
Reactome; R-RNO-3000480; Scavenging by Class A Receptors.
Reactome; R-RNO-3000497; Scavenging by Class H Receptors.
Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-RNO-432142; Platelet sensitization by LDL.
Reactome; R-RNO-5686938; Regulation of TLR by endogenous ligand.
Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
Reactome; R-RNO-8866423; VLDL assembly.
Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
Reactome; R-RNO-8963888; Chylomicron assembly.
Reactome; R-RNO-8963901; Chylomicron remodeling.
Reactome; R-RNO-8964026; Chylomicron clearance.
Reactome; R-RNO-8964038; LDL clearance.
Reactome; R-RNO-8964046; VLDL clearance.
Reactome; R-RNO-975634; Retinoid metabolism and transport.
PRO; PR:Q7TMA5; -.
Proteomes; UP000002494; Chromosome 6.
Bgee; ENSRNOG00000005542; Expressed in 4 organ(s), highest expression level in liver.
ExpressionAtlas; Q7TMA5; baseline and differential.
Genevisible; Q7TMA5; RN.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0070971; C:endoplasmic reticulum exit site; IEA:Ensembl.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0034364; C:high-density lipoprotein particle; IDA:RGD.
GO; GO:0034363; C:intermediate-density lipoprotein particle; IEA:Ensembl.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
GO; GO:0034362; C:low-density lipoprotein particle; IDA:RGD.
GO; GO:0034359; C:mature chylomicron; IEA:Ensembl.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0034361; C:very-low-density lipoprotein particle; IDA:RGD.
GO; GO:0031983; C:vesicle lumen; IDA:RGD.
GO; GO:0012506; C:vesicle membrane; IDA:RGD.
GO; GO:0017127; F:cholesterol transporter activity; IEA:Ensembl.
GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
GO; GO:0035473; F:lipase binding; IEA:Ensembl.
GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IEA:Ensembl.
GO; GO:0005543; F:phospholipid binding; IEA:Ensembl.
GO; GO:0048844; P:artery morphogenesis; IEA:Ensembl.
GO; GO:0071379; P:cellular response to prostaglandin stimulus; IEP:RGD.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
GO; GO:0033344; P:cholesterol efflux; IEA:Ensembl.
GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl.
GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
GO; GO:0009566; P:fertilization; IEA:Ensembl.
GO; GO:0030317; P:flagellated sperm motility; IEA:Ensembl.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0006629; P:lipid metabolic process; IDA:RGD.
GO; GO:0042158; P:lipoprotein biosynthetic process; IEA:Ensembl.
GO; GO:0042159; P:lipoprotein catabolic process; IEA:Ensembl.
GO; GO:0042953; P:lipoprotein transport; IEA:Ensembl.
GO; GO:0034383; P:low-density lipoprotein particle clearance; IEA:Ensembl.
GO; GO:0034374; P:low-density lipoprotein particle remodeling; IEA:Ensembl.
GO; GO:0007399; P:nervous system development; IEA:Ensembl.
GO; GO:0010886; P:positive regulation of cholesterol storage; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; IEA:Ensembl.
GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
GO; GO:0045540; P:regulation of cholesterol biosynthetic process; IEA:Ensembl.
GO; GO:0009743; P:response to carbohydrate; IDA:RGD.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
GO; GO:0010033; P:response to organic substance; IEP:RGD.
GO; GO:0010269; P:response to selenium ion; IEP:RGD.
GO; GO:0009615; P:response to virus; IEA:Ensembl.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
GO; GO:0019433; P:triglyceride catabolic process; IMP:RGD.
GO; GO:0006642; P:triglyceride mobilization; IEA:Ensembl.
CDD; cd00043; CYCLIN; 1.
Gene3D; 1.25.10.20; -; 1.
Gene3D; 2.30.230.10; -; 1.
InterPro; IPR022176; ApoB100_C.
InterPro; IPR013763; Cyclin-like.
