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Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1 (GPI-HBP1) (GPI-anchored HDL-binding protein 1) (High density lipoprotein-binding protein 1)

 HDBP1_HUMAN             Reviewed;         184 AA.
Q8IV16; Q6P3T2; Q86W15;
05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
07-DEC-2004, sequence version 2.
27-SEP-2017, entry version 120.
RecName: Full=Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1;
Short=GPI-HBP1;
Short=GPI-anchored HDL-binding protein 1;
AltName: Full=High density lipoprotein-binding protein 1;
Flags: Precursor;
Name=GPIHBP1; Synonyms=HBP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Shan Y.X., Yu L.;
"Isolation and characterization of human HBP1 gene.";
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PHE-14.
TISSUE=Brain, and PNS;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
INTERACTION WITH APOA5 AND LPL, AND CHARACTERIZATION OF VARIANT
ARG-56.
PubMed=17997385; DOI=10.1016/j.bbalip.2007.10.005;
Gin P., Beigneux A.P., Davies B., Young M.F., Ryan R.O., Bensadoun A.,
Fong L.G., Young S.G.;
"Normal binding of lipoprotein lipase, chylomicrons, and apo-AV to
GPIHBP1 containing a G56R amino acid substitution.";
Biochim. Biophys. Acta 1771:1464-1468(2007).
[5]
REVIEW.
PubMed=21844202; DOI=10.1194/jlr.R018689;
Young S.G., Davies B.S., Voss C.V., Gin P., Weinstein M.M.,
Tontonoz P., Reue K., Bensadoun A., Fong L.G., Beigneux A.P.;
"GPIHBP1, an endothelial cell transporter for lipoprotein lipase.";
J. Lipid Res. 52:1869-1884(2011).
[6]
VARIANT ARG-56.
PubMed=17883852; DOI=10.1186/1476-511X-6-23;
Wang J., Hegele R.A.;
"Homozygous missense mutation (G56R) in glycosylphosphatidylinositol-
anchored high-density lipoprotein-binding protein 1 (GPI-HBP1) in two
siblings with fasting chylomicronemia (MIM 144650).";
Lipids Health Dis. 6:23-23(2007).
[7]
VARIANT HLPP1D PRO-115, AND CHARACTERIZATION OF VARIANT HLPP1D
PRO-115.
PubMed=19304573; DOI=10.1161/ATVBAHA.109.186577;
Beigneux A.P., Franssen R., Bensadoun A., Gin P., Melford K.,
Peter J., Walzem R.L., Weinstein M.M., Davies B.S.J.,
Kuivenhoven J.A., Kastelein J.J.P., Fong L.G., Dallinga-Thie G.M.,
Young S.G.;
"Chylomicronemia with a mutant GPIHBP1 (Q115P) that cannot bind
lipoprotein lipase.";
Arterioscler. Thromb. Vasc. Biol. 29:956-962(2009).
[8]
VARIANTS HLPP1D SER-65 AND GLY-68, AND CHARACTERIZATION OF VARIANTS
HLPP1D SER-65 AND GLY-68.
PubMed=20026666; DOI=10.1194/jlr.M002717;
Olivecrona G., Ehrenborg E., Semb H., Makoveichuk E., Lindberg A.,
Hayden M.R., Gin P., Davies B.S., Weinstein M.M., Fong L.G.,
Beigneux A.P., Young S.G., Olivecrona T., Hernell O.;
"Mutation of conserved cysteines in the Ly6 domain of GPIHBP1 in
familial chylomicronemia.";
J. Lipid Res. 51:1535-1545(2010).
[9]
VARIANTS HLPP1D PHE-89 AND ARG-175, VARIANT PHE-14, CHARACTERIZATION
OF VARIANTS HLPP1D PHE-89 AND ARG-175, AND CHARACTERIZATION OF VARIANT
PHE-14.
PubMed=21816778; DOI=10.1210/jc.2011-1444;
Charriere S., Peretti N., Bernard S., Di Filippo M., Sassolas A.,
Merlin M., Delay M., Debard C., Lefai E., Lachaux A., Moulin P.,
Marcais C.;
"GPIHBP1 C89F neomutation and hydrophobic C-terminal domain G175R
mutation in two pedigrees with severe hyperchylomicronemia.";
J. Clin. Endocrinol. Metab. 96:E1675-E1679(2011).
[10]
VARIANT HLPP1D TYR-68.
