Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Dynamin (EC 3.6.5.5) (Protein shibire) (dDyn)

 DYN_DROME               Reviewed;         877 AA.
P27619; Q0KHS4; Q9VXM2;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
28-FEB-2003, sequence version 2.
30-AUG-2017, entry version 186.
RecName: Full=Dynamin;
EC=3.6.5.5;
AltName: Full=Protein shibire;
AltName: Full=dDyn;
Name=shi; ORFNames=CG18102;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
STRAIN=Canton-S; TISSUE=Head;
PubMed=1828536; DOI=10.1038/351583a0;
Chen M.S., Obar R.A., Schroeder C.C., Austin T.W., Poodry C.A.,
Wadsworth S.C., Vallee R.B.;
"Multiple forms of dynamin are encoded by shibire, a Drosophila gene
involved in endocytosis.";
Nature 351:583-586(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND MUTAGENESIS OF
GLY-141 AND GLY-268.
STRAIN=Oregon-R;
PubMed=1674590; DOI=10.1038/351411a0;
van der Bliek A.M., Meyerowitz E.M.;
"Dynamin-like protein encoded by the Drosophila shibire gene
associated with vesicular traffic.";
Nature 351:411-414(1991).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=Berkeley; TISSUE=Embryo;
Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W.,
Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E.,
George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G.,
Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S.,
Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M.,
Celniker S.E.;
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-756; SER-764 AND
SER-767, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
-!- FUNCTION: Microtubule-associated force-producing protein which is
involved in the production of microtubule bundles and which is
able to bind and hydrolyze GTP. Implicated in endocytic protein
sorting.
-!- CATALYTIC ACTIVITY: GTP + H(2)O = GDP + phosphate.
-!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton.
Note=Microtubule-associated.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=4, D, F;
IsoId=P27619-1; Sequence=Displayed;
Name=2; Synonyms=3, A, B;
IsoId=P27619-2; Sequence=VSP_001330, VSP_001331;
-!- MISCELLANEOUS: Shibire mutation is the cause of temperature-
sensitive paralysis. This is believed to be due to a reversible
block of endocytosis, which prevents membrane cycling and thus
depletes synaptic vesicles.
-!- MISCELLANEOUS: 'Shibire' means 'paralyzed' in Japanese.
-!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
superfamily. Dynamin/Fzo/YdjA family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA42061.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA. There is a 6 amino acid insertion at position 634 due to a chimera of DNA from chromosome arms X and 3L.; Evidence={ECO:0000305};
Sequence=CAA42067.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA. There is a 6 amino acid insertion at position 634 due to a chimera of DNA from chromosome arms X and 3L.; Evidence={ECO:0000305};
Sequence=CAA42068.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA. There is a 6 amino acid insertion at position 634 due to a chimera of DNA from chromosome arms X and 3L.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X59448; CAA42067.1; ALT_SEQ; mRNA.
EMBL; X59449; CAA42068.1; ALT_SEQ; mRNA.
EMBL; X59435; CAA42061.1; ALT_SEQ; mRNA.
EMBL; X59436; CAA42062.1; -; mRNA.
EMBL; AE014298; AAF48536.2; -; Genomic_DNA.
EMBL; AE014298; AAS65368.1; -; Genomic_DNA.
EMBL; BT010049; AAQ22518.1; -; mRNA.
PIR; S15413; S15413.
PIR; S16130; S16130.
PIR; S17974; S17974.
PIR; S17975; S17975.
PIR; S34399; S34399.
RefSeq; NP_001036278.1; NM_001042813.2. [P27619-2]
RefSeq; NP_001036279.1; NM_001042814.2. [P27619-2]
RefSeq; NP_001162766.1; NM_001169295.1. [P27619-1]
RefSeq; NP_001162768.1; NM_001169297.2.
RefSeq; NP_524853.2; NM_080114.4. [P27619-2]
RefSeq; NP_727910.1; NM_167470.3. [P27619-1]
RefSeq; NP_727911.1; NM_167471.5. [P27619-2]
RefSeq; NP_996465.1; NM_206742.1. [P27619-1]
RefSeq; NP_996466.1; NM_206743.2. [P27619-1]
RefSeq; NP_996467.1; NM_206744.3. [P27619-2]
RefSeq; NP_996468.1; NM_206745.3. [P27619-2]
UniGene; Dm.3444; -.
