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Paternally-expressed gene 3 protein (ASF-1)

 PEG3_MOUSE              Reviewed;        1571 AA.
Q3URU2; O54978; Q3TQ69; Q5EBP7; Q61138; Q6GQS0; Q80U47; Q8R5N0;
Q9QX53;
19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
11-OCT-2005, sequence version 1.
05-DEC-2018, entry version 117.
RecName: Full=Paternally-expressed gene 3 protein;
AltName: Full=ASF-1;
Name=Peg3; Synonyms=Kiaa0287, Pw1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
DEVELOPMENTAL STAGE.
PubMed=8563758; DOI=10.1038/ng0296-186;
Kuroiwa Y., Kaneko-Ishino T., Kagitani F., Kohda T., Li L.-L.,
Tada M., Suzuki R., Yokoyama M., Shiroishi T., Wakana S., Barton S.C.,
Ishino F., Surani M.A.;
"Peg3 imprinted gene on proximal chromosome 7 encodes for a zinc
finger protein.";
Nat. Genet. 12:186-190(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
STRAIN=B6C3H F1;
PubMed=11260267; DOI=10.1046/j.1365-2443.2001.00412.x;
Kohda T., Asai A., Kuroiwa Y., Kobayashi S., Aisaka K., Nagashima G.,
Yoshida M.C., Kondo Y., Kagiyama N., Kirino T., Kaneko-Ishino T.,
Ishino F.;
"Tumour suppressor activity of human imprinted gene PEG3 in a glioma
cell line.";
Genes Cells 6:237-247(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=12693553; DOI=10.1093/dnares/10.1.35;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
Nakajima D., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
II. The complete nucleotide sequences of 400 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:35-48(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Head;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J; TISSUE=Brain, and Head;
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]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-352 (ISOFORM 1).
PubMed=10704281; DOI=10.1006/geno.1999.6103;
Li L.-L., Szeto I.Y.-Y., Cattanach B.M., Ishino F., Surani M.A.;
"Organization and parent-of-origin-specific methylation of imprinted
Peg3 gene on mouse proximal chromosome 7.";
Genomics 63:333-340(2000).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 191-1571 (ISOFORM 1), SUBCELLULAR
LOCATION, SUBUNIT, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
STRAIN=129/Sv; TISSUE=Limb bud;
PubMed=8806818; DOI=10.1006/dbio.1996.0172;
Relaix F., Weng X., Marazzi G., Yang E., Copeland N.G., Jenkins N.,
Spence S.E., Sassoon D.;
"Pw1, a novel zinc finger gene implicated in the myogenic and neuronal
lineages.";
Dev. Biol. 177:383-396(1996).
[8]
FUNCTION, AND INTERACTION WITH TRAF2.
PubMed=9500555; DOI=10.1038/ng0398-287;
Relaix F., Wei X.-J., Wu X., Sassoon D.A.;
"Peg3/Pw1 is an imprinted gene involved in the TNF-NFkappaB signal
transduction pathway.";
Nat. Genet. 18:287-291(1998).
[9]
FUNCTION.
PubMed=10195900; DOI=10.1126/science.284.5412.330;
Li L.-L., Keverne E.B., Aparicio S.A., Ishino F., Barton S.C.,
Surani M.A.;
"Regulation of maternal behavior and offspring growth by paternally
expressed Peg3.";
Science 284:330-333(1999).
[10]
FUNCTION, INDUCTION, AND INTERACTION WITH SIAH1A AND SIAH2.
PubMed=10681424; DOI=10.1073/pnas.040378897;
Relaix F., Wei X., Li W., Pan J., Lin Y., Bowtell D.D., Sassoon D.A.,
Wu X.;
"Pw1/Peg3 is a potential cell death mediator and cooperates with
Siah1a in p53-mediated apoptosis.";
Proc. Natl. Acad. Sci. U.S.A. 97:2105-2110(2000).
[11]
TISSUE SPECIFICITY.
PubMed=11331620; DOI=10.1093/hmg/10.10.1093;
Hiby S.E., Lough M., Keverne E.B., Surani M.A., Loke Y.W., King A.;
"Paternal monoallelic expression of PEG3 in the human placenta.";
Hum. Mol. Genet. 10:1093-1100(2001).