PubMed=21314738; DOI=10.1111/j.1365-2796.2011.02361.x;
Coca-Prieto I., Kroupa O., Gonzalez-Santos P., Magne J.,
Olivecrona G., Ehrenborg E., Valdivielso P.;
"Childhood-onset chylomicronaemia with reduced plasma lipoprotein
lipase activity and mass: identification of a novel GPIHBP1
mutation.";
J. Intern. Med. 270:224-228(2011).
[11]
VARIANTS HLPP1D TYR-65; ARG-108; PRO-115 AND PHE-144.
PubMed=22239554; DOI=10.1111/j.1365-2796.2012.02516.x;
Surendran R.P., Visser M.E., Heemelaar S., Wang J., Peter J.,
Defesche J.C., Kuivenhoven J.A., Hosseini M., Peterfy M.,
Kastelein J.J., Johansen C.T., Hegele R.A., Stroes E.S.,
Dallinga-Thie G.M.;
"Mutations in LPL, APOC2, APOA5, GPIHBP1 and LMF1 in patients with
severe hypertriglyceridaemia.";
J. Intern. Med. 272:185-196(2012).
[12]
VARIANT PHE-14, VARIANT HLPP1D ARG-68, CHARACTERIZATION OF VARIANT
PHE-14, AND CHARACTERIZATION OF VARIANT HLPP1D ARG-68.
PubMed=23831619; DOI=10.5551/jat.18861;
Yamamoto H., Onishi M., Miyamoto N., Oki R., Ueda H., Ishigami M.,
Hiraoka H., Matsuzawa Y., Kihara S.;
"Novel combined GPIHBP1 mutations in a patient with
hypertriglyceridemia associated with CAD.";
J. Atheroscler. Thromb. 20:777-784(2013).
[13]
CHARACTERIZATION OF VARIANTS HLPP1D SER-65; TYR-65; ARG-68; GLY-68;
TYR-68; PHE-89; ARG-108 AND PRO-115, SUBUNIT, INTERACTION WITH LPL,
AND MUTAGENESIS OF TYR-66; LEU-71; THR-91; LEU-92; ILE-93; GLY-101;
THR-104; THR-105; HIS-106; SER-107; THR-108; TRP-109; GLN-115 AND
VAL-126.
PubMed=25387803; DOI=10.1161/CIRCRESAHA.116.305085;
Beigneux A.P., Fong L.G., Bensadoun A., Davies B.S., Oberer M.,
Gaardsvoll H., Ploug M., Young S.G.;
"GPIHBP1 missense mutations often cause multimerization of GPIHBP1 and
thereby prevent lipoprotein lipase binding.";
Circ. Res. 116:624-632(2015).
[14]
VARIANT HLPP1D ARG-83.
PubMed=27578123; DOI=10.1016/j.jacl.2016.03.009;
Rabacchi C., D'Addato S., Palmisano S., Lucchi T., Bertolini S.,
Calandra S., Tarugi P.;
"Clinical and genetic features of 3 patients with familial
chylomicronemia due to mutations in GPIHBP1 gene.";
J. Clin. Lipidol. 10:915-921(2016).
-!- FUNCTION: Plays a key role in the lipolytic processing of
chylomicrons. Required for the transport of lipoprotein lipase LPL
into the capillary lumen (By similarity). {ECO:0000250}.
-!- SUBUNIT: Mostly monomer, but also homodimer and homooligomer
(PubMed:25387803). Interacts with high affinity with high-density
lipoprotein (HDL) (By similarity). Only monomer interacts with
lipoprotein lipase (LPL) (PubMed:25387803, PubMed:17997385).
Interacts with chylomicrons and APOA5 (PubMed:17997385).
{ECO:0000250|UniProtKB:Q9D1N2, ECO:0000269|PubMed:17997385,
ECO:0000269|PubMed:25387803}.