ProteinModelPortal; P27619; -.
SMR; P27619; -.
BioGrid; 69991; 16.
DIP; DIP-17621N; -.
IntAct; P27619; 4.
MINT; MINT-806233; -.
STRING; 7227.FBpp0305866; -.
iPTMnet; P27619; -.
PaxDb; P27619; -.
PRIDE; P27619; -.
EnsemblMetazoa; FBtr0074118; FBpp0073928; FBgn0003392. [P27619-2]
EnsemblMetazoa; FBtr0074119; FBpp0073929; FBgn0003392. [P27619-2]
EnsemblMetazoa; FBtr0074121; FBpp0089278; FBgn0003392. [P27619-2]
EnsemblMetazoa; FBtr0074122; FBpp0089279; FBgn0003392. [P27619-2]
EnsemblMetazoa; FBtr0074123; FBpp0089280; FBgn0003392. [P27619-1]
EnsemblMetazoa; FBtr0074124; FBpp0089277; FBgn0003392. [P27619-1]
EnsemblMetazoa; FBtr0111036; FBpp0110335; FBgn0003392. [P27619-2]
EnsemblMetazoa; FBtr0111037; FBpp0110336; FBgn0003392. [P27619-2]
EnsemblMetazoa; FBtr0301594; FBpp0290809; FBgn0003392. [P27619-1]
EnsemblMetazoa; FBtr0301595; FBpp0290810; FBgn0003392. [P27619-1]
GeneID; 45928; -.
KEGG; dme:Dmel_CG18102; -.
UCSC; CG18102-RA; d. melanogaster. [P27619-1]
CTD; 45928; -.
FlyBase; FBgn0003392; shi.
eggNOG; KOG0446; Eukaryota.
eggNOG; COG0699; LUCA.
GeneTree; ENSGT00760000119213; -.
InParanoid; P27619; -.
KO; K01528; -.
OrthoDB; EOG091G0EIQ; -.
PhylomeDB; P27619; -.
BRENDA; 3.6.5.5; 1994.
Reactome; R-DME-196025; Formation of annular gap junctions.
Reactome; R-DME-203641; NOSTRIN mediated eNOS trafficking.
Reactome; R-DME-8856828; Clathrin-mediated endocytosis.
ChiTaRS; shi; fly.
GenomeRNAi; 45928; -.
PRO; PR:P27619; -.
Proteomes; UP000000803; Chromosome X.
Bgee; FBgn0003392; -.
ExpressionAtlas; P27619; differential.
Genevisible; P27619; DM.
GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0031966; C:mitochondrial membrane; IBA:GO_Central.
GO; GO:0072686; C:mitotic spindle; IDA:FlyBase.
GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
GO; GO:0098793; C:presynapse; IEA:GOC.
GO; GO:0070864; C:sperm individualization complex; IDA:FlyBase.
GO; GO:0045202; C:synapse; IMP:FlyBase.
GO; GO:0003779; F:actin binding; IDA:FlyBase.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
GO; GO:0008017; F:microtubule binding; IDA:FlyBase.
GO; GO:0034334; P:adherens junction maintenance; IMP:FlyBase.
GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
GO; GO:0007349; P:cellularization; IMP:FlyBase.
GO; GO:0007268; P:chemical synaptic transmission; IMP:FlyBase.
GO; GO:0072583; P:clathrin-dependent endocytosis; IMP:FlyBase.
GO; GO:0061883; P:clathrin-dependent endocytosis involved in vitellogenesis; IMP:FlyBase.
GO; GO:0046667; P:compound eye retinal cell programmed cell death; IMP:FlyBase.
GO; GO:0001661; P:conditioned taste aversion; IMP:FlyBase.
GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:FlyBase.
GO; GO:0046843; P:dorsal appendage formation; IMP:FlyBase.
