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Septin-4 (Brain protein H5) (Peanut-like protein 2)

 SEPT4_MOUSE             Reviewed;         478 AA.
P28661; B2KGM6; Q3UVH1; Q3UZC3; Q5ND10; Q5ND15; Q5ND16; Q7TPM7;
Q80VX1;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
01-DEC-1992, sequence version 1.
23-MAY-2018, entry version 151.
RecName: Full=Septin-4;
AltName: Full=Brain protein H5;
AltName: Full=Peanut-like protein 2;
Name=Sept4; Synonyms=Pnutl2;
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 [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=BALB/cJ; TISSUE=Brain;
PubMed=12106288; DOI=10.1111/j.1460-9568.1990.tb00460.x;
Kato K.;
"A collection of cDNA clones with specific expression patterns in
mouse brain.";
Eur. J. Neurosci. 2:704-711(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), INTERACTION WITH DPYSL5,
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION, AND
DEVELOPMENTAL STAGE.
TISSUE=Brain;
PubMed=12581152; DOI=10.1046/j.1365-2443.2003.00617.x;
Takahashi S., Inatome R., Yamamura H., Yanagi S.;
"Isolation and expression of a novel mitochondrial septin that
interacts with CRMP/CRAM in the developing neurones.";
Genes Cells 8:81-93(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 5 AND 6).
STRAIN=C57BL/6J; TISSUE=Cerebellum, and Embryo;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
SPLICING.
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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).
[7]
PROTEIN SEQUENCE OF 282-290, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[9]
SUBCELLULAR LOCATION.
PubMed=17546647; DOI=10.1002/humu.20554;
Sudo K., Ito H., Iwamoto I., Morishita R., Asano T., Nagata K.;
"SEPT9 sequence alternations causing hereditary neuralgic amyotrophy
are associated with altered interactions with SEPT4/SEPT11 and
resistance to Rho/Rhotekin-signaling.";
Hum. Mutat. 28:1005-1013(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-29; SER-68;
SER-117; SER-118; SER-325; SER-432 AND THR-434, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Filament-forming cytoskeletal GTPase. Forms a
filamentous structure with SEPT12, SEPT6, SEPT2 and probably SEPT4
at the sperm annulus which is required for the structural
integrity and motility of the sperm tail during postmeiotic
differentiation (By similarity). May play a role in cytokinesis
(Potential). May play a role in platelet secretion (By
similarity). {ECO:0000250, ECO:0000250|UniProtKB:O43236,
ECO:0000305}.
-!- SUBUNIT: Septins polymerize into heterooligomeric protein
complexes that form filaments, and can associate with cellular
membranes, actin filaments and microtubules. GTPase activity is
required for filament formation (By similarity). Interacts with
SEPT8 (By similarity). Component of a septin core octomeric
complex consisting of SEPT12, SEPT7, SEPT6 and SEPT2 or SEPT4 in
the order 12-7-6-2-2-6-7-12 or 12-7-6-4-4-6-7-12 and located in
the sperm annulus (By similarity). Isoform 4 interacts with
DPYSL5. {ECO:0000250, ECO:0000250|UniProtKB:O43236,
ECO:0000269|PubMed:12581152}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12581152,
ECO:0000269|PubMed:17546647}. Cytoplasm, cytoskeleton
{ECO:0000250}. Cell projection, cilium, flagellum
{ECO:0000250|UniProtKB:O43236}. Note=Found in the sperm annulus.
{ECO:0000250|UniProtKB:O43236}.
-!- SUBCELLULAR LOCATION: Isoform 4: Mitochondrion. Note=In retinoic
acid-treated P19 cells, isoform 4 is found first in the
mitochondria and at later times, as neuronal differentiation
proceeds, in the cytosol.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1;
IsoId=P28661-1; Sequence=Displayed;
Name=2;
IsoId=P28661-2; Sequence=VSP_038308;
Name=3;
IsoId=P28661-3; Sequence=VSP_038313, VSP_038314;
Note=No experimental confirmation available.;
Name=4; Synonyms=Mitochondrial septin, M-septin;
IsoId=P28661-4; Sequence=VSP_038309;
Name=5;
IsoId=P28661-5; Sequence=VSP_038307, VSP_038310, VSP_038313,
VSP_038314;
Note=No experimental confirmation available.;
Name=6;
IsoId=P28661-6; Sequence=VSP_038308, VSP_038311, VSP_038312;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in the brain. Abundant in areas of
high cell density, particularly in the stria terminalis. Isoform 4
is predominantly expressed in embryonic mouse brain and dorsal
root ganglion neurons. {ECO:0000269|PubMed:12581152}.