-!- SUBCELLULAR LOCATION: Apical cell membrane
{ECO:0000250|UniProtKB:Q9D1N2}; Lipid-anchor, GPI-anchor
{ECO:0000250|UniProtKB:Q9D1N2}. Basolateral cell membrane
{ECO:0000250|UniProtKB:Q9D1N2}; Lipid-anchor, GPI-anchor
{ECO:0000250|UniProtKB:Q9D1N2}. Cell membrane
{ECO:0000250|UniProtKB:Q9D1N2}; Peripheral membrane protein
{ECO:0000250|UniProtKB:Q9D1N2}; Extracellular side
{ECO:0000250|UniProtKB:Q9D1N2}.
-!- PTM: Glycosylation of Asn-78 is critical for cell surface
localization and the binding of chylomicrons and lipoprotein
lipase. {ECO:0000250}.
-!- POLYMORPHISM: The missense variant Arg-56 may be associated with
severe hypertriglyceridemia and chylomicronemia.
-!- DISEASE: Hyperlipoproteinemia 1D (HLPP1D) [MIM:615947]: An
autosomal recessive disorder characterized by
hyperlipoproteinemia, decreased plasma LPL levels in some
patients, high plasma triglyceride levels, and refractory fasting
chylomicronemia. {ECO:0000269|PubMed:19304573,
ECO:0000269|PubMed:20026666, ECO:0000269|PubMed:21314738,
ECO:0000269|PubMed:21816778, ECO:0000269|PubMed:22239554,
ECO:0000269|PubMed:23831619, ECO:0000269|PubMed:25387803,
ECO:0000269|PubMed:27578123}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
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EMBL; AY245915; AAO86519.1; -; mRNA.
EMBL; CH471162; EAW82276.1; -; Genomic_DNA.
EMBL; BC035810; AAH35810.2; -; mRNA.
EMBL; BC063857; AAH63857.1; -; mRNA.
CCDS; CCDS34954.1; -.
RefSeq; NP_001288701.1; NM_001301772.1.
RefSeq; NP_835466.2; NM_178172.5.
UniGene; Hs.426410; -.
ProteinModelPortal; Q8IV16; -.
BioGrid; 130712; 6.
IntAct; Q8IV16; 1.
STRING; 9606.ENSP00000329266; -.
iPTMnet; Q8IV16; -.
PhosphoSitePlus; Q8IV16; -.
BioMuta; GPIHBP1; -.
DMDM; 74728020; -.
PaxDb; Q8IV16; -.
PeptideAtlas; Q8IV16; -.
PRIDE; Q8IV16; -.
DNASU; 338328; -.
Ensembl; ENST00000622500; ENSP00000480053; ENSG00000277494.
GeneID; 338328; -.
KEGG; hsa:338328; -.
UCSC; uc033cbs.1; human.
CTD; 338328; -.
DisGeNET; 338328; -.
EuPathDB; HostDB:ENSG00000277494.1; -.
GeneCards; GPIHBP1; -.
HGNC; HGNC:24945; GPIHBP1.
HPA; HPA066302; -.
MalaCards; GPIHBP1; -.
MIM; 612757; gene.
MIM; 615947; phenotype.
neXtProt; NX_Q8IV16; -.
Orphanet; 411; Hyperlipoproteinemia type 1.
Orphanet; 70470; Hyperlipoproteinemia type 5.
PharmGKB; PA162390135; -.
eggNOG; ENOG410J46G; Eukaryota.
eggNOG; ENOG41116TR; LUCA.
HOGENOM; HOG000112872; -.
InParanoid; Q8IV16; -.
KO; K20001; -.
OrthoDB; EOG091G0UW5; -.
PhylomeDB; Q8IV16; -.
TreeFam; TF338440; -.
Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
Reactome; R-HSA-8963889; Assembly of active LPL and LIPC lipase complexes.
Reactome; R-HSA-8963901; Chylomicron remodeling.
Reactome; R-HSA-975634; Retinoid metabolism and transport.
GenomeRNAi; 338328; -.
PRO; PR:Q8IV16; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000277494; -.
CleanEx; HS_GPIHBP1; -.
CleanEx; HS_HBP1; -.
Genevisible; Q8IV16; HS.
GO; GO:0031362; C:anchored component of external side of plasma membrane; IDA:BHF-UCL.