GO; GO:0003374; P:dynamin family protein polymerization involved in mitochondrial fission; IBA:GO_Central.
GO; GO:0006897; P:endocytosis; IDA:FlyBase.
GO; GO:0007427; P:epithelial cell migration, open tracheal system; IMP:FlyBase.
GO; GO:0060429; P:epithelium development; IMP:FlyBase.
GO; GO:0030198; P:extracellular matrix organization; IMP:FlyBase.
GO; GO:0007293; P:germarium-derived egg chamber formation; IMP:FlyBase.
GO; GO:0030536; P:larval feeding behavior; IMP:FlyBase.
GO; GO:0007612; P:learning; IMP:FlyBase.
GO; GO:0090148; P:membrane fission; IMP:FlyBase.
GO; GO:0061025; P:membrane fusion; IBA:GO_Central.
GO; GO:0007613; P:memory; IMP:FlyBase.
GO; GO:0000266; P:mitochondrial fission; IBA:GO_Central.
GO; GO:1903475; P:mitotic actomyosin contractile ring assembly; IMP:FlyBase.
GO; GO:0001738; P:morphogenesis of a polarized epithelium; IMP:FlyBase.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:UniProtKB.
GO; GO:0008355; P:olfactory learning; IDA:FlyBase.
GO; GO:0007424; P:open tracheal system development; IMP:FlyBase.
GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase.
GO; GO:0030838; P:positive regulation of actin filament polymerization; IMP:UniProtKB.
GO; GO:0045747; P:positive regulation of Notch signaling pathway; IMP:FlyBase.
GO; GO:0007637; P:proboscis extension reflex; IMP:FlyBase.
GO; GO:0072659; P:protein localization to plasma membrane; IMP:FlyBase.
GO; GO:0006898; P:receptor-mediated endocytosis; NAS:FlyBase.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; IGI:FlyBase.
GO; GO:0032970; P:regulation of actin filament-based process; IGI:FlyBase.
GO; GO:0040008; P:regulation of growth; IMP:FlyBase.
GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; IMP:FlyBase.
GO; GO:0050803; P:regulation of synapse structure or activity; IMP:FlyBase.
GO; GO:0035152; P:regulation of tube architecture, open tracheal system; IMP:FlyBase.
GO; GO:0007435; P:salivary gland morphogenesis; IMP:FlyBase.
GO; GO:0007614; P:short-term memory; IMP:FlyBase.
GO; GO:0007291; P:sperm individualization; IMP:FlyBase.
GO; GO:0016185; P:synaptic vesicle budding from presynaptic endocytic zone membrane; IMP:FlyBase.
GO; GO:0048488; P:synaptic vesicle endocytosis; IDA:FlyBase.
GO; GO:0048499; P:synaptic vesicle membrane organization; IMP:FlyBase.
GO; GO:0036465; P:synaptic vesicle recycling; IMP:FlyBase.
GO; GO:0048489; P:synaptic vesicle transport; IDA:FlyBase.
GO; GO:0035186; P:syncytial blastoderm mitotic cell cycle; IMP:FlyBase.
GO; GO:0016192; P:vesicle-mediated transport; TAS:FlyBase.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR027188; DNM2.
InterPro; IPR000375; Dynamin_central.
InterPro; IPR001401; Dynamin_GTPase.
InterPro; IPR019762; Dynamin_GTPase_CS.
InterPro; IPR022812; Dynamin_SF.
InterPro; IPR030381; G_DYNAMIN_dom.
InterPro; IPR003130; GED.
InterPro; IPR020850; GED_dom.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR011993; PH_dom-like.
InterPro; IPR001849; PH_domain.
PANTHER; PTHR11566; PTHR11566; 1.
PANTHER; PTHR11566:SF94; PTHR11566:SF94; 1.
Pfam; PF01031; Dynamin_M; 1.
Pfam; PF00350; Dynamin_N; 1.
Pfam; PF02212; GED; 1.
Pfam; PF00169; PH; 1.
PRINTS; PR00195; DYNAMIN.
SMART; SM00053; DYNc; 1.
SMART; SM00302; GED; 1.
