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Low density lipoprotein receptor adapter protein 1 (Autosomal recessive hypercholesterolemia protein)

 ARH_HUMAN               Reviewed;         308 AA.
Q5SW96; A2BHI5; Q6TQS9; Q8N2Y0; Q9UFI9;
30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 3.
25-OCT-2017, entry version 133.
RecName: Full=Low density lipoprotein receptor adapter protein 1 {ECO:0000305};
AltName: Full=Autosomal recessive hypercholesterolemia protein {ECO:0000303|PubMed:11326085};
Name=LDLRAP1 {ECO:0000312|HGNC:HGNC:18640};
Synonyms=ARH {ECO:0000303|PubMed:11326085};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PRO-202, AND VARIANT ARH
HIS-202.
PubMed=11326085; DOI=10.1126/science.1060458;
Garcia C.K., Wilund K.R., Arca M., Zuliani G., Fellin R., Maioli M.,
Calandra S., Bertolini S., Cossu F., Grishin N., Barnes R.,
Cohen J.C., Hobbs H.H.;
"Autosomal recessive hypercholesterolemia caused by mutations in a
putative LDL receptor adaptor protein.";
Science 292:1394-1398(2001).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PRO-202.
PubMed=12417523; DOI=10.1093/hmg/11.24.3019;
Wilund K.R., Yi M., Campagna F., Arca M., Zuliani G., Fellin R.,
Ho Y.K., Garcia J.V., Hobbs H.H., Cohen J.C.;
"Molecular mechanisms of autosomal recessive hypercholesterolemia.";
Hum. Mol. Genet. 11:3019-3030(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-202.
TISSUE=Uterus;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-202.
TISSUE=Brain;
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).
[6]
INTERACTION WITH LDLR; CLATHRIN AND AP-2 COMPLEX, MUTAGENESIS OF
PHE-165; 212-LEU-LEU-213; ASP-214; GLU-216 AND ARG-266, MOTIF, AND
REGION.
PubMed=12221107; DOI=10.1074/jbc.M208539200;
He G., Gupta S., Yi M., Michaely P., Hobbs H.H., Cohen J.C.;
"ARH is a modular adaptor protein that interacts with the LDL
receptor, clathrin, and AP-2.";
J. Biol. Chem. 277:44044-44049(2002).
[7]
CHARACTERIZATION, INTERACTION WITH CLATHRIN AND AP-2 COMPLEX, AND
SUBCELLULAR LOCATION.
PubMed=12451172; DOI=10.1073/pnas.252630799;
Mishra S.K., Watkins S.C., Traub L.M.;
"The autosomal recessive hypercholesterolemia (ARH) protein interfaces
directly with the clathrin-coat machinery.";
Proc. Natl. Acad. Sci. U.S.A. 99:16099-16104(2002).
[8]
FUNCTION, AND INTERACTION WITH AP2B1.
PubMed=15728179; DOI=10.1074/jbc.M501029200;
Mishra S.K., Keyel P.A., Edeling M.A., Dupin A.L., Owen D.J.,
Traub L.M.;
"Functional dissection of an AP-2 beta2 appendage-binding sequence
within the autosomal recessive hypercholesterolemia protein.";
J. Biol. Chem. 280:19270-19280(2005).
[9]
INTERACTION WITH AP2B1, AND MUTAGENESIS OF ASP-256.
PubMed=16903783; DOI=10.1371/journal.pbio.0040262;
Schmid E.M., Ford M.G.J., Burtey A., Praefcke G.J.K., Peak-Chew S.-Y.,
Mills I.G., Benmerah A., McMahon H.T.;
"Role of the AP2 beta-appendage hub in recruiting partners for
clathrin-coated vesicle assembly.";
PLoS Biol. 4:E262-E262(2006).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-186, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[14]
X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 252-267 IN COMPLEX WITH
AP2B1, AND DOMAIN.
PubMed=16516836; DOI=10.1016/j.devcel.2006.01.016;
Edeling M.A., Mishra S.K., Keyel P.A., Steinhauser A.L., Collins B.M.,
Roth R., Heuser J.E., Owen D.J., Traub L.M.;
"Molecular switches involving the AP-2 beta2 appendage regulate
endocytic cargo selection and clathrin coat assembly.";
Dev. Cell 10:329-342(2006).
[15]
VARIANTS MET-56 AND PRO-202.