InterPro; IPR036915; Cyclin-like_sf.
InterPro; IPR006671; Cyclin_N.
InterPro; IPR015819; Lipid_transp_b-sht_shell.
InterPro; IPR001747; Lipid_transpt_N.
InterPro; IPR009454; Lipid_transpt_open_b-sht.
InterPro; IPR011030; Lipovitellin_superhlx_dom.
InterPro; IPR015816; Vitellinogen_b-sht_N.
InterPro; IPR015255; Vitellinogen_open_b-sht.
Pfam; PF12491; ApoB100_C; 1.
Pfam; PF00134; Cyclin_N; 1.
Pfam; PF06448; DUF1081; 1.
Pfam; PF09172; DUF1943; 1.
Pfam; PF01347; Vitellogenin_N; 1.
SMART; SM00385; CYCLIN; 1.
SMART; SM01169; DUF1943; 1.
SMART; SM00638; LPD_N; 1.
SUPFAM; SSF47954; SSF47954; 2.
SUPFAM; SSF48431; SSF48431; 1.
SUPFAM; SSF56968; SSF56968; 2.
PROSITE; PS51211; VITELLOGENIN; 1.
1: Evidence at protein level;
Acetylation; Atherosclerosis; Cholesterol metabolism; Chylomicron;
Complete proteome; Cytoplasm; Disulfide bond; Glycoprotein;
Heparin-binding; LDL; Lipid metabolism; Lipid transport; Lipoprotein;
Palmitate; Phosphoprotein; Reference proteome; RNA editing; Secreted;
Signal; Steroid metabolism; Sterol metabolism; Transport; VLDL.
SIGNAL 1 27 {ECO:0000250}.
CHAIN 28 4743 Apolipoprotein B-100.
/FTId=PRO_0000293536.
CHAIN 28 2146 Apolipoprotein B-48.
/FTId=PRO_0000293537.
DOMAIN 33 660 Vitellogenin. {ECO:0000255|PROSITE-
ProRule:PRU00557}.
REGION 29 113 Heparin-binding. {ECO:0000250}.
REGION 219 293 Heparin-binding. {ECO:0000250}.
REGION 890 947 Heparin-binding. {ECO:0000250}.
REGION 2010 2145 Heparin-binding. {ECO:0000250}.
REGION 3123 3198 Heparin-binding. {ECO:0000250}.
REGION 3136 3146 Basic (possible receptor binding region).
{ECO:0000250}.
REGION 3336 3356 LDL receptor binding. {ECO:0000250}.
REGION 3346 3479 Heparin-binding. {ECO:0000250}.
REGION 3349 3357 Basic (possible receptor binding region).
{ECO:0000250}.
MOD_RES 1973 1973 N6-acetyllysine.
{ECO:0000250|UniProtKB:P04114}.
MOD_RES 2006 2006 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 3981 3981 Phosphoserine.
{ECO:0000250|UniProtKB:P04114}.
MOD_RES 3985 3985 Phosphothreonine.
{ECO:0000250|UniProtKB:P04114}.
CARBOHYD 172 172 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 971 971 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1336 1336 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1345 1345 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1491 1491 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2094 2094 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2522 2522 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2662 2662 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2741 2741 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2791 2791 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2897 2897 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2944 2944 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3063 3063 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3186 3186 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3299 3299 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3321 3321 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3428 3428 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3715 3715 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3828 3828 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 4203 4203 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 4232 4232 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 65 84 {ECO:0000255|PROSITE-ProRule:PRU00557}.
DISULFID 173 199 {ECO:0000255|PROSITE-ProRule:PRU00557}.
DISULFID 232 248 {ECO:0000255|PROSITE-ProRule:PRU00557}.
DISULFID 372 377 {ECO:0000255|PROSITE-ProRule:PRU00557}.
DISULFID 466 501 {ECO:0000255|PROSITE-ProRule:PRU00557}.
DISULFID 954 964 {ECO:0000255|PROSITE-ProRule:PRU00557}.
