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AP-4 complex subunit beta-1 (AP-4 adaptor complex subunit beta) (Adaptor-related protein complex 4 subunit beta-1) (Beta subunit of AP-4) (Beta4-adaptin)

 AP4B1_HUMAN             Reviewed;         739 AA.
Q9Y6B7; B7Z4X3; Q59EJ4; Q96CL6;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
20-FEB-2007, sequence version 2.
18-JUL-2018, entry version 154.
RecName: Full=AP-4 complex subunit beta-1 {ECO:0000305};
AltName: Full=AP-4 adaptor complex subunit beta;
AltName: Full=Adaptor-related protein complex 4 subunit beta-1;
AltName: Full=Beta subunit of AP-4;
AltName: Full=Beta4-adaptin;
Name=AP4B1 {ECO:0000312|HGNC:HGNC:572};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, SUBCELLULAR
LOCATION, TOPOLOGY, AND VARIANT SER-480.
TISSUE=Skeletal muscle;
PubMed=10066790; DOI=10.1074/jbc.274.11.7278;
Dell'Angelica E.C., Mullins C., Bonifacino J.S.;
"AP-4, a novel protein complex related to clathrin adaptors.";
J. Biol. Chem. 274:7278-7285(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Lung;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
SER-480.
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[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] (ISOFORM 1).
TISSUE=Skin;
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]
FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=10436028; DOI=10.1091/mbc.10.8.2787;
Hirst J., Bright N.A., Rous B., Robinson M.S.;
"Characterization of a fourth adaptor-related protein complex.";
Mol. Biol. Cell 10:2787-2802(1999).
[7]
INVOLVEMENT IN SPG47.
PubMed=21620353; DOI=10.1016/j.ajhg.2011.04.019;
Abou Jamra R., Philippe O., Raas-Rothschild A., Eck S.H., Graf E.,
Buchert R., Borck G., Ekici A., Brockschmidt F.F., Nothen M.M.,
Munnich A., Strom T.M., Reis A., Colleaux L.;
"Adaptor protein complex 4 deficiency causes severe autosomal-
recessive intellectual disability, progressive spastic paraplegia, shy
character, and short stature.";
Am. J. Hum. Genet. 88:788-795(2011).
[8]
INTERACTION WITH TEPSIN, AND SUBCELLULAR LOCATION.
PubMed=22472443; DOI=10.1083/jcb.201111049;
Borner G.H., Antrobus R., Hirst J., Bhumbra G.S., Kozik P.,
Jackson L.P., Sahlender D.A., Robinson M.S.;
"Multivariate proteomic profiling identifies novel accessory proteins
of coated vesicles.";
J. Cell Biol. 197:141-160(2012).
[9]
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).
[10]
INTERACTION WITH TEPSIN, REGION, AND MUTAGENESIS OF TRP-635 AND
TYR-682.
PubMed=26542808; DOI=10.1074/jbc.M115.683409;
Mattera R., Guardia C.M., Sidhu S.S., Bonifacino J.S.;
"Bivalent motif-ear interactions mediate the association of the
accessory protein tepsin with the AP-4 adaptor complex.";
J. Biol. Chem. 290:30736-30749(2015).
[11]
INTERACTION WITH TEPSIN, AND MUTAGENESIS OF ILE-669; ALA-670 AND
TYR-682.
PubMed=26756312; DOI=10.1111/tra.12375;
Frazier M.N., Davies A.K., Voehler M., Kendall A.K., Borner G.H.,
Chazin W.J., Robinson M.S., Jackson L.P.;
"Molecular basis for the interaction between AP4 beta4 and its
accessory protein, tepsin.";
Traffic 17:400-415(2016).
[12]
STRUCTURE BY NMR OF 610-739.
Northeast structural genomics consortium (NESG);
"Solution NMR structure of beta-adaptin appendage domain of human
adapter protein complex 4 subunit beta, Northeast structural genomics
consortium (NESG) target HR8998C.";
Submitted (JAN-2014) to the PDB data bank.
-!- FUNCTION: Component of the adaptor protein complex 4 (AP-4).