PubMed=20124734; DOI=10.5551/jat.2873;
Harada K., Miyamoto Y., Morisaki H., Ohta N., Yamanaka I., Kokubo Y.,
Makino H., Harada-Shiba M., Okayama A., Tomoike H., Okamura T.,
Tomonori O., Saito Y., Yoshimasa Y., Morisaki T.;
"A novel Thr56Met mutation of the autosomal recessive
hypercholesterolemia gene associated with hypercholesterolemia.";
J. Atheroscler. Thromb. 17:131-140(2010).
-!- FUNCTION: Adapter protein (clathrin-associated sorting protein
(CLASP)) required for efficient endocytosis of the LDL receptor
(LDLR) in polarized cells such as hepatocytes and lymphocytes, but
not in non-polarized cells (fibroblasts). May be required for LDL
binding and internalization but not for receptor clustering in
coated pits. May facilitate the endocytocis of LDLR and LDLR-LDL
complexes from coated pits by stabilizing the interaction between
the receptor and the structural components of the pits. May also
be involved in the internalization of other LDLR family members.
Binds to phosphoinositides, which regulate clathrin bud assembly
at the cell surface. Required for trafficking of LRP2 to the
endocytic recycling compartment which is necessary for LRP2
proteolysis, releasing a tail fragment which translocates to the
nucleus and mediates transcriptional repression (By similarity).
{ECO:0000250|UniProtKB:D3ZAR1, ECO:0000269|PubMed:15728179}.
-!- SUBUNIT: Interacts (via PID domain) with LDLR (via NPXY motif)
(PubMed:12221107). Binds to soluble clathrin trimers
(PubMed:12221107). Interacts with AP2B1; the interaction mediates
the association with the AP-2 complex (PubMed:12221107). Interacts
with VLDLR (By similarity). Interacts with LRP2 (By similarity).
{ECO:0000250|UniProtKB:D3ZAR1, ECO:0000250|UniProtKB:Q8C142,
ECO:0000269|PubMed:12221107}.
-!- INTERACTION:
P63010:AP2B1; NbExp=4; IntAct=EBI-747813, EBI-432924;
P63010-2:AP2B1; NbExp=4; IntAct=EBI-747813, EBI-11529439;
P31273:HOXC8; NbExp=4; IntAct=EBI-747813, EBI-1752118;
Q9UPT6:MAPK8IP3; NbExp=4; IntAct=EBI-747813, EBI-717887;
Q8NDX1-2:PSD4; NbExp=5; IntAct=EBI-747813, EBI-12215623;
Q9H668:STN1; NbExp=8; IntAct=EBI-747813, EBI-746930;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12451172}.
-!- TISSUE SPECIFICITY: Expressed at high levels in the kidney, liver,
and placenta, with lower levels detectable in brain, heart,
muscle, colon, spleen, intestine, lung, and leukocytes.
-!- DOMAIN: The [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif mediates
interaction the AP-2 complex subunit AP2B1.
{ECO:0000269|PubMed:16516836}.
-!- DOMAIN: The PID domain mediates interaction with the NPXY
internalization motif of LDLR. {ECO:0000250|UniProtKB:D3ZAR1}.
-!- DISEASE: Hypercholesterolemia, autosomal recessive (ARH)
[MIM:603813]: A familial condition characterized by elevated
circulating cholesterol contained in either low-density
lipoproteins alone or also in very-low-density lipoproteins.
{ECO:0000269|PubMed:11326085}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
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EMBL; AY389348; AAQ90407.1; -; Genomic_DNA.
EMBL; AL117654; CAB56030.2; -; mRNA.
EMBL; AL606491; CAI16483.1; -; Genomic_DNA.
EMBL; BX572623; CAI16483.1; JOINED; Genomic_DNA.
EMBL; BX572623; CAM12863.1; -; Genomic_DNA.
EMBL; AL606491; CAM12863.1; JOINED; Genomic_DNA.
EMBL; BC029770; AAH29770.2; -; mRNA.
CCDS; CCDS30639.1; -.
PIR; T17340; T17340.
RefSeq; NP_056442.2; NM_015627.2.
UniGene; Hs.590911; -.
PDB; 2G30; X-ray; 1.60 A; P=252-267.
PDBsum; 2G30; -.
ProteinModelPortal; Q5SW96; -.
SMR; Q5SW96; -.
BioGrid; 117561; 11.
ELM; Q5SW96; -.
IntAct; Q5SW96; 15.
STRING; 9606.ENSP00000363458; -.
iPTMnet; Q5SW96; -.
PhosphoSitePlus; Q5SW96; -.
BioMuta; LDLRAP1; -.
DMDM; 116241254; -.
EPD; Q5SW96; -.
MaxQB; Q5SW96; -.
PaxDb; Q5SW96; -.
PeptideAtlas; Q5SW96; -.
PRIDE; Q5SW96; -.
DNASU; 26119; -.