SEQUENCE 4743 AA; 536024 MW; B01AD103F8EC5320 CRC64;
MGPQRPALRA PLLLLFLLLF LDTSVWAQDA TRFKHLRKYV YSYEAESSSG VRGTADSRSA
TKINCKVELE VPQVCTLIMR TSQCTLKEVY GFNPEGKALM KKTKNSEEFA SAMSRYELKL
AFPEGKRVAL YPDLGEPNYI LNIKRGIISA LLVPPETEED KQVLFQDTVY GNCSTQVTVN
SRKGTVATEM STERNLQHCD GFQPISTSVS PLALIKGLVR PLSTLISSSQ SCQYTLEPKR
KHVSEAICNE QHLFLPFSYK NKYGIMTHVT QKLSLEDTPK INSRFFRGGI NQVGLAFEST
KSTSPPKQAD AVLKTLQELK KLSISEQNAQ RANLFHKLVT ELRGLSGEAI TSLLPQLIEV
SSPITLQALI QCGQPECYTH ILQWLKTEKA HPLLIDIVTY LMALIPNPSV QRLQEIFNTA
KELQSRATLY ALSHAVNSYY AIMDHSRSPV LEDIAGYLMK QIDNECMGDE DRTFLILRVI
GNMGRTMERV MPALKSSVLN CVRSTKPSLQ IQKAALQALR KMEMGDEVRT ILFDTFVNDV
APVEKRLAAY LLLMRSPSSS DINKIAKLLQ WEQSEQVKNF VASHIANILN SEELYVQDLK
NLIKNALVNS RLPTIMDFRK FSRNYQISKS VSIPLFDPVS AKIEGNLVFD PSSYLPKESM
LKTTLTVFGI ASLDLFEIGL EGKGFEPTLE ALFGKQGFFP DSVNKALYWV NGQVPDRVSK
VLVDHFGYTK DDKHEQDMVN GIMPIVDKLI KELKSKEIPE ARAYLRILGK ELGFVRLQDL
QVLGKLLLNG AQTFRGVPQM IVQAIREGSK DDLFLHYIFM ENAFELPTGV GLQLQVSSSG
VFTPGIKAGV RLELANIQAE LVAKPSVSLE FVTNMGIIIP DFAKSGVQMN TNFFHESGLE
ARVALKAGQL KVIIPSPKRP VKLFSGSNTL HLVSTTKTEV IPPLIENRKS WSTCKPFFTG
MNYCTTGAYS NASSTESASY YPLTGDTRYE LELKPTGEVE QYSASATYEL LKEDKSLVDT
LKFLVQAEGV QQSEATAMFK YNRRSRTLSS EVLIPGFDVN FGTILRVNDE SSKDKNTYKL
ILDIQNKKIT EVSVVGHVSY DKKGDGKVKG VVSIPRLQAE ARSEVHTHWS PTKLLFQMDS
SATAYGSTIS KRVAWRYDNE KIEFDWNTGT NVDTKKVASN FPVDLSRYPR MVHEYANGLL
DHRVPQTDMT FRHMGSKLIV DHLNGLSELN LPKVGLPDFH IPDNLFLKTD GRVKYTLNKN
RIEIDIPLPL GGKSSKDLKV PESVRTPALN FKSVGFHLPS QEVQIPTFTI PKTHQLQVPL
LGILDLSTNV YSNLYNWSVS YTGGNTSRDH FSLQAQYRMK ADSVVDLFSY SVQGSGETTY
DSKSTFTLSC DGSLHHKFLD SKFKVSHVEK FGNNPVSKGL LTFETSSALG PQMSATVQLD
SKKKQHLYVK DIKVDGQFRV FSLYAQGEYG LSYERDSMTG QMSGESNMKF NSTYFQGTNQ
IVGMYQDGML SVTSTSDLQD GIFKNTASLK YENYELTLKS DSSGQYENFA ASNKLDMTFS
KQSALLRSEH QANYKSLRLV TLLSGSLTSQ GVELNADILG TDKINTGAHK STLKIAQDGV
STSATTNLKY SPLLLENELN AELGLSGASM KLSTSGRFKE HHAKFSLDGR AALTEVSLGS
IYQAMILGAD SKNVFNFKLS REGLKLSNDM MGSYAEMKLD HTHSLRISGL SLDFFSKMDN
IYSGDKFYKQ NFNLQLQPYS FGITLSNDLK YDALVLTNNG RLRLEPLKLN VGGNFKGTYQ
