GENTAUR Molecular Products.
Monoclonal Antibody, ELISA Kit, Polyclonal Antibody, Recombinant/Purified Protein.Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery
Protocadherin-8 (Activity-regulated cadherin-like protein) (Arcadlin)
PCDH8_RAT Reviewed; 1069 AA.
D3ZE55; A1A5N4; Q9WVR2;
08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
08-FEB-2011, sequence version 2.
22-NOV-2017, entry version 56.
RecName: Full=Protocadherin-8;
AltName: Full=Activity-regulated cadherin-like protein;
Short=Arcadlin;
Flags: Precursor;
Name=Pcdh8;
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 [MRNA] (ISOFORM 2), FUNCTION, SUBUNIT, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
TISSUE=Hippocampus;
PubMed=10383464; DOI=10.1074/jbc.274.27.19473;
Yamagata K., Andreasson K.I., Sugiura H., Maru E., Dominique M.,
Irie Y., Miki N., Hayashi Y., Yoshioka M., Kaneko K., Kato H.,
Worley P.F.;
"Arcadlin is a neural activity-regulated cadherin involved in long
term potentiation.";
J. Biol. Chem. 274:19473-19479(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-694.
STRAIN=Brown Norway/NHsdMcwi; TISSUE=Embryonic 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).
[4]
FUNCTION, INTERACTION WITH CDH2; CDH11 AND TAOK2, AND INDUCTION.
PubMed=17988630; DOI=10.1016/j.neuron.2007.08.020;
Yasuda S., Tanaka H., Sugiura H., Okamura K., Sakaguchi T., Tran U.,
Takemiya T., Mizoguchi A., Yagita Y., Sakurai T., De Robertis E.M.,
Yamagata K.;
"Activity-induced protocadherin arcadlin regulates dendritic spine
number by triggering N-cadherin endocytosis via TAO2beta and p38 MAP
kinases.";
Neuron 56:456-471(2007).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1052, 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: Calcium-dependent cell-adhesion protein. May play a role
in activity-induced synaptic reorganization underlying long term
memory. Could be involved in CDH2 internalization through
TAOK2/p38 MAPK pathway. In hippocampal neurons, may play a role in
the down-regulation of dendritic spines, maybe through its action
on CDH2 endocytosis. {ECO:0000269|PubMed:10383464,
ECO:0000269|PubMed:17988630}.
-!- SUBUNIT: The N-terminal extracellular domain forms homophilic
interactions; these interactions activate p38 MAPK via TAOK2 and
trigger endocytosis. Interacts with CDH2; this interaction may
lead to CDH2 cointernalization. Interacts with CDH11. Interacts
with TAOK2. {ECO:0000269|PubMed:10383464,
ECO:0000269|PubMed:17988630}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass
type I membrane protein {ECO:0000250}. Cell projection, dendrite
{ECO:0000269|PubMed:10383464}. Cell junction, synapse, presynaptic
cell membrane {ECO:0000269|PubMed:10383464}. Cell junction,
synapse, postsynaptic cell membrane {ECO:0000269|PubMed:10383464}.
Note=Also expressed in the cell bodies of neurons of the
hippocampus and cortex. Localized to excitatory, but not with
inhibitory, synapses.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=D3ZE55-1; Sequence=Displayed;
Note=No experimental confirmation available.;
Name=2;
IsoId=D3ZE55-2; Sequence=VSP_040565;
Note=May be the only physiologically relevant isoform.
{ECO:0000305|PubMed:10383464};
-!- TISSUE SPECIFICITY: Enriched in brain relative to peripheral
tissues, with low expression in the testis. Expressed in
hippocampal neurons (at protein level).
{ECO:0000269|PubMed:10383464}.
-!- DEVELOPMENTAL STAGE: At E17, expressed in the auditory circuit,
most prominently in the inferior colliculus, and later in the
medial geniculate and the auditory cortex at P0. At P0, also
expressed in targets of retinal projections, such as the superior
colliculus, the suprachiasmatic nucleus, and the ventrolateral
geniculate nucleus. At the same stage, detected in selected
structures of the limbic circuit, including the anterior limbic
thalamic nuclei, the hippocampus, amygdala and habenula.