-!- DEVELOPMENTAL STAGE: Widely expressed in embryos at 7 dpc. Isoform
4 predominantly expressed in the brain at 14 dpc and on postnatal
day 1. {ECO:0000269|PubMed:12581152}.
-!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-
like GTPase superfamily. Septin GTPase family.
{ECO:0000255|PROSITE-ProRule:PRU01056}.
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EMBL; X61452; CAA43692.1; -; mRNA.
EMBL; AB078010; BAC55241.1; -; mRNA.
EMBL; AK133933; BAE21934.1; -; mRNA.
EMBL; AK135143; BAE22437.1; -; mRNA.
EMBL; AK137299; BAE23298.1; -; mRNA.
EMBL; AL596086; CAI35128.2; -; Genomic_DNA.
EMBL; AL596086; CAI35129.1; -; Genomic_DNA.
EMBL; AL596086; CAI35132.1; -; Genomic_DNA.
EMBL; AL596086; CAI35133.1; -; Genomic_DNA.
EMBL; AL596086; CAI35134.1; -; Genomic_DNA.
EMBL; CU406988; CAQ52271.1; -; Genomic_DNA.
EMBL; CU406988; CAQ52272.1; -; Genomic_DNA.
EMBL; CU406988; CAQ52274.1; -; Genomic_DNA.
EMBL; CU406988; CAQ52275.1; -; Genomic_DNA.
EMBL; CU406988; CAQ52276.1; -; Genomic_DNA.
EMBL; CH466556; EDL15822.1; -; Genomic_DNA.
EMBL; BC055101; AAH55101.1; -; mRNA.
CCDS; CCDS25213.1; -. [P28661-1]
CCDS; CCDS70275.1; -. [P28661-5]
CCDS; CCDS70276.1; -. [P28661-3]
CCDS; CCDS70277.1; -. [P28661-4]
PIR; S16867; S16867.
RefSeq; NP_001271321.1; NM_001284392.1. [P28661-4]
RefSeq; NP_001271323.1; NM_001284394.1. [P28661-3]
RefSeq; NP_001271327.1; NM_001284398.1. [P28661-5]
RefSeq; NP_035259.1; NM_011129.2. [P28661-1]
RefSeq; XP_006532561.1; XM_006532498.3. [P28661-2]
UniGene; Mm.2214; -.
ProteinModelPortal; P28661; -.
SMR; P28661; -.
BioGrid; 202286; 5.
IntAct; P28661; 3.
MINT; P28661; -.
STRING; 10090.ENSMUSP00000018544; -.
iPTMnet; P28661; -.
PhosphoSitePlus; P28661; -.
MaxQB; P28661; -.
PaxDb; P28661; -.
PeptideAtlas; P28661; -.
PRIDE; P28661; -.
DNASU; 18952; -.
Ensembl; ENSMUST00000018544; ENSMUSP00000018544; ENSMUSG00000020486. [P28661-1]
Ensembl; ENSMUST00000063156; ENSMUSP00000060127; ENSMUSG00000020486. [P28661-4]
Ensembl; ENSMUST00000107960; ENSMUSP00000103594; ENSMUSG00000020486. [P28661-3]
Ensembl; ENSMUST00000107962; ENSMUSP00000103596; ENSMUSG00000020486. [P28661-2]
Ensembl; ENSMUST00000122067; ENSMUSP00000112960; ENSMUSG00000020486. [P28661-5]
GeneID; 18952; -.
KEGG; mmu:18952; -.
UCSC; uc007kts.2; mouse. [P28661-6]
UCSC; uc007ktu.2; mouse. [P28661-5]
UCSC; uc007ktw.2; mouse. [P28661-1]
UCSC; uc007ktx.2; mouse. [P28661-3]
UCSC; uc007kty.2; mouse. [P28661-4]
CTD; 5414; -.