NNELKHIYTI SYTDLVVASY RADTVATVQG VEFSHRLNAD IEGLASSVDV TTSYSSDPLH
FNNVFRFVLA PFTLGVDTHT SGDGKMSLWG EHTGQMYSKF LLKAEPLALT FSHDYKGSTS
HNLLYKNSVS TALEHTLSAL LTPAEQTSSW KFKTSLNDKV YSQEFEAYNT KDKIGIELSG
RADLSGLYSP IKVPFFYSEP VNVLNSLEIN DAFDEPREFT IDAVVKYDKN QDVHTISLPF
FQSLPDYLER NRRGIISLLE AMKGELQRLS VDQFVRKYRV ALSRLPQQIH DYLNASDWER
QVAGAKEKLT SFMENYRITD NDVLIALDSA KINLNEKLSQ LETYAIQFDQ YIRDNYDAQD
LKRTIAQIID RIIEKLKMLD EQYHIRVNLA KSIHNLYLFV ENVDLNQISS SGASWIQNVD
TKYQIRIQIQ EKLQHLRTQI HNIDIQQLAA ELKQQIEALD VPMHLDQLRT AILFQRISVI
IERVKYFVMN LIEDFKVTEK INTFRVIVRE LIEKYEVDRQ IQVLMDKSIE LAHRYSLSEP
LQKLSNVLQQ IEIKDYYDKL VGFIDDTVEW IKAVSFKNII EELNRLIDMS VKKLKAFDYH
QFVDKTNSKI REMTQRINAE IQALELPQKT EALKLWVEDF KTTVSNSLEK LKDTKVTVVV
DWLQDGLAQI KAQFQDALED VRDRIYQMDI QGELERCLSL VSQVYSTVVT YISDWWTLTA
KNITDFAEQY STQKWAESVK ALVEQGFIVP EIQTFLGTMP AFEVSLHALQ EANFQTPDFI
VPLTDLRIPS IWINFKMLKN VKIPLRFSTP EFTLLNTFRV RSFTIDLLEI KAKIIRTIDQ
MLSSELQWPL PEVYLRDLEM VNISLARLSL PDFHVPEITI PEFTIPNVNL KDLQVPDLHI
PEFQLPHLSC TTEIPAFGKL HSVLKIQSPL FILDASANIQ NITTSENKAE IVASVTARGE
SKFEALNFDF QAQAQFLELN ANPLVLKESV NFSSKHVRME HEGKILVSGK ALEGKSDTVA
RLHTEKNTVE FNNGIVVKIN NQFTLDSQTK YFHKLSVPRL DFSSKASLNN EIKTLLEAGH
MAWTSSGTGS WNWACPNFSD EGIHSSKISF IVDGPIASFG LSNNINGKHL RVVQKLTSES
GFLNYSRFEV ESKVESQHVG SSILTAEGRA LLGDAKAEMT GEHNANLNGK VIGTLKNSLF
FSAQPFEITA STNNEGNLKV SFPLKLTGKI DFLNNYALFL SPHAQQASWQ LSTRFNQYKY
NQNFSAINNE HNMEASIVMN GDANLDFLNI PLTIPEINLP YTRFTTPLLK DFSIWEETGL
KEFLKTTKQS FDLSIKAQYK KNRDKHSVVI PLKMFYEFML NNVNSWDRKF EKVRDNALHF
LTASYNETKI KFDKYKTENS LNQPSRTFQN RGHTIPVLNI EVSPFAVETL ASSHVIPKAI
RTPSVTIPGP NIIVPSYRLV LPSLQLPVFH IPRTLFKFSL PDFKKLSTID NIYIPAMGNF
TYDFSFKSSV ITLNTNAGLY NQSDLVARFL SSSSFVTDAL QYKLEGTSRL MRKKVLKLAT
AVSLTNKFLK GSHDSTISLT KKNMEASVKT TANLHAPIFT MNFKQELNGN TKSKPTVSSS
IELNYDFNSS KLHSAAKGGV DHKFSLESLT SYLSIESFTK GNIKGSFLSQ EYSGSVANEA
NVYLNSKGTR SSVRLQGASN FAGIWNFEVG ENFAGEATLR RIYGTWEHNM INHLQVFSYF
DTKGKQTCRA TLELSPWTMS TLLQVHVSQP SPLFDLHHFD QEVILKASTK NQKVSWKSEV
QVESQVLQHN AHFSNDQEEV RLDIAGSLEG QLWDLENFFL PAFGKSLREL LQIDGKRQYL