[12]
FUNCTION, AND INDUCTION.
PubMed=11943780; DOI=10.1074/jbc.M201907200;
Johnson M.D., Wu X., Aithmitti N., Morrison R.S.;
"Peg3/Pw1 is a mediator between p53 and Bax in DNA damage-induced
neuronal death.";
J. Biol. Chem. 277:23000-23007(2002).
-!- FUNCTION: Induces apoptosis in cooperation with SIAH1A. Acts as a
mediator between p53/TP53 and BAX in a neuronal death pathway that
is activated by DNA damage. Acts synergistically with TRAF2 and
inhibits TNF induced apoptosis through activation of NF-kappa-B.
Plays a role in regulating maternal behavior and offspring growth.
{ECO:0000269|PubMed:10195900, ECO:0000269|PubMed:10681424,
ECO:0000269|PubMed:11943780, ECO:0000269|PubMed:9500555}.
-!- SUBUNIT: Homodimer. Interacts with SIAH1A and SIAH2. Interacts
with TRAF2. {ECO:0000269|PubMed:10681424,
ECO:0000269|PubMed:8806818, ECO:0000269|PubMed:9500555}.
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q3URU2-1; Sequence=Displayed;
Name=2;
IsoId=Q3URU2-2; Sequence=VSP_020375, VSP_020376, VSP_020377;
-!- TISSUE SPECIFICITY: Brain, glial cells, neurons, skeletal muscle,
uterus and placenta. In the placenta it found in all trophoblast
cells. {ECO:0000269|PubMed:11260267, ECO:0000269|PubMed:11331620,
ECO:0000269|PubMed:8563758, ECO:0000269|PubMed:8806818}.
-!- DEVELOPMENTAL STAGE: Strongly expressed upon gastrulation and
subsequently becomes restricted to skeletal muscle and subregions
of the CNS. At E9.5, expressed in the branchial arches, somites
and gut but little in the heart and neural tissues. At E12.5
strongly expressed in the cranial skeleton, tongue, vertebral
cartilage, pituitary and the luminal epithelium.
{ECO:0000269|PubMed:8563758, ECO:0000269|PubMed:8806818}.
-!- INDUCTION: Induced during p53/TP53 mediated apoptosis. Up-
regulated by DNA damage in cortical neurons in the presence of
p53/TP53. {ECO:0000269|PubMed:10681424,
ECO:0000269|PubMed:11943780}.
-!- DOMAIN: The SCAN domain enables PEG3 homo- or heterodimerization
to control gene expression in a combinatorial fashion.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC52770.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
Sequence=BAB85589.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
Sequence=BAC65520.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF038939; AAB96922.1; -; mRNA.
EMBL; AB003040; BAB85589.1; ALT_FRAME; mRNA.
EMBL; AK141217; BAE24595.1; -; mRNA.
EMBL; AK163845; BAE37516.1; -; mRNA.
EMBL; AK122238; BAC65520.2; ALT_INIT; Transcribed_RNA.
EMBL; BC072661; AAH72661.1; -; mRNA.
EMBL; BC085183; AAH85183.1; -; mRNA.
EMBL; BC089344; AAH89344.1; -; mRNA.
EMBL; AF105266; AAF16868.1; -; Genomic_DNA.
EMBL; AF105264; AAF16868.1; JOINED; Genomic_DNA.
EMBL; AF105265; AAF16868.1; JOINED; Genomic_DNA.
EMBL; U48804; AAC52770.1; ALT_FRAME; Genomic_DNA.
CCDS; CCDS20783.1; -. [Q3URU2-1]
PIR; T14155; T14155.
PIR; T30173; T30173.
RefSeq; NP_032843.2; NM_008817.2. [Q3URU2-1]
RefSeq; XP_017177520.1; XM_017322031.1. [Q3URU2-1]
RefSeq; XP_017177521.1; XM_017322032.1. [Q3URU2-1]
UniGene; Mm.389800; -.