MGI; MGI:1270156; Sept4.
eggNOG; KOG2655; Eukaryota.
eggNOG; COG5019; LUCA.
GeneTree; ENSGT00910000144020; -.
HOVERGEN; HBG065093; -.
InParanoid; P28661; -.
KO; K16943; -.
OMA; FSGNESC; -.
OrthoDB; EOG091G07TS; -.
PhylomeDB; P28661; -.
TreeFam; TF101079; -.
ChiTaRS; Sept4; mouse.
PRO; PR:P28661; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000020486; -.
CleanEx; MM_SEPT4; -.
ExpressionAtlas; P28661; baseline and differential.
Genevisible; P28661; MM.
GO; GO:0042995; C:cell projection; IDA:MGI.
GO; GO:0005739; C:mitochondrion; HDA:MGI.
GO; GO:0031514; C:motile cilium; IMP:MGI.
GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0031105; C:septin complex; ISO:MGI.
GO; GO:0097227; C:sperm annulus; IDA:MGI.
GO; GO:0036126; C:sperm flagellum; IDA:MGI.
GO; GO:0005525; F:GTP binding; ISO:MGI.
GO; GO:0003924; F:GTPase activity; ISO:MGI.
GO; GO:0000287; F:magnesium ion binding; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0007420; P:brain development; IMP:MGI.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; ISO:MGI.
GO; GO:0031398; P:positive regulation of protein ubiquitination; ISO:MGI.
GO; GO:0051260; P:protein homooligomerization; ISO:MGI.
GO; GO:0048240; P:sperm capacitation; IMP:MGI.
GO; GO:0030382; P:sperm mitochondrion organization; IMP:MGI.
GO; GO:0007286; P:spermatid development; IMP:MGI.
CDD; cd01850; CDC_Septin; 1.
InterPro; IPR030379; G_SEPTIN_dom.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR016491; Septin.
InterPro; IPR030643; Septin4.
PANTHER; PTHR18884:SF71; PTHR18884:SF71; 1.
Pfam; PF00735; Septin; 1.
PIRSF; PIRSF006698; Septin; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS51719; G_SEPTIN; 1.
1: Evidence at protein level;
Alternative splicing; Cell cycle; Cell division; Cell projection;
Cilium; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton;
Differentiation; Direct protein sequencing; Flagellum; GTP-binding;
Mitochondrion; Nucleotide-binding; Phosphoprotein; Reference proteome;
Spermatogenesis.
CHAIN 1 478 Septin-4.
/FTId=PRO_0000173520.
DOMAIN 141 414 Septin-type G. {ECO:0000255|PROSITE-
ProRule:PRU01056}.
NP_BIND 151 158 GTP. {ECO:0000250}.
NP_BIND 290 298 GTP. {ECO:0000250}.
REGION 151 158 G1 motif. {ECO:0000255|PROSITE-
ProRule:PRU01056}.
REGION 208 211 G3 motif. {ECO:0000255|PROSITE-
ProRule:PRU01056}.
REGION 289 292 G4 motif. {ECO:0000255|PROSITE-
ProRule:PRU01056}.
COILED 447 478 {ECO:0000255}.
BINDING 185 185 GTP. {ECO:0000250}.
BINDING 211 211 GTP; via amide nitrogen. {ECO:0000250}.
BINDING 348 348 GTP; via amide nitrogen and carbonyl
oxygen. {ECO:0000250}.
BINDING 363 363 GTP. {ECO:0000250}.
MOD_RES 28 28 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 29 29 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 68 68 Phosphoserine.
{ECO:0000244|PubMed:16452087,
ECO:0000244|PubMed:21183079}.
MOD_RES 117 117 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 118 118 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 325 325 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 432 432 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 434 434 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
VAR_SEQ 1 118 Missing (in isoform 5).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_038307.
VAR_SEQ 1 20 MDHSLGWQGNSVPEDGTEAG -> M (in isoform 2
and isoform 6).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_038308.
VAR_SEQ 21 119 Missing (in isoform 4).
{ECO:0000303|PubMed:12581152}.
/FTId=VSP_038309.