QASTSLHYTK NPNGYLLSLP VQELTDRFII PGLKLNDFSG IKIYKKLSTS PFALNLTMLP
KVKFPGVDLL TQYSKPEGSS VPTFETTIPE IQLTVSQFTL PKSFPVGNTV FDLNKLTNLI
ADVDLPSITL PEQTIEIPSL EFSVPAGIFI PFFGELTAHV GMASPLYNVT WSTGWKNKAD
HVETFLDSTC SSTLQFLEYA LKVVGTHRIE NDKFIYKIKG TLQHCDFNVK YNEDGIFEGL
WDLEGEAHLD ITSPALTDFH LHYKEDKTSV SASAASPAIG TVSLDASTDD QSVRLNVYFR
PQSPPDNKLS IFKMEWRDKE SDGETYIKIN WEEEAAFRLL DSLKSNVPKA SEAVYDYVKK
YHLGHASSEL RKSLQNDAEH AIRMVDEMNV NAQRVTRDTY QSLYKKMLAQ ESQSIPEKLK
KMVLGSLVRI TQKYHMAVTW LMDSVIHFLK FNRVQFPGNA GTYTVDELYT IAMRETKKLL
SQLFNGLGHL FSYVQDQVEK SRVINDITFK CPFSPTPCKL KDVLLIFRED LNILSNLGQQ
DINFTTILSD FQSFLERLLD IIEEKIECLK NNESTCVPDH INMFFKTHIP FAFKSLRENI
YSVFSEFNDF VQSILQEGSY KLQQVHQYMK AFREEYFDPS VVGWTVKYYE IEEKMVDLIK
TLLAPLRDFY SEYSVTAADF ASKMSTQVEQ FVSRDIREYL SMLADINGKG REKVAELSIV
VKERIKSWST AVAEITSDYL RQLHSKLQDF SDQLSGYYEK FVAESTRLID LSIQNYHMFL
RYIAELLKKL QVATANNGLL KRGDFEAAVK LGIACLYNEG LSVSDEAYAE VNGLKASRFF
SMDERLNMGS DPFIWLSICP PCFRKLRDFA GKGCWEAQPA LAKDCAGGSQ LGLEGKAFSE
SVCQLFQASQ AVNKQQIFSV QKGLSDTVRY ILIGWLVEVA PMKDFTSLCL HLTVECVGRY
LQRKLVPRYK LQLLGIACMV ICTWFISKEI LTIREAVRLT DNTYKYKDLV RVKREIISAL
EGKIRIPTVV DYKEVLLTLV PVTPRTQYLC SFLCELTLSV YTPAHLASAA LLLARLMHGQ
TQP


Related products :

Catalog number Product name Quantity
20-272-192023 Apolipoprotein J - Mouse monoclonal [Hs - 3] to Apolipoprotein J; Complement-associated protein SP-40.40; Complement cytolysis inhibitor; CLI; NA1_NA2; Apolipoprotein J; Apo-J; Testosterone-repressed 0.05 mg
U1890m CLIA kit Apoc3,Apo-CIII,ApoC-III,Apolipoprotein C3,Apolipoprotein C-III,Mouse,Mus musculus 96T
E0604Rb ELISA APOA1,Apo-AI,ApoA-I,Apolipoprotein A1,Apolipoprotein A-I,Oryctolagus cuniculus,Rabbit 96T
U0604Rb CLIA APOA1,Apo-AI,ApoA-I,Apolipoprotein A1,Apolipoprotein A-I,Oryctolagus cuniculus,Rabbit 96T
E0604Rb ELISA kit APOA1,Apo-AI,ApoA-I,Apolipoprotein A1,Apolipoprotein A-I,Oryctolagus cuniculus,Rabbit 96T
E0252m ELISA Apoc1,Apoc1b,Apo-CIB,ApoC-IB,Apolipoprotein C1,Apolipoprotein C-I,Mouse,Mus musculus 96T