ProteinModelPortal; Q3URU2; -.
BioGrid; 202106; 3.
IntAct; Q3URU2; 1.
MINT; Q3URU2; -.
STRING; 10090.ENSMUSP00000050750; -.
iPTMnet; Q3URU2; -.
PhosphoSitePlus; Q3URU2; -.
MaxQB; Q3URU2; -.
PaxDb; Q3URU2; -.
PeptideAtlas; Q3URU2; -.
PRIDE; Q3URU2; -.
Ensembl; ENSMUST00000051209; ENSMUSP00000050750; ENSMUSG00000002265. [Q3URU2-1]
GeneID; 18616; -.
KEGG; mmu:18616; -.
UCSC; uc009fbw.1; mouse. [Q3URU2-1]
CTD; 5178; -.
MGI; MGI:104748; Peg3.
eggNOG; KOG1721; Eukaryota.
eggNOG; COG5048; LUCA.
GeneTree; ENSGT00940000162525; -.
HOVERGEN; HBG079943; -.
InParanoid; Q3URU2; -.
KO; K09230; -.
OMA; NCEKLVT; -.
OrthoDB; EOG091G0V3Z; -.
PhylomeDB; Q3URU2; -.
TreeFam; TF337075; -.
ChiTaRS; Peg3; mouse.
PRO; PR:Q3URU2; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000002265; Expressed in 302 organ(s), highest expression level in respiratory primordium.
CleanEx; MM_PEG3; -.
ExpressionAtlas; Q3URU2; baseline and differential.
Genevisible; Q3URU2; MM.
GO; GO:0005776; C:autophagosome; IDA:MGI.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
Pfam; PF00096; zf-C2H2; 5.
SMART; SM00355; ZnF_C2H2; 12.
SUPFAM; SSF57667; SSF57667; 7.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 11.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 12.
1: Evidence at protein level;
Alternative splicing; Apoptosis; Complete proteome; Cytoplasm;
Metal-binding; Nucleus; Reference proteome; Repeat; Zinc; Zinc-finger.
CHAIN 1 1571 Paternally-expressed gene 3 protein.
/FTId=PRO_0000249229.
REPEAT 942 946 1-1.
REPEAT 967 971 1-2.
REPEAT 987 991 2-1.
REPEAT 992 996 1-3.
REPEAT 997 1001 2-2.
REPEAT 1002 1006 1-4.
REPEAT 1007 1011 2-3.
REPEAT 1012 1016 1-5.
REPEAT 1017 1021 1-6.
REPEAT 1022 1026 1-7.
REPEAT 1027 1031 1-8.
REPEAT 1032 1036 1-9.
REPEAT 1047 1051 1-10.
ZN_FING 325 347 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 378 400 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 436 458 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 520 542 C2H2-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 850 872 C2H2-type 5. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 1091 1113 C2H2-type 6. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 1147 1169 C2H2-type 7. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 1209 1231 C2H2-type 8. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 1266 1289 C2H2-type 9. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 1317 1339 C2H2-type 10; degenerate.
{ECO:0000255|PROSITE-ProRule:PRU00042}.
ZN_FING 1488 1510 C2H2-type 11. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 1547 1569 C2H2-type 12. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
REGION 199 265 10 X 5 AA repeat of P-H-X-X-E.
REGION 199 265 3 X 5 AA repeat of P-H-D-D-K.
COMPBIAS 228 231 Poly-Ser.
COMPBIAS 695 698 Poly-Ser.
COMPBIAS 771 774 Poly-Ser.
VAR_SEQ 989 1048 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_020375.
VAR_SEQ 1202 1254 PAVSGSAIRCRQCGQGFIHSSALNEHMRQHRDNEIMEQSEL
SDEIFIQGLALT -> ASSLPNSSGTTTPKFTRMSPMSMGP
PTPMPPFSPSPSGSTSHCTNAKIAASPS (in isoform
2). {ECO:0000303|PubMed:15489334}.
/FTId=VSP_020376.
VAR_SEQ 1255 1571 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_020377.
CONFLICT 5 5 E -> G (in Ref. 1 and 2). {ECO:0000305}.