SMART; SM00233; PH; 1.
SUPFAM; SSF50729; SSF50729; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS00410; G_DYNAMIN_1; 1.
PROSITE; PS51718; G_DYNAMIN_2; 1.
PROSITE; PS51388; GED; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm; Cytoskeleton;
Endocytosis; GTP-binding; Hydrolase; Microtubule; Motor protein;
Nucleotide-binding; Phosphoprotein; Reference proteome.
CHAIN 1 877 Dynamin.
/FTId=PRO_0000206576.
DOMAIN 23 289 Dynamin-type G.
DOMAIN 513 621 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 650 741 GED. {ECO:0000255|PROSITE-
ProRule:PRU00720}.
NP_BIND 33 41 GTP. {ECO:0000250|UniProtKB:O00429}.
NP_BIND 200 206 GTP. {ECO:0000250|UniProtKB:O00429}.
NP_BIND 231 234 GTP. {ECO:0000250|UniProtKB:O00429}.
COMPBIAS 744 827 Pro-rich.
MOD_RES 756 756 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 764 764 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 767 767 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
VAR_SEQ 830 830 V -> R (in isoform 2).
{ECO:0000303|PubMed:1674590,
ECO:0000303|PubMed:1828536}.
/FTId=VSP_001330.
VAR_SEQ 831 877 Missing (in isoform 2).
{ECO:0000303|PubMed:1674590,
ECO:0000303|PubMed:1828536}.
/FTId=VSP_001331.
MUTAGEN 141 141 G->S: In allele shi-TS2; temperature
sensitive larval and adult paralysis.
{ECO:0000269|PubMed:1674590}.
MUTAGEN 268 268 G->D: In allele shi-TS1; temperature
sensitive larval and adult paralysis.
{ECO:0000269|PubMed:1674590}.
CONFLICT 594 594 K -> R (in Ref. 1; CAA42067/CAA42068).
{ECO:0000305}.
SEQUENCE 877 AA; 97809 MW; 5B85F96491490B14 CRC64;
MDSLITIVNK LQDAFTSLGV HMQLDLPQIA VVGGQSAGKS SVLENFVGKD FLPRGSGIVT
RRPLILQLIN GVTEYGEFLH IKGKKFSSFD EIRKEIEDET DRVTGSNKGI SNIPINLRVY
SPHVLNLTLI DLPGLTKVAI GDQPVDIEQQ IKQMIFQFIR KETCLILAVT PANTDLANSD
ALKLAKEVDP QGVRTIGVIT KLDLMDEGTD ARDILENKLL PLRRGYIGVV NRSQKDIEGR
KDIHQALAAE RKFFLSHPSY RHMADRLGTP YLQRVLNQQL TNHIRDTLPG LRDKLQKQML
TLEKEVEEFK HFQPGDASIK TKAMLQMIQQ LQSDFERTIE GSGSALVNTN ELSGGAKINR
IFHERLRFEI VKMACDEKEL RREISFAIRN IHGIRVGLFT PDMAFEAIVK RQIALLKEPV
IKCVDLVVQE LSVVVRMCTA KMSRYPRLRE ETERIITTHV RQREHSCKEQ ILLLIDFELA
YMNTNHEDFI GFANAQNKSE NANKTGTRQL GNQVIRKGHM VIQNLGIMKG GSRPYWFVLT
SESISWYKDE DEKEKKFMLP LDGLKLRDIE QGFMSMSRRV TFALFSPDGR NVYKDYKQLE
LSCETVEDVE SWKASFLRAG VYPEKQETQE NGDESASEES SSDPQLERQV ETIRNLVDSY
MKIVTKTTRD MVPKAIMMLI INNAKDFING ELLAHLYASG DQAQMMEESA ESATRREEML
RMYRACKDAL QIIGDVSMAT VSSPLPPPVK NDWLPSGLDN PRLSPPSPGG VRGKPGPPAQ
SSLGGRNPPL PPSTGRPAPA IPNRPGGGAP PLPGGRPGGS LPPPMLPSRV SGAVGGAIVQ
QSGANRYVPE SMRGQVNQAV GQAAINELSN AFSSRFK


Related products :

Catalog number Product name Quantity