U1890b CLIA APOC3,Apo-CIII,ApoC-III,Apolipoprotein C3,Apolipoprotein C-III,Bos taurus,Bovine 96T
E1890b ELISA kit APOC3,Apo-CIII,ApoC-III,Apolipoprotein C3,Apolipoprotein C-III,Bos taurus,Bovine 96T
U1890m CLIA Apoc3,Apo-CIII,ApoC-III,Apolipoprotein C3,Apolipoprotein C-III,Mouse,Mus musculus 96T
U1890r CLIA Apoc3,Apo-CIII,ApoC-III,Apolipoprotein C3,Apolipoprotein C-III,Rat,Rattus norvegicus 96T
E1890r ELISA kit Apoc3,Apo-CIII,ApoC-III,Apolipoprotein C3,Apolipoprotein C-III,Rat,Rattus norvegicus 96T
U0604h CLIA APOA1,Apo-AI,ApoA-I,Apolipoprotein A1,Apolipoprotein A-I,Homo sapiens,Human 96T
E1890m ELISA kit Apoc3,Apo-CIII,ApoC-III,Apolipoprotein C3,Apolipoprotein C-III,Mouse,Mus musculus 96T
Y051160 Anti-human Apolipoprotein Apolipoprotein-H (β2-Glycoprotein-I )Peroxidase Conjugated IgG Antibody 100μg
E0604h ELISA APOA1,Apo-AI,ApoA-I,Apolipoprotein A1,Apolipoprotein A-I,Homo sapiens,Human 96T
U1890b CLIA kit APOC3,Apo-CIII,ApoC-III,Apolipoprotein C3,Apolipoprotein C-III,Bos taurus,Bovine 96T
E0252m ELISA kit Apoc1,Apoc1b,Apo-CIB,ApoC-IB,Apolipoprotein C1,Apolipoprotein C-I,Mouse,Mus musculus 96T
E1890r ELISA Apoc3,Apo-CIII,ApoC-III,Apolipoprotein C3,Apolipoprotein C-III,Rat,Rattus norvegicus 96T
E0604h ELISA kit APOA1,Apo-AI,ApoA-I,Apolipoprotein A1,Apolipoprotein A-I,Homo sapiens,Human 96T
Y051160 Anti-human Apolipoprotein Apolipoprotein-H β2-Glycoprotein-I Peroxidase Conjugated IgG antibody 250ug
E1890m ELISA Apoc3,Apo-CIII,ApoC-III,Apolipoprotein C3,Apolipoprotein C-III,Mouse,Mus musculus 96T
U1890r CLIA kit Apoc3,Apo-CIII,ApoC-III,Apolipoprotein C3,Apolipoprotein C-III,Rat,Rattus norvegicus 96T
U0252m CLIA Apoc1,Apoc1b,Apo-CIB,ApoC-IB,Apolipoprotein C1,Apolipoprotein C-I,Mouse,Mus musculus 96T
E1890b ELISA APOC3,Apo-CIII,ApoC-III,Apolipoprotein C3,Apolipoprotein C-III,Bos taurus,Bovine 96T
E0604m ELISA kit Apoa1,Apo-AI,ApoA-I,Apolipoprotein A1,Apolipoprotein A-I,Mouse,Mus musculus 96T

Kits Elisa; taq POLYMERASE

Search in Google:

google

Share this page:
share on twitter rss feedsfacebookgoogle gentaur



Quick order!