CONFLICT 156 156 T -> A (in Ref. 1; AAB96922).
{ECO:0000305}.
CONFLICT 321 321 G -> W (in Ref. 2; BAB85589).
{ECO:0000305}.
CONFLICT 351 351 N -> T (in Ref. 6). {ECO:0000305}.
CONFLICT 370 371 KG -> RS (in Ref. 1 and 2).
{ECO:0000305}.
CONFLICT 382 382 E -> V (in Ref. 2; BAB85589).
{ECO:0000305}.
CONFLICT 403 403 E -> R (in Ref. 7). {ECO:0000305}.
CONFLICT 567 568 Missing (in Ref. 7). {ECO:0000305}.
CONFLICT 570 570 K -> E (in Ref. 2; BAB85589).
{ECO:0000305}.
CONFLICT 608 608 R -> G (in Ref. 2; BAB85589).
{ECO:0000305}.
CONFLICT 614 614 F -> S (in Ref. 2; BAB85589).
{ECO:0000305}.
CONFLICT 645 645 K -> E (in Ref. 2; BAB85589).
{ECO:0000305}.
CONFLICT 648 648 F -> L (in Ref. 1; AAB96922).
{ECO:0000305}.
CONFLICT 660 660 Y -> C (in Ref. 1; AAB96922).
{ECO:0000305}.
CONFLICT 669 669 G -> A (in Ref. 7). {ECO:0000305}.
CONFLICT 712 712 E -> K (in Ref. 7). {ECO:0000305}.
CONFLICT 736 737 ND -> MN (in Ref. 2; BAB85589).
{ECO:0000305}.
CONFLICT 856 856 G -> R (in Ref. 7). {ECO:0000305}.
CONFLICT 979 979 D -> V (in Ref. 1; AAB96922).
{ECO:0000305}.
CONFLICT 1011 1011 K -> E (in Ref. 7). {ECO:0000305}.
CONFLICT 1051 1051 E -> Q (in Ref. 5; AAH89344).
{ECO:0000305}.
CONFLICT 1123 1123 E -> G (in Ref. 7). {ECO:0000305}.
CONFLICT 1171 1171 Missing (in Ref. 3; BAC65520).
{ECO:0000305}.
CONFLICT 1181 1181 D -> Y (in Ref. 1 and 2). {ECO:0000305}.
CONFLICT 1401 1401 N -> I (in Ref. 1 and 2). {ECO:0000305}.
SEQUENCE 1571 AA; 178932 MW; 915E13EF0751C6EE CRC64;
MYHHEDDTNS DMNSDDDMSR SGRETPPPRP SHAFGSERDL ERRGRSRDVE PRDRWPYTRN
PRSRLPQRDL SLPVMSRPHF GLDRDDDRRS MDYESRSQDA ESYQNVVELK EDKKPQNPIQ
DNLENYRKLL SLGVQLAEDD RHSHMTQGHS SRSKRTAYPS TSRGLKPMPE AKKPSHRRGI
CEDESSHGVI MEKFIKDVAR NPKSGRAREL NERPPPRFPR PNDNWKDSSS SRRESVIQER
GYEGSAFRGG FRFNADLASR SRALERKRRY HFDSDERGSG HEHKSCVRKK PFECGAEMRQ
AMSMGNLNSP SFSESQSIDF GANPYVCDEC GRQFSVISEF VEHQIMHTRE NLYEYGESFI
HSVAVNEVQK GQGGGKRFEC KECGETFSRS AALAEHRQIH AREYLAECRD QEDEETIMPS
PTFSELQKMY GKDKFYECKV CKETFLHSSA LIEHQKIHGR GNSDDRDNER ERERDRLRAR
AREQRERERE RERERELGEP FLTCPNFNEF RKMYRKDKIY ECKVCGESFL HLSSLREHQK
IHTRGNPFEN KSRMCEETFV PSQSLRRRQK TYREKLFDFN NARDALMGNS DSSEHQKNRS
RRNFFEGRGF EKPFVESQKS HTITRPPENK DDDKPFTISV NPNDKLKFPI MENGSQGKSY
ERSVIHSLGS AEAQKSHGGL GFSKPRPVAE SSTQSSSSIY YPRAHSGGNT YEGKEYKDSI
IHSLPAPRPL KRHRANDHIQ CDEGGESSIY IPDIINKGRK IPAREDAYEG SSSSNYHTPN