GO; GO:0016324; C:apical plasma membrane; ISS:BHF-UCL.
GO; GO:0016323; C:basolateral plasma membrane; ISS:BHF-UCL.
GO; GO:0009897; C:external side of plasma membrane; IDA:BHF-UCL.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0034364; C:high-density lipoprotein particle; IEA:UniProtKB-KW.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0035478; F:chylomicron binding; IDA:BHF-UCL.
GO; GO:0008035; F:high-density lipoprotein particle binding; IEA:Ensembl.
GO; GO:0035473; F:lipase binding; IPI:BHF-UCL.
GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
GO; GO:0071813; F:lipoprotein particle binding; IDA:UniProtKB.
GO; GO:0008320; F:protein transmembrane transporter activity; ISS:BHF-UCL.
GO; GO:0006501; P:C-terminal protein lipidation; TAS:Reactome.
GO; GO:0042632; P:cholesterol homeostasis; ISS:BHF-UCL.
GO; GO:0034371; P:chylomicron remodeling; TAS:Reactome.
GO; GO:0006886; P:intracellular protein transport; ISS:BHF-UCL.
GO; GO:0006869; P:lipid transport; IEA:Ensembl.
GO; GO:0090321; P:positive regulation of chylomicron remnant clearance; ISS:BHF-UCL.
GO; GO:0051006; P:positive regulation of lipoprotein lipase activity; IMP:BHF-UCL.
GO; GO:0017038; P:protein import; ISS:BHF-UCL.
GO; GO:0034394; P:protein localization to cell surface; ISS:BHF-UCL.
GO; GO:0050821; P:protein stabilization; ISS:BHF-UCL.
GO; GO:0051004; P:regulation of lipoprotein lipase activity; TAS:Reactome.
GO; GO:0071503; P:response to heparin; IMP:BHF-UCL.
GO; GO:0001523; P:retinoid metabolic process; TAS:Reactome.
GO; GO:0045056; P:transcytosis; ISS:BHF-UCL.
GO; GO:0070328; P:triglyceride homeostasis; IMP:BHF-UCL.
InterPro; IPR016054; LY6_UPA_recep-like.
Pfam; PF00021; UPAR_LY6; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Disease mutation; Disulfide bond;
Glycoprotein; GPI-anchor; HDL; Lipid-binding; Lipoprotein; Membrane;
Polymorphism; Reference proteome; Signal; Transport.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 151 Glycosylphosphatidylinositol-anchored
high density lipoprotein-binding protein
1.
/FTId=PRO_0000318208.
PROPEP 152 184 Removed in mature form. {ECO:0000305}.
/FTId=PRO_0000429858.
DOMAIN 63 148 UPAR/Ly6.
COMPBIAS 25 31 Poly-Glu.
COMPBIAS 40 50 Poly-Glu.
LIPID 151 151 GPI-anchor amidated glycine.
{ECO:0000250|UniProtKB:Q9D1N2}.
CARBOHYD 78 78 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 65 89 {ECO:0000250}.
DISULFID 68 77 {ECO:0000250}.
DISULFID 83 110 {ECO:0000250}.
DISULFID 114 130 {ECO:0000250}.
DISULFID 131 136 {ECO:0000250}.
VARIANT 14 14 C -> F (polymorphism; it may act as a
disease modifier contributing to severe
HLPP1D when associated with R-68 or F-89;
results in decreased GPIHBP1 expression
at the cell surface; does not affect
interaction with LPL when associated in
cis with R-68 in one individual;
dbSNP:rs11538389).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:21816778,
ECO:0000269|PubMed:23831619}.
/FTId=VAR_044503.
VARIANT 56 56 G -> R (polymorphism; no discernible
effect on interaction with LPL,
chylomicrons or APOA5;
dbSNP:rs587777636).
{ECO:0000269|PubMed:17883852,
ECO:0000269|PubMed:17997385}.
/FTId=VAR_044504.
VARIANT 65 65 C -> S (in HLPP1D; does not affect
protein expression at the cell surface;
does not interact with LPL; promotes
formation of dimers and oligomers
severely reducing number of monomers;
dbSNP:rs587777638).
{ECO:0000269|PubMed:20026666,
ECO:0000269|PubMed:25387803}.