Adaptor protein complexes are vesicle coat components involved
both in vesicle formation and cargo selection. They control the
vesicular transport of proteins in different trafficking pathways
(PubMed:10066790, PubMed:10436028). AP-4 forms a non clathrin-
associated coat on vesicles departing the trans-Golgi network
(TGN) and may be involved in the targeting of proteins from the
trans-Golgi network (TGN) to the endosomal-lysosomal system. It is
also involved in protein sorting to the basolateral membrane in
epithelial cells and the proper asymmetric localization of
somatodendritic proteins in neurons. AP-4 is involved in the
recognition and binding of tyrosine-based sorting signals found in
the cytoplasmic part of cargos, but may also recognize other types
of sorting signal (Probable). {ECO:0000269|PubMed:10066790,
ECO:0000269|PubMed:10436028, ECO:0000305|PubMed:10066790,
ECO:0000305|PubMed:10436028}.
-!- SUBUNIT: Adaptor protein complex 4 (AP-4) is a heterotetramer
composed of two large adaptins (epsilon-type subunit AP4E1 and
beta-type subunit AP4B1), a medium adaptin (mu-type subunit AP4M1)
and a small adaptin (sigma-type AP4S1) (PubMed:10066790,
PubMed:10436028). Interacts with TEPSIN; this interaction requires
the presence of a functional AP-4 complex (PubMed:22472443,
PubMed:26542808, PubMed:26756312). Interacts with GRIA2; probably
indirect it mediates the somatodendritic localization of GRIA2 in
neurons (By similarity). {ECO:0000250|UniProtKB:Q9WV76,
ECO:0000269|PubMed:10066790, ECO:0000269|PubMed:10436028,
ECO:0000269|PubMed:22472443, ECO:0000269|PubMed:26542808,
ECO:0000269|PubMed:26756312}.
-!- INTERACTION:
Q9H609:ZNF576; NbExp=5; IntAct=EBI-1047606, EBI-3921014;
-!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
membrane {ECO:0000269|PubMed:10066790,
ECO:0000269|PubMed:10436028, ECO:0000269|PubMed:22472443};
Peripheral membrane protein {ECO:0000269|PubMed:10066790}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9Y6B7-1; Sequence=Displayed;
Name=2;
IsoId=Q9Y6B7-2; Sequence=VSP_055787, VSP_055788, VSP_055789;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:10436028}.
-!- DISEASE: Spastic paraplegia 47, autosomal recessive (SPG47)
[MIM:614066]: A form of spastic paraplegia, a neurodegenerative
disorder characterized by a slow, gradual, progressive weakness
and spasticity of the lower limbs. SPG47 is characterized by
neonatal hypotonia that progresses to hypertonia and spasticity,
and severe mental retardation with poor or absent speech
development. {ECO:0000269|PubMed:21620353}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAD93054.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AF092094; AAD20448.1; -; mRNA.
EMBL; AK298037; BAH12709.1; -; mRNA.
EMBL; AB209817; BAD93054.1; ALT_INIT; mRNA.
EMBL; AL137856; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC014146; AAH14146.1; -; mRNA.
CCDS; CCDS865.1; -. [Q9Y6B7-1]
RefSeq; NP_001240781.1; NM_001253852.2. [Q9Y6B7-1]
RefSeq; NP_001240782.1; NM_001253853.2.
RefSeq; NP_001295241.1; NM_001308312.1.
RefSeq; NP_006585.2; NM_006594.4. [Q9Y6B7-1]
UniGene; Hs.515048; -.
UniGene; Hs.736555; -.
PDB; 2MJ7; NMR; -; A=610-739.
PDBsum; 2MJ7; -.
ProteinModelPortal; Q9Y6B7; -.
SMR; Q9Y6B7; -.
BioGrid; 115943; 10.
CORUM; Q9Y6B7; -.
DIP; DIP-24209N; -.
IntAct; Q9Y6B7; 9.
STRING; 9606.ENSP00000256658; -.
iPTMnet; Q9Y6B7; -.
PhosphoSitePlus; Q9Y6B7; -.
BioMuta; AP4B1; -.
DMDM; 126302520; -.
EPD; Q9Y6B7; -.
PaxDb; Q9Y6B7; -.
PeptideAtlas; Q9Y6B7; -.
PRIDE; Q9Y6B7; -.
ProteomicsDB; 86647; -.
DNASU; 10717; -.
Ensembl; ENST00000256658; ENSP00000256658; ENSG00000134262. [Q9Y6B7-1]
Ensembl; ENST00000369569; ENSP00000358582; ENSG00000134262. [Q9Y6B7-1]
GeneID; 10717; -.
KEGG; hsa:10717; -.