VSRAEPPSLS GESHDSKQDV TFSVPSSSVR EHQKARAKKK YIEPRNNETS VIHSLPFGEL
LAGHRRAKFF ECQECGEAFA RRSELIEHQK IHDRERPSGS RHYERSVIRS LAPSDPQTSY
AQERFIQEQV RKFRAFGQRS TTSNNLSVQK IYAQETFNAE EPHDKETHGQ KIHDKEPYGK
EPSGKEPHGD EPQDKEPLDQ EMRSEEPHDD KPHGQEPHDD KPHGQEPHDD KPHGQEPHGD
EPHGQEPHGD EPHDKEPIDQ EMRSEEPHSE ESHGDEPHGE ESHGQEKVED ATIQASVSEE
HQKDDAGDAI YECQDCGLGF TDLNDLTSHQ DTHSRKALVD SREYAHSEVH AHSVSEFEKK
CSGEKLYECP KCGESFIHSS LLFEHQRVHE QDQLYSVKAC DDAFIALLPV RPRRNCTVER
NPAVSGSAIR CRQCGQGFIH SSALNEHMRQ HRDNEIMEQS ELSDEIFIQG LALTEYQGSE
TEEKLFECTI CGECFFTAKQ LGDHHTKVHK DEPYEYGPSY THASFLTEPL RKHIPLYECK
DCGQSFLDDT VIAERMVFHP EREGGSEIVA ATAQEVEANV LIPQEVLRIQ GSNAEAAEPE
VEAAEPEVEA AEPEVEAAEP NGEAEGPDGE AAEPDGEAEQ PNGEAEQPNG DADEPDGAGI
EDPEERADEP EEDVEEPEGD ADEPDGADIE DPEEEGEDQE IEVEEPYYNC HECAETFASS
SAFGEHLKSH ASVIIFEPAN APGECSGYIE RASTSAGGAE QADDKYFKCD VCGQLFNDRL
SLARHQNSHT G


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CSB-EL017773HU Human Paternally-expressed gene 3 protein(PEG3) ELISA kit SpeciesHuman 96T
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bs-1084P Peptides: PEG10(Paternally expressed gene 10) Protein Length:12-25 amino acids. 200ug lyophilized
EIAAB30526 Homo sapiens,Human,KIAA0287,Paternally-expressed gene 3 protein,PEG3,Zinc finger and SCAN domain-containing protein 24,ZSCAN24
PELI2 PEG3 Gene paternally expressed 3
PELI1 PEG10 Gene paternally expressed 10
EIAAB36381 Bos taurus,Bovine,Paternally expressed gene 11 protein homolog,PEG11,Retrotransposon-derived protein PEG11,Retrotransposon-like protein 1,RTL1
E3142h Human Paternally Expressed Protein 10 ELISA Kit 96T
E3532h Human Paternally Expressed Protein 3 ELISA Kit 96T
EIAAB36382 Homo sapiens,Human,Mammalian retrotransposon derived protein 1,MAR1,MART1,Paternally expressed gene 11 protein,PEG11,Retrotransposon-derived protein PEG11,Retrotransposon-like protein 1,RTL1
EIAAB36380 Mammalian retrotransposon derived protein 1,Mar1,Mart1,Mouse,Mus musculus,Paternally expressed gene 11 protein,Peg11,Retrotransposon-derived protein PEG11,Retrotransposon-like protein 1,Rtl1
ARP38756_P050 PEG3 (paternally expressed 3) 50 µg
201-20-4146 PEG10{paternally expressed 10}rabbit.pAb 0.2ml
GS-1599a paternally expressed 10 primary antibody, Host: Rabbit 200ul
MA-20295 Mouse Monoclonal Anti-Human paternally expressed 10 (PEG10) 100 ul


 

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