Ensembl; ENST00000374338; ENSP00000363458; ENSG00000157978.
GeneID; 26119; -.
KEGG; hsa:26119; -.
UCSC; uc001bkl.5; human.
CTD; 26119; -.
DisGeNET; 26119; -.
EuPathDB; HostDB:ENSG00000157978.11; -.
GeneCards; LDLRAP1; -.
H-InvDB; HIX0023695; -.
HGNC; HGNC:18640; LDLRAP1.
HPA; CAB003705; -.
HPA; HPA050358; -.
MalaCards; LDLRAP1; -.
MIM; 603813; phenotype.
MIM; 605747; gene.
neXtProt; NX_Q5SW96; -.
OpenTargets; ENSG00000157978; -.
Orphanet; 391665; Homozygous familial hypercholesterolemia.
PharmGKB; PA128394641; -.
eggNOG; KOG3536; Eukaryota.
eggNOG; ENOG410ZHJT; LUCA.
GeneTree; ENSGT00530000062937; -.
HOGENOM; HOG000030906; -.
HOVERGEN; HBG058060; -.
InParanoid; Q5SW96; -.
KO; K12474; -.
OMA; FEFWQVS; -.
OrthoDB; EOG091G0TOH; -.
PhylomeDB; Q5SW96; -.
TreeFam; TF314159; -.
Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
Reactome; R-HSA-8964026; Chylomicron clearance.
Reactome; R-HSA-8964038; LDL clearance.
EvolutionaryTrace; Q5SW96; -.
GeneWiki; Low_density_lipoprotein_receptor_adapter_protein_1; -.
GenomeRNAi; 26119; -.
PRO; PR:Q5SW96; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000157978; -.
CleanEx; HS_LDLRAP1; -.
Genevisible; Q5SW96; HS.
GO; GO:0030424; C:axon; ISS:BHF-UCL.
GO; GO:0009925; C:basal plasma membrane; IDA:UniProtKB.
GO; GO:0030665; C:clathrin-coated vesicle membrane; TAS:Reactome.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005769; C:early endosome; IDA:UniProtKB.
GO; GO:0005883; C:neurofilament; ISS:BHF-UCL.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0055037; C:recycling endosome; IDA:BHF-UCL.
GO; GO:0001540; F:amyloid-beta binding; IPI:BHF-UCL.
GO; GO:0035612; F:AP-2 adaptor complex binding; IDA:BHF-UCL.
GO; GO:0035615; F:clathrin adaptor activity; IDA:BHF-UCL.
GO; GO:0030276; F:clathrin binding; IDA:UniProtKB.
GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IPI:BHF-UCL.
GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:BHF-UCL.
GO; GO:0001784; F:phosphotyrosine residue binding; IDA:UniProtKB.
GO; GO:0030159; F:receptor signaling complex scaffold activity; IMP:UniProtKB.
GO; GO:0035591; F:signaling adaptor activity; IDA:BHF-UCL.
GO; GO:0042982; P:amyloid precursor protein metabolic process; IMP:BHF-UCL.
GO; GO:0042632; P:cholesterol homeostasis; IMP:BHF-UCL.
GO; GO:0008203; P:cholesterol metabolic process; NAS:UniProtKB.
GO; GO:0034383; P:low-density lipoprotein particle clearance; IMP:BHF-UCL.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0090205; P:positive regulation of cholesterol metabolic process; IC:BHF-UCL.
GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; IMP:UniProtKB.
GO; GO:1905602; P:positive regulation of receptor-mediated endocytosis involved in cholesterol transport; IMP:BHF-UCL.
GO; GO:0031623; P:receptor internalization; IMP:BHF-UCL.
GO; GO:0006898; P:receptor-mediated endocytosis; IDA:BHF-UCL.
GO; GO:0090118; P:receptor-mediated endocytosis involved in cholesterol transport; IMP:BHF-UCL.
GO; GO:0043393; P:regulation of protein binding; IMP:UniProtKB.
GO; GO:1903076; P:regulation of protein localization to plasma membrane; IMP:BHF-UCL.
GO; GO:0006810; P:transport; NAS:UniProtKB.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR011993; PH_dom-like.
InterPro; IPR006020; PTB/PI_dom.
Pfam; PF00640; PID; 1.
SMART; SM00462; PTB; 1.
SUPFAM; SSF50729; SSF50729; 1.
PROSITE; PS01179; PID; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Atherosclerosis; Cholesterol metabolism;
Complete proteome; Cytoplasm; Disease mutation; Endocytosis;
Hyperlipidemia; Lipid metabolism; Phosphoprotein; Polymorphism;
Reference proteome; Steroid metabolism; Sterol metabolism.