VAR_SEQ 119 119 E -> M (in isoform 5).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_038310.
VAR_SEQ 221 223 CWK -> WYV (in isoform 6).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_038311.
VAR_SEQ 224 478 Missing (in isoform 6).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_038312.
VAR_SEQ 426 431 NKLTRE -> KDRSRN (in isoform 3 and
isoform 5). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_038313.
VAR_SEQ 432 478 Missing (in isoform 3 and isoform 5).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_038314.
CONFLICT 394 394 D -> N (in Ref. 3; BAE21934).
{ECO:0000305}.
SEQUENCE 478 AA; 54936 MW; 36655DE54A6C4908 CRC64;
MDHSLGWQGN SVPEDGTEAG IKHFLEDSSD DAELSKFVKD FPGSEPYHSA ESKTRVARPQ
ILEPRPQSPD LCDDDVEFRG SLWPQPSDSQ QYFSAPAPLS PSSRPRSPWG KLDPYDSSED
DKEYVGFATL PNQVHRKSVK KGFDFTLMVA GESGLGKSTL VNSLFLTDLY RDRKLLGAEE
RIMQTVEITK HAVDIEEKGV RLRLTIVDTP GFGDAVNNTE CWKPVAEYID QQFEQYFRDE
SGLNRKNIQD NRVHCCLYFI SPFGHGLRPL DVEFMKALHQ RVNIVPILAK ADTLTPPEVD
RKKCKIREEI EHFGIKIYQF PDCDSDEDED FKLQDQALKE SIPFAVIGSN TVVEARGRRV
RGRLYPWGIV EVENPGHCDF VKLRTMLVRT HMQDLKDVTR ETHYENYRAQ CIQSMTRLVV
KERNRNKLTR ESGTDFPIPA VPPGTDPETE KLIREKDEEL RRMQEMLHKI QRQMKETH


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U2256h CLIA CDCrel-1,Cell division control-related protein 1,Homo sapiens,Human,Peanut-like protein 1,PNUTL1,SEPT5,Septin-5 96T
U2256h CLIA kit CDCrel-1,Cell division control-related protein 1,Homo sapiens,Human,Peanut-like protein 1,PNUTL1,SEPT5,Septin-5 96T
E2256h ELISA kit CDCrel-1,Cell division control-related protein 1,Homo sapiens,Human,Peanut-like protein 1,PNUTL1,SEPT5,Septin-5 96T
AS09 566 Antibody: Peanut protein, Immunogen: Arachis hypogaea protein extract, Host: hen, polyclonal, Confirmed reactivity: peanut proteins 100
R6021 Peanut ELISA Kit (48 wells), Peanut protein detection by ELISA (LOD <0.5ppm; range 1-30ppm peanut)
R6020 Peanut ELISA Kit (96 wells), Peanut protein detection by ELISA (LOD <0.5ppm; range 1-30ppm peanut)
R6021 Peanut ELISA Kit Peanut protein detection by ELISA (LOD <0.5ppm; range 1-30ppm peanut) 48 wells
R6020 Peanut ELISA Kit Peanut protein detection by ELISA (LOD <0.5ppm; range 1-30ppm peanut) 96 wells
20-272-190217 ARTS - Mouse monoclonal [ARTS51] to ARTS; Peanut-like protein 2; Brain protein H5; Cell division control-related protein 2; hCDCREL-2; Bradeion beta; CE5B3 beta; Cerebral protein 7 Monoclonal 0.05 ml
18-272-195086 ARTS - Rabbit polyclonal to ARTS; Peanut-like protein 2; Brain protein H5; Cell division control-related protein 2; hCDCREL-2; Bradeion beta; CE5B3 beta; Cerebral protein 7 Polyclonal 0.05 ml
EIAAB10913 Brain specific protein 4,Brain-specific gene 4 protein,Bsg4,Bsp4,DENN domain-containing protein 4B,Dennd4b,Kiaa0476,Mouse,Mus musculus
18-003-42046 POU domain. class 6. transcription factor 1 - mPOU homeobox protein; Brain-specific homeobox_POU domain protein 5; Brain-5; Brn-5 protein Polyclonal 0.05 mg Aff Pur


 

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