{ECO:0000269|PubMed:10383464}.
-!- INDUCTION: Rapidly and transiently induced by maximal
electroconvulsive seizure in the hippocampal granule cells, and
modestly induced in the pyramidal cells. Also induced by cAMP.
{ECO:0000269|PubMed:10383464, ECO:0000269|PubMed:17988630}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB026154; BAA82442.1; -; mRNA.
EMBL; CH473951; EDM02373.1; -; Genomic_DNA.
EMBL; BC128737; AAI28738.1; -; mRNA.
RefSeq; NP_074059.1; NM_022868.1.
RefSeq; XP_008769119.1; XM_008770897.2. [D3ZE55-1]
UniGene; Rn.23337; -.
SMR; D3ZE55; -.
STRING; 10116.ENSRNOP00000017599; -.
iPTMnet; D3ZE55; -.
PhosphoSitePlus; D3ZE55; -.
SwissPalm; D3ZE55; -.
UniCarbKB; D3ZE55; -.
PaxDb; D3ZE55; -.
PRIDE; D3ZE55; -.
Ensembl; ENSRNOT00000017599; ENSRNOP00000017599; ENSRNOG00000013101. [D3ZE55-1]
GeneID; 64865; -.
KEGG; rno:64865; -.
CTD; 5100; -.
RGD; 69350; Pcdh8.
eggNOG; KOG3594; Eukaryota.
eggNOG; ENOG410XQHI; LUCA.
GeneTree; ENSGT00900000140770; -.
HOVERGEN; HBG054878; -.
InParanoid; D3ZE55; -.
KO; K16499; -.
OMA; QWDTPLI; -.
OrthoDB; EOG091G00QD; -.
PhylomeDB; D3ZE55; -.
PRO; PR:D3ZE55; -.
Proteomes; UP000002494; Chromosome 15.
Bgee; ENSRNOG00000013101; -.
Genevisible; D3ZE55; RN.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
GO; GO:0007268; P:chemical synaptic transmission; IDA:RGD.
GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
GO; GO:0007616; P:long-term memory; TAS:RGD.
GO; GO:0016331; P:morphogenesis of embryonic epithelium; ISO:RGD.
GO; GO:0007399; P:nervous system development; IBA:GO_Central.
GO; GO:0001756; P:somitogenesis; ISO:RGD.
InterPro; IPR002126; Cadherin.
InterPro; IPR015919; Cadherin-like.
InterPro; IPR020894; Cadherin_CS.
InterPro; IPR013164; Cadherin_N.
InterPro; IPR030711; Protocadherin-8.
PANTHER; PTHR24028:SF46; PTHR24028:SF46; 1.
Pfam; PF00028; Cadherin; 5.
Pfam; PF08266; Cadherin_2; 1.
PRINTS; PR00205; CADHERIN.
SMART; SM00112; CA; 6.
SUPFAM; SSF49313; SSF49313; 6.
PROSITE; PS00232; CADHERIN_1; 5.
PROSITE; PS50268; CADHERIN_2; 6.
1: Evidence at protein level;
Alternative splicing; Calcium; Cell adhesion; Cell junction;
Cell membrane; Cell projection; Complete proteome; Glycoprotein;
Membrane; Phosphoprotein; Postsynaptic cell membrane;
Reference proteome; Repeat; Signal; Synapse; Transmembrane;
Transmembrane helix.
SIGNAL 1 29 {ECO:0000255}.
CHAIN 30 1069 Protocadherin-8.
/FTId=PRO_0000404297.
TOPO_DOM 30 747 Extracellular. {ECO:0000255}.
TRANSMEM 748 768 Helical. {ECO:0000255}.
TOPO_DOM 769 1069 Cytoplasmic. {ECO:0000255}.
DOMAIN 30 135 Cadherin 1. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 136 245 Cadherin 2. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 247 354 Cadherin 3. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 393 497 Cadherin 4. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 498 609 Cadherin 5. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 615 721 Cadherin 6. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
MOD_RES 1052 1052 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
CARBOHYD 616 616 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 779 875 Missing (in isoform 2).
{ECO:0000303|PubMed:10383464}.
/FTId=VSP_040565.
CONFLICT 351 351 A -> P (in Ref. 1; BAA82442).