CHAIN 1 308 Low density lipoprotein receptor adapter
protein 1.
/FTId=PRO_0000064675.
DOMAIN 42 196 PID. {ECO:0000255|PROSITE-
ProRule:PRU00148}.
REGION 249 276 AP-2 complex binding.
{ECO:0000269|PubMed:12221107}.
MOTIF 212 216 Clathrin box.
{ECO:0000269|PubMed:12221107}.
MOTIF 257 266 [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif.
{ECO:0000269|PubMed:16516836}.
COMPBIAS 23 26 Poly-Gly.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 14 14 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 186 186 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 202 202 Phosphoserine.
{ECO:0000250|UniProtKB:Q8C142}.
VARIANT 56 56 T -> M (probable disease-associated
mutation found in patients with
hypercholesterolemia; dbSNP:rs752849346).
{ECO:0000269|PubMed:20124734}.
/FTId=VAR_076925.
VARIANT 202 202 S -> H (in ARH; Lebanon; requires 2
nucleotide substitutions;
dbSNP:rs386629678).
{ECO:0000269|PubMed:11326085}.
/FTId=VAR_023320.
VARIANT 202 202 S -> P (in dbSNP:rs6687605).
{ECO:0000269|PubMed:11326085,
ECO:0000269|PubMed:12417523,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17974005,
ECO:0000269|PubMed:20124734}.
/FTId=VAR_028403.
MUTAGEN 165 165 F->A: Abolishes LDLR cytoplasmic tail
binding. {ECO:0000269|PubMed:12221107}.
MUTAGEN 165 165 F->V: Abolishes LDLR cytoplasmic tail
binding. {ECO:0000269|PubMed:12221107}.
MUTAGEN 212 213 LL->AA: Abolishes clathrin binding.
{ECO:0000269|PubMed:12221107}.
MUTAGEN 214 214 D->A: Abolishes clathrin binding.
{ECO:0000269|PubMed:12221107}.
MUTAGEN 216 216 E->A: Abolishes clathrin binding.
{ECO:0000269|PubMed:12221107}.
MUTAGEN 256 256 D->R: Abolishes interaction with AP2B1.
{ECO:0000269|PubMed:16903783}.
MUTAGEN 266 266 R->A: Abolishes AP-2 complex binding.
{ECO:0000269|PubMed:12221107}.
HELIX 256 266 {ECO:0000244|PDB:2G30}.
SEQUENCE 308 AA; 33885 MW; DE83168CB328D2A7 CRC64;
MDALKSAGRA LIRSPSLAKQ SWGGGGRHRK LPENWTDTRE TLLEGMLFSL KYLGMTLVEQ
PKGEELSAAA IKRIVATAKA SGKKLQKVTL KVSPRGIILT DNLTNQLIEN VSIYRISYCT
ADKMHDKVFA YIAQSQHNQS LECHAFLCTK RKMAQAVTLT VAQAFKVAFE FWQVSKEEKE
KRDKASQEGG DVLGARQDCT PSLKSLVATG NLLDLEETAK APLSTVSANT TNMDEVPRPQ
ALSGSSVVWE LDDGLDEAFS RLAQSRTNPQ VLDTGLTAQD MHYAQCLSPV DWDKPDSSGT
EQDDLFSF


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LRPAP1-1384H Protein: Recombinant Human Low Density Lipoprotein Receptor-Related Protein Associated Protein 1, His-tagged 20ug
GATM-1925H Protein: Recombinant Human Low Density Lipoprotein Receptor-Related Protein Associated Protein 1, His-tagged 50ug
LRPAP1-1384H Protein Recombinant Human Low Density Lipoprotein Receptor-Related Protein Associated Protein 1, His-tagged 20ug
GATM-1925H Protein Recombinant Human Low Density Lipoprotein Receptor-Related Protein Associated Protein 1, His-tagged 50ug
EIAAB42483 Adaptor protein Wyatt,Homo sapiens,Human,MAL,MyD88 adapter-like protein,TIR domain-containing adapter protein,TIRAP,Toll_interleukin-1 receptor domain-containing adapter protein
pro-1029 Recombinant Human Low Density Lipoprotein Receptor-Related Protein Associated Protein 1 5
pro-1029 Recombinant Human Low Density Lipoprotein Receptor-Related Protein Associated Protein 1 20
E1509m Human ELISA Kit FOR Low-density lipoprotein receptor-related protein 5-like protein 96T
LRRC1 LRPAP1 Gene low density lipoprotein receptor-related protein associated protein 1
pro-1029 Recombinant Human Low Density Lipoprotein Receptor-Related Protein Associated Protein 1 1mg


 

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