/FTId=VAR_071881.
VARIANT 65 65 C -> Y (in HLPP1D; does not interact with
LPL; promotes formation of dimers and
oligomers severely reducing number of
monomers; dbSNP:rs587777638).
{ECO:0000269|PubMed:22239554,
ECO:0000269|PubMed:25387803}.
/FTId=VAR_077634.
VARIANT 68 68 C -> G (in HLPP1D; does not affect
protein expression at the cell surface;
does not interact with LPL; promotes
formation of dimers and oligomers
reducing number of monomers;
dbSNP:rs587777639).
{ECO:0000269|PubMed:20026666,
ECO:0000269|PubMed:25387803}.
/FTId=VAR_071882.
VARIANT 68 68 C -> R (in HLPP1D; unknown pathological
significance; results in decreased
GPIHBP1 expression; promotes formation of
dimers and oligomers severely reducing
number of monomers; does not affect
interaction with LPL when associated in
cis with F-14 in one individual).
{ECO:0000269|PubMed:23831619,
ECO:0000269|PubMed:25387803}.
/FTId=VAR_077635.
VARIANT 68 68 C -> Y (in HLPP1D; does not interact with
LPL; promotes formation of dimers and
oligomers severely reducing number of
monomers). {ECO:0000269|PubMed:21314738,
ECO:0000269|PubMed:25387803}.
/FTId=VAR_077636.
VARIANT 83 83 C -> R (in HLPP1D).
{ECO:0000269|PubMed:27578123}.
/FTId=VAR_077637.
VARIANT 89 89 C -> F (in HLPP1D; drastically affects
interaction with LPL; promotes formation
of dimers and oligomers reducing number
of monomers; dbSNP:rs587777640).
{ECO:0000269|PubMed:21816778,
ECO:0000269|PubMed:25387803}.
/FTId=VAR_071883.
VARIANT 108 108 T -> R (in HLPP1D; does not interact with
LPL; promotes formation of dimers and
oligomers reducing number of monomers).
{ECO:0000269|PubMed:22239554,
ECO:0000269|PubMed:25387803}.
/FTId=VAR_077638.
VARIANT 115 115 Q -> P (in HLPP1D; a patient with
chylomicronemia; does not affect protein
expression at the cell surface; does not
interact with LPL; does not interact with
chylomicrons; promotes formation of
dimers and oligomers reducing number of
monomers; dbSNP:rs587777637).
{ECO:0000269|PubMed:19304573,
ECO:0000269|PubMed:22239554,
ECO:0000269|PubMed:25387803}.
/FTId=VAR_058086.
VARIANT 144 144 S -> F (in HLPP1D; dbSNP:rs78367243).
{ECO:0000269|PubMed:22239554}.
/FTId=VAR_077639.
VARIANT 175 175 G -> R (in HLPP1D; affects protein
expression at the cell surface; reduces
interaction with LPL; dbSNP:rs145844329).
{ECO:0000269|PubMed:21816778}.
/FTId=VAR_071884.
MUTAGEN 66 66 Y->A: Promotes formation of dimers and
oligomers reducing number of monomers.
{ECO:0000269|PubMed:25387803}.
MUTAGEN 71 71 L->A: Promotes formation of dimers and
oligomers reducing number of monomers.
{ECO:0000269|PubMed:25387803}.
MUTAGEN 91 91 T->A: Promotes formation of dimers and
oligomers reducing number of monomers.
{ECO:0000269|PubMed:25387803}.
MUTAGEN 92 92 L->A: Only slightly increased formation
of dimers and oligomers. No effect on
number of monomers. Loss of LPL
interaction.
{ECO:0000269|PubMed:25387803}.
MUTAGEN 93 93 I->A: Promotes formation of dimers and
oligomers reducing number of monomers.
{ECO:0000269|PubMed:25387803}.
MUTAGEN 101 101 G->S: Promotes formation of dimers and
oligomers reducing number of monomers.
Retained some interaction with LPL.
{ECO:0000269|PubMed:25387803}.
MUTAGEN 104 104 T->A: Promotes formation of dimers and
oligomers reducing number of monomers.
Retained some interaction with LPL.
{ECO:0000269|PubMed:25387803}.