UCSC; uc001eeb.4; human. [Q9Y6B7-1]
CTD; 10717; -.
DisGeNET; 10717; -.
EuPathDB; HostDB:ENSG00000134262.12; -.
GeneCards; AP4B1; -.
HGNC; HGNC:572; AP4B1.
HPA; HPA028162; -.
HPA; HPA028652; -.
MalaCards; AP4B1; -.
MIM; 607245; gene.
MIM; 614066; phenotype.
neXtProt; NX_Q9Y6B7; -.
OpenTargets; ENSG00000134262; -.
Orphanet; 280763; Severe intellectual disability and progressive spastic paraplegia.
PharmGKB; PA24864; -.
eggNOG; KOG1061; Eukaryota.
eggNOG; COG5096; LUCA.
GeneTree; ENSGT00530000063138; -.
HOGENOM; HOG000294128; -.
HOVERGEN; HBG050521; -.
InParanoid; Q9Y6B7; -.
KO; K12401; -.
OMA; MSNNDMV; -.
OrthoDB; EOG091G058E; -.
PhylomeDB; Q9Y6B7; -.
TreeFam; TF354235; -.
Reactome; R-HSA-432720; Lysosome Vesicle Biogenesis.
Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
GeneWiki; AP4B1; -.
GenomeRNAi; 10717; -.
PRO; PR:Q9Y6B7; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000134262; -.
CleanEx; HS_AP4B1; -.
ExpressionAtlas; Q9Y6B7; baseline and differential.
Genevisible; Q9Y6B7; HS.
GO; GO:0030124; C:AP-4 adaptor complex; IDA:UniProtKB.
GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0031904; C:endosome lumen; TAS:Reactome.
GO; GO:0019898; C:extrinsic component of membrane; IDA:UniProtKB.
GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
GO; GO:0030276; F:clathrin binding; IEA:InterPro.
GO; GO:0008104; P:protein localization; IC:UniProtKB.
GO; GO:0006605; P:protein targeting; IC:UniProtKB.
GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
Gene3D; 1.25.10.10; -; 1.
Gene3D; 3.30.310.10; -; 1.
InterPro; IPR026739; AP_beta.
InterPro; IPR016342; AP_complex_bsu_1_2_4.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR015151; B-adaptin_app_sub_C.
InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
InterPro; IPR012295; TBP_dom_sf.
PANTHER; PTHR11134; PTHR11134; 1.
Pfam; PF01602; Adaptin_N; 1.
Pfam; PF09066; B2-adapt-app_C; 1.
PIRSF; PIRSF002291; AP_complex_beta; 1.
SMART; SM01020; B2-adapt-app_C; 1.
SUPFAM; SSF48371; SSF48371; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Golgi apparatus; Hereditary spastic paraplegia; Membrane;
Neurodegeneration; Polymorphism; Protein transport;
Reference proteome; Transport.
CHAIN 1 739 AP-4 complex subunit beta-1.
/FTId=PRO_0000193750.
REGION 534 600 Hinge. {ECO:0000305|PubMed:26542808}.
REGION 601 739 Ear; mediates interaction with TEPSIN.
{ECO:0000269|PubMed:26542808}.
VAR_SEQ 113 205 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055787.
VAR_SEQ 373 395 GIARTYTDQCVQILTELLGLRQE -> RCLLLFLLENLDQP
ARKLWLEEP (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055788.
VAR_SEQ 396 739 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055789.
VARIANT 480 480 L -> S (in dbSNP:rs1217401).
{ECO:0000269|PubMed:10066790,
ECO:0000269|Ref.3}.
/FTId=VAR_030804.
MUTAGEN 635 635 W->A: Decreased interaction with TEPSIN.
{ECO:0000269|PubMed:26542808}.
MUTAGEN 669 669 I->A: Decreased interaction with TEPSIN;
when associated with S-670.
{ECO:0000269|PubMed:26756312}.
MUTAGEN 670 670 A->S: Decreased interaction with TEPSIN;
when associated with A-669.
{ECO:0000269|PubMed:26756312}.
MUTAGEN 682 682 Y->A,V: Decreased interaction with
TEPSIN. {ECO:0000269|PubMed:26542808,
ECO:0000269|PubMed:26756312}.
CONFLICT 140 140 A -> V (in Ref. 1; AAD20448).
{ECO:0000305}.
HELIX 628 637 {ECO:0000244|PDB:2MJ7}.