Enter catalog number :


Gentaur; yes we can

Pathways :
No related Items

Related Genes :
[APOBR APOB48R] Apolipoprotein B receptor (Apolipoprotein B-100 receptor) (Apolipoprotein B-48 receptor) (Apolipoprotein B48 receptor) (apoB-48R)
[Or22b AN12 DOR22A.2 dor67 Or22A.2 CG4231] Odorant receptor 22b
[APOA1] Apolipoprotein A-I (Apo-AI) (ApoA-I) (Apolipoprotein A1) [Cleaved into: Proapolipoprotein A-I (ProapoA-I); Truncated apolipoprotein A-I (Apolipoprotein A-I(1-242))]
[APOC1] Apolipoprotein C-I (Apo-CI) (ApoC-I) (Apolipoprotein C1) [Cleaved into: Truncated apolipoprotein C-I]
[APOA2] Apolipoprotein A-II (Apo-AII) (ApoA-II) (Apolipoprotein A2) [Cleaved into: Proapolipoprotein A-II (ProapoA-II); Truncated apolipoprotein A-II (Apolipoprotein A-II(1-76))]
[Pre C,C C core E PC pre-C pre-C/C PreC preC PreC/C preC/C precore-core HBVgp4] Capsid protein (Core antigen) (Core protein) (HBcAg) (p21.5)
[APOE] Apolipoprotein E (Apo-E)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)] (Fragment)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[APOC3] Apolipoprotein C-III (Apo-CIII) (ApoC-III) (Apolipoprotein C3)
[LPA] Apolipoprotein(a) (Apo(a)) (Lp(a)) (EC 3.4.21.-)
[CLU APOJ CLI KUB1 AAG4] Clusterin (Aging-associated gene 4 protein) (Apolipoprotein J) (Apo-J) (Complement cytolysis inhibitor) (CLI) (Complement-associated protein SP-40,40) (Ku70-binding protein 1) (NA1/NA2) (Testosterone-repressed prostate message 2) (TRPM-2) [Cleaved into: Clusterin beta chain (ApoJalpha) (Complement cytolysis inhibitor a chain); Clusterin alpha chain (ApoJbeta) (Complement cytolysis inhibitor b chain)]
[APOA5 RAP3 UNQ411/PRO773] Apolipoprotein A-V (Apo-AV) (ApoA-V) (Apolipoprotein A5) (Regeneration-associated protein 3)
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[Apoc3] Apolipoprotein C-III (Apo-CIII) (ApoC-III) (Apolipoprotein C3)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[botB] Botulinum neurotoxin type B (BoNT/B) (Bontoxilysin-B) [Cleaved into: Botulinum neurotoxin B light chain (LC) (EC 3.4.24.69); Botulinum neurotoxin B heavy chain (HC)]
[Apoc3] Apolipoprotein C-III (Apo-CIII) (ApoC-III) (Apolipoprotein C3)
[S100b] Protein S100-B (S-100 protein beta chain) (S-100 protein subunit beta) (S100 calcium-binding protein B)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]

Bibliography :
[6501314] Low-density lipoprotein receptor binding determinants switch from apolipoprotein E to apolipoprotein B during conversion of hypertriglyceridemic very-low-density lipoprotein to low-density lipoproteins.