MUTAGEN 105 105 T->A: Promotes formation of dimers and
oligomers reducing number of monomers.
{ECO:0000269|PubMed:25387803}.
MUTAGEN 106 106 H->L: Promotes formation of dimers and
oligomers severely reducing number of
monomers. {ECO:0000269|PubMed:25387803}.
MUTAGEN 107 107 S->A: Promotes formation of dimers and
oligomers reducing number of monomers.
{ECO:0000269|PubMed:25387803}.
MUTAGEN 108 108 T->A: Retained some interaction with LPL.
No effect on number of monomers.
{ECO:0000269|PubMed:25387803}.
MUTAGEN 109 109 W->C,P,T: Promotes formation of dimers
and oligomers reducing number of
monomers. Loss of LPL interaction.
{ECO:0000269|PubMed:25387803}.
MUTAGEN 109 109 W->S,Y,H,A,F: Only slightly increased
formation of dimers and oligomers. No
effect on number of monomers. Loss of LPL
interaction.
{ECO:0000269|PubMed:25387803}.
MUTAGEN 115 115 Q->K: No effect on number of monomers.
{ECO:0000269|PubMed:25387803}.
MUTAGEN 126 126 V->A: Promotes formation of dimers and
oligomers reducing number of monomers.
{ECO:0000269|PubMed:25387803}.
SEQUENCE 184 AA; 19806 MW; 89FF61B08A008C70 CRC64;
MKALGAVLLA LLLCGRPGRG QTQQEEEEED EDHGPDDYDE EDEDEVEEEE TNRLPGGRSR
VLLRCYTCKS LPRDERCNLT QNCSHGQTCT TLIAHGNTES GLLTTHSTWC TDSCQPITKT
VEGTQVTMTC CQSSLCNVPP WQSSRVQDPT GKGAGGPRGS SETVGAALLL NLLAGLGAMG
ARRP


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E81435Hu ELISA Kit for Glycosylphosphatidylinositol Anchored High Density Lipoprotein Binding Protein 1 (GPIHBP1), Organism Homo sapiens (Human), Detection range 0.156-10ng_mL 96T/Kit
CSB-EL009719HU Human glycosylphosphatidylinositol anchored high density lipoprotein binding protein 1 (GPIHBP1) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL009719MO Mouse glycosylphosphatidylinositol anchored high density lipoprotein binding protein 1 (GPIHBP1) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
EIAAB45780 HBP,HDL-binding protein,HDLBP,High density lipoprotein-binding protein,Homo sapiens,Human,VGL,Vigilin
EIAAB45782 Hbp,HDL-binding protein,Hdlbp,High density lipoprotein-binding protein,Rat,Rattus norvegicus,Vigilin
EIAAB45783 HDL-binding protein,Hdlbp,High density lipoprotein-binding protein,Mouse,Mus musculus,Vigilin
AC-405L High Density Chelate Kit, Kit + 40 empty mini columns Includes 2 ml High Density Metal Free, 2 ml High Density Nickel, 2 ml High Density Zinc and 2 ml High Density Cobalt Agarose High Binding Capaci 1 Kit
AC-405L High Density Chelate Kit, Kit + 40 empty mini columns Includes 2 ml High Density Metal Free, 2 ml High Density Nickel, 2 ml High Density Zinc and 2 ml High Density Cobalt Agarose High Binding Capacity 1Kit
18-003-44194 Vigilin - High density lipoprotein-binding protein; HDL-binding protein Polyclonal 0.05 mg Aff Pur
29-350 HDLBP is high density lipoprotein-binding protein, also known as vigilin, is a 110-kD protein that specifically binds HDL molecules and may function in the removal of excess cellular cholesterol.High 0.05 mg
AC-405 High Density Chelate Kit, Kit Includes 2 ml High Density Metal Free, 2 ml High Density Nickel, 2 ml High Density Zinc and 2 ml High Density Cobalt Agarose High Binding Capacity 1Kit
AC-405 High Density Chelate Kit, Kit Includes 2 ml High Density Metal Free, 2 ml High Density Nickel, 2 ml High Density Zinc and 2 ml High Density Cobalt Agarose High Binding Capacity 1 Kit


 

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