STRAND 641 647 {ECO:0000244|PDB:2MJ7}.
HELIX 654 663 {ECO:0000244|PDB:2MJ7}.
STRAND 667 671 {ECO:0000244|PDB:2MJ7}.
STRAND 677 687 {ECO:0000244|PDB:2MJ7}.
STRAND 692 699 {ECO:0000244|PDB:2MJ7}.
STRAND 701 703 {ECO:0000244|PDB:2MJ7}.
STRAND 705 714 {ECO:0000244|PDB:2MJ7}.
HELIX 717 735 {ECO:0000244|PDB:2MJ7}.
SEQUENCE 739 AA; 83260 MW; B6FC92215BDA5EDC CRC64;
MPYLGSEDVV KELKKALCNP HIQADRLRYR NVIQRVIRYM TQGLDMSGVF MEMVKASATV
DIVQKKLVYL YMCTYAPLKP DLALLAINTL CKDCSDPNPM VRGLALRSMC SLRMPGVQEY
IQQPILNGLR DKASYVRRVA VLGCAKMHNL HGDSEVDGAL VNELYSLLRD QDPIVVVNCL
RSLEEILKQE GGVVINKPIA HHLLNRMSKL DQWGQAEVLN FLLRYQPRSE EELFDILNLL
DSFLKSSSPG VVMGATKLFL ILAKMFPHVQ TDVLVRVKGP LLAACSSESR ELCFVALCHV
RQILHSLPGH FSSHYKKFFC SYSEPHYIKL QKVEVLCELV NDENVQQVLE ELRGYCTDVS
ADFAQAAIFA IGGIARTYTD QCVQILTELL GLRQEHITTV VVQTFRDLVW LCPQCTEAVC
QALPGCEENI QDSEGKQALI WLLGVHGERI PNAPYVLEDF VENVKSETFP AVKMELLTAL
LRLFLSRPAE CQDMLGRLLY YCIEEEKDMA VRDRGLFYYR LLLVGIDEVK RILCSPKSDP
TLGLLEDPAE RPVNSWASDF NTLVPVYGKA HWATISKCQG AERCDPELPK TSSFAASGPL
IPEENKERVQ ELPDSGALML VPNRQLTADY FEKTWLSLKV AHQQVLPWRG EFHPDTLQMA
LQVVNIQTIA MSRAGSRPWK AYLSAQDDTG CLFLTELLLE PGNSEMQISV KQNEARTETL
NSFISVLETV IGTIEEIKS


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EIAAB32876 11S regulator complex subunit beta,Activator of multicatalytic protease subunit 2,Homo sapiens,Human,PA28b,PA28beta,Proteasome activator 28 subunit beta,Proteasome activator complex subunit 2,PSME2,RE
EIAAB32873 11S regulator complex subunit beta,Activator of multicatalytic protease subunit 2,PA28b,PA28beta,Proteasome activator 28 subunit beta,Proteasome activator complex subunit 2,Psme2,Rat,Rattus norvegicus
EIAAB32875 11S regulator complex subunit beta,Activator of multicatalytic protease subunit 2,Mouse,Mus musculus,PA28b,Pa28b1,PA28beta,Proteasome activator 28 subunit beta,Proteasome activator complex subunit 2,P
CSB-EL001860RA Rat adaptor-related protein complex 1, beta 1 subunit (AP1B1) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL001874DO Dog adaptor-related protein complex 3, beta 1 subunit (AP3B1) ELISA kit, Species Dog, Sample Type serum, plasma 96T
CSB-EL001871RA Rat adaptor-related protein complex 2, beta 1 subunit (AP2B1) ELISA kit, Species Rat, Sample Type serum, plasma 96T
EIAAB32777 Macropain subunit C13,Multicatalytic endopeptidase complex subunit C13,Proteasome component C13,Proteasome subunit beta type-8,Proteasome subunit beta-5i,Psmb8,Rat,Rattus norvegicus
EIAAB39001 Homo sapiens,Human,Proximal sequence element-binding transcription factor subunit beta,PSE-binding factor subunit beta,PTF subunit beta,Small nuclear RNA-activating complex polypeptide 3,SNAP50,SNAPc
EIAAB32773 Macropain subunit C13,Multicatalytic endopeptidase complex subunit C13,Pig,Proteasome component C13,Proteasome subunit beta type-8,Proteasome subunit beta-5i,PSMB8,Sus scrofa


 

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