EIAAB11600 DLP1,DNM1L,Dnm1p_Vps1p-like protein,DRP1,DVLP,Dymple,Dynamin family member proline-rich carboxyl-terminal domain less,Dynamin-1-like protein,Dynamin-like protein,Dynamin-like protein 4,Dynamin-like pr
32-146 Dynamin-1 (Dyn1), with 864-amino acid protein (about 95kDa), belongs to the dynamin family. Dynamin-1 (neuron-specific), dynamin-2 (ubiquitously expressed), and dynamin-3 (expressed only in the testis 0.1 mL
32-147 Dynamin-2 (Dyn2), with 870-amino acid protein (about 95kDa), belongs to the dynamin family. Dynamin-1 (neuron-specific), dynamin-2 (ubiquitously expressed), and dynamin-3 (expressed only in the testis 0.1 mL
EIAAB11598 Dnm1l,Drp1,Dymple,Dynamin family member proline-rich carboxyl-terminal domain less,Dynamin-1-like protein,Dynamin-related protein 1,Mouse,Mus musculus
EIAAB29675 Dynamin PRD-interacting protein,Dynamin proline-rich domain-interacting protein,Pacsin1,Protein kinase C and casein kinase substrate in neurons protein 1,Rat,Rattus norvegicus,SdpI,Synaptic, dynamin-a
U1962r CLIA kit B-dynamin,D100,Dnm,Dnm1,Dynamin, brain,Dynamin-1,Rat,Rattus norvegicus 96T
E1962r ELISA kit B-dynamin,D100,Dnm,Dnm1,Dynamin, brain,Dynamin-1,Rat,Rattus norvegicus 96T
EIAAB12198 DNM3,Dynamin, testicular,Dynamin-3,Homo sapiens,Human,KIAA0820,T-dynamin
U1962r CLIA B-dynamin,D100,Dnm,Dnm1,Dynamin, brain,Dynamin-1,Rat,Rattus norvegicus 96T
E1962r ELISA B-dynamin,D100,Dnm,Dnm1,Dynamin, brain,Dynamin-1,Rat,Rattus norvegicus 96T
EIAAB11601 Dlp1,Dnm1l,Dynamin-1-like protein,Dynamin-like protein,Rat,Rattus norvegicus
EIAAB12197 Dnm3,Dyn3,Dynamin, testicular,Dynamin-3,Rat,Rattus norvegicus,T-dynamin
bs-0574P Peptides: Dynamin 2(Anti-Human Dynamin-2 ) Protein Length:12-25 amino acids. 200ug lyophilized
SHI-101AP Rabbit Anti-Shibire Antibody 100
P-SHI Rabbit Shibire Antibody Blocking Peptide 100
PC-SHI Rabbit Shibire Antibody Positive Control 100
SHI-101AP Rabbit Affinity Purified Shibire Antibody 250
E1164m ELISA kit Dnm2,Dyn2,Dynamin UDNM,Dynamin-2,Mouse,Mus musculus 96T
U1164m CLIA Dnm2,Dyn2,Dynamin UDNM,Dynamin-2,Mouse,Mus musculus 96T
E1164m ELISA Dnm2,Dyn2,Dynamin UDNM,Dynamin-2,Mouse,Mus musculus 96T
Mab-606045 Monoclonal Antibodies: Dynamin-1; Specificity: Dynamin-1 ; Application: WB, IHC, Elisa 0.1ml
Mab-607011 Monoclonal Antibodies: Dynamin-2; Specificity: Dynamin-2 ; Application: WB, IHC, Elisa 0.1ml
LF-MA10088 anti-Dynamin 2 (6C9), Mouse monoclonal to Dynamin 2, Isotype IgG1, Host Mouse 100 ug
SHI-FITC Rabbit FITC-Conjugated Shibire Antibody 5 Applications
LF-PA41410 anti-Dynamin 1, Rabbit polyclonal to Dynamin 1, Isotype IgG, Host Rabbit 100 ul


 

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