{ECO:0000305}.
SEQUENCE 1069 AA; 113191 MW; 307DB9763F69D7D3 CRC64;
MSPVKRWGSP CLFPLQLFSL CWVLSVAQSK TVRYSTFEED APGTVIGTLA EDLHMKVSGD
TSFRLMKQFN SSLLRVREGD GQLTVGDAGL DRERLCGQSP QCVLAFDVVS FSQEQFRLVH
VEVEVRDVND HAPRFPRAQI PVEVSESAPV GTRIPLEVPV DEDVGANGLQ SVRLAEPHSP
FRVELQTRAD GAQCADLVLL QELDRESQAS YSLELVAQDG GRPPRSATAA LSVRVLDAND
HSPAFPQGAV AEVELAEDAP VGSLLLDLDA ADPDEGPNGD VVFTFGARTP PEARHLFRLD
PRSGRLTLAG QVDYERQDTY ELDVRAQDRG PGPRTATCKV IVRIRDVNDN APDISITPLA
APGAPATSPF AAAAAAAALG GADAASSAGS GTQETGVTSL VPEGAARESL VALVSTSDRD
SGANGQVRCA LYGHEHFRLQ PAYAGSYLVV TAASLDRERI AEYNLTLVAE DRGAPPLRTV
RPYTVRVGDE NDNAPLFTKP VYEVSVRENN PPGAYLATVA ARDPDLGRNG QVTYRLVEAE
VGRSGEAVST YVSVDPATGA IYALRSFDYE TLRQLDVRVQ ASDGGSPQLS SNALVQVRVL
DQNDHSPVLV HPAPANGSLE VAVPGRSTKD TAVARIQARD ADEGANGELA FDLLQQEPRE
AFSIGRHTGE IVLTGDLSQE PPGRVFKALL VISDGGRPPL TTTATVSFVV TAGGGSAVPA
SAGSPEHFRP PGSRLAPSGP SLQWDTPLIV IIVLAGSCTL LLAAIIAIAT TCNRRKKEVR
KGGALREERP GAAGGGASAP GSPDETARGT GPRPNMFDVL TFPGSGKAPF GSPAADAPPP
AVAAAEVPGS EGGSATGESA CHFEGQQRLR GAHAEPYSAS PGFGKEPAPP VAVWKGHSFN
TISGREAEKF SGKDSGKGDS DFNDSDSDIS GDALKKDLIN HMQSGLWACT AECKILGHSD
RCWSPSCAGP NTHPPPHPPA QMSTFCKSTS LPRDPLRRDN YYQAQLPKTV GLQSVYEKVL
HRDYDRTVTL LSPPRPGRLP DLQEIGVPLY ESPPGGRYVS PKKGTNENV
Related products :
GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45
Fax 0032 16 50 90 45
info@gentaur.com | Gentaur
GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur
GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50
Fax 01 43 25 01 60
RCS Paris B 484 237 888
SIRET 48423788800017
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
france@gentaur.com | Gentaur
GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88
Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur
GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com
Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123
GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel: 0208-080893 Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62 SWIFT RABONL2U
GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur
ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF
GENTAUR Poland Sp. z o.o.
ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX 058 710 33 48
poland@gentaur.com | Gentaur
Other countries
Österreich +43720880899
Canada Montreal +15149077481
Ceská republika Praha +420246019719
Danmark +4569918806
Finland Helsset +358942419041
Magyarország Budapest +3619980547
Ireland Dublin+35316526556
Luxembourg+35220880274
Norge Oslo+4721031366
Sverige Stockholm+46852503438
Schweiz Züri+41435006251
US New York+17185132983
GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo
Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur
Pathways :
WP1983: Splicing factor NOVA regulated synpatic proteins
WP1049: G Protein Signaling Pathways
WP1059: Diurnally regulated genes with circadian orthologs
WP1165: G Protein Signaling Pathways
WP1175: Diurnally regulated genes with circadian orthologs
WP1268: Diurnally regulated genes with circadian orthologs
WP1306: Diurnally regulated genes with circadian orthologs
WP1371: G Protein Signaling Pathways
WP1379: Diurnally regulated genes with circadian orthologs
WP1438: Influenza A virus infection
WP1455: Serotonin Transporter Activity
WP1488: CFTR activity in the plasma membrane
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP152: FGF signaling pathway
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1601: Fluoropyrimidine Activity
WP1602: Nicotine Activity on Dopaminergic Neurons
WP1603: Nicotine Activity on Chromaffin Cells
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
Related Genes :
[PCDH11Y PCDH11 PCDH22 PCDHY] Protocadherin-11 Y-linked (Protocadherin-11) (Protocadherin on the Y chromosome) (PCDH-Y) (Protocadherin prostate cancer) (Protocadherin-PC) (Protocadherin-22)
[PCDH11X KIAA1326 PCDH11 PCDHX] Protocadherin-11 X-linked (Protocadherin-11) (Protocadherin on the X chromosome) (PCDH-X) (Protocadherin-S)
[Pcdh8 Papc] Protocadherin-8 (Arcadlin) (Paraxial protocadherin)
[PCDH8] Protocadherin-8 (Arcadlin)
[Pcdh8] Protocadherin-8 (Activity-regulated cadherin-like protein) (Arcadlin)
[Pcdhb8] Protocadherin beta-8 (PCDH-beta-8)
[FAT2 CDHF8 KIAA0811 MEGF1] Protocadherin Fat 2 (hFat2) (Cadherin family member 8) (Multiple epidermal growth factor-like domains protein 1) (Multiple EGF-like domains protein 1)
[PCDHB8 PCDH3I] Protocadherin beta-8 (PCDH-beta-8) (Protocadherin-3I)
[CDHR5 MUCDHL MUPCDH UNQ2781/PRO7168] Cadherin-related family member 5 (Mu-protocadherin) (Mucin and cadherin-like protein) (Mucin-like protocadherin) (MLPCDH)
[FAT1 CDHF7 FAT] Protocadherin Fat 1 (Cadherin family member 7) (Cadherin-related tumor suppressor homolog) (Protein fat homolog) [Cleaved into: Protocadherin Fat 1, nuclear form]
[PCDH1] Protocadherin-1 (Cadherin-like protein 1) (Protocadherin-42) (PC42)
[CDHR2 PCDH24 PCLKC] Cadherin-related family member 2 (Protocadherin LKC) (PC-LKC) (Protocadherin-24)
[DCHS2 CDH27 CDHJ PCDH23 PCDHJ] Protocadherin-23 (Cadherin-27) (Cadherin-like protein CDHJ) (Cadherin-like protein VR8) (Protein dachsous homolog 2) (Protocadherin PCDHJ)
[Pcdh15] Protocadherin-15
[PCDH15 USH1F] Protocadherin-15
[PCDH19 KIAA1313] Protocadherin-19
[Pcdha4 Cnr1] Protocadherin alpha-4 (PCDH-alpha-4)
[Pcdh15] Protocadherin-15
[PCDHA8] Protocadherin alpha-8 (PCDH-alpha-8)
[stan fmi CG11895] Protocadherin-like wing polarity protein stan (Protein flamingo) (Protein starry night)
[Pcdha7] Protocadherin alpha-7 (PCDH-alpha-7)
[Pcdhb6] Protocadherin beta-6 (PCDH-beta-6)
[PCDH17 PCDH68 PCH68] Protocadherin-17 (Protocadherin-68)
[PCDHA10 CNRS8] Protocadherin alpha-10 (PCDH-alpha-10)
[Cdhr5 Mucdhl Mupcdh] Cadherin-related family member 5 (GP100) (Mu-protocadherin)
[PCDHB9 PCDH3H] Protocadherin beta-9 (PCDH-beta-9) (Protocadherin-3H)
[PCDHB16 KIAA1621 PCDH3X] Protocadherin beta-16 (PCDH-beta-16) (Protocadherin-3X)
[PCDHA4] Protocadherin alpha-4 (PCDH-alpha-4)
[Pcdha4 Cnrv4] Protocadherin alpha-4 (PCDH-alpha-4) (Cadherin-related neuronal receptor 4)
[PCDH7 BHPCDH] Protocadherin-7 (Brain-heart protocadherin) (BH-Pcdh)
Bibliography :
No related Items
Enter catalog number :
Favorites Pages:
No Favorits