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Anillin (Actin-binding protein 8) (ABP8) (Protein scraps)

 ANLN_DROME              Reviewed;        1239 AA.
Q9V4P1; Q24240; Q8MKN2; Q8T067;
21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 3.
18-JUL-2018, entry version 137.
RecName: Full=Anillin;
AltName: Full=Actin-binding protein 8;
Short=ABP8;
AltName: Full=Protein scraps;
Name=scra; Synonyms=ani; ORFNames=CG2092;
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] (ISOFORM A), INTERACTION WITH ACTIN,
SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
TISSUE=Embryo;
PubMed=7559773; DOI=10.1083/jcb.131.1.165;
Field C.M., Alberts B.M.;
"Anillin, a contractile ring protein that cycles from the nucleus to
the cell cortex.";
J. Cell Biol. 131:165-178(1995).
[2]
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).
[3]
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=9013326;
Hime G.R., Brill J.A., Fuller M.T.;
"Assembly of ring canals in the male germ line from structural
components of the contractile ring.";
J. Cell Sci. 109:2779-2788(1996).
[6]
SUBCELLULAR LOCATION.
PubMed=9477328;
Rothwell W.F., Fogarty P., Field C.M., Sullivan W.;
"Nuclear-fallout, a Drosophila protein that cycles from the cytoplasm
to the centrosomes, regulates cortical microfilament organization.";
Development 125:1295-1303(1998).
[7]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=9655801;
de Cuevas M., Spradling A.C.;
"Morphogenesis of the Drosophila fusome and its implications for
oocyte specification.";
Development 125:2781-2789(1998).
[8]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=10381388;
Giansanti M.G., Bonaccorsi S., Gatti M.;
"The role of anillin in meiotic cytokinesis of Drosophila males.";
J. Cell Sci. 112:2323-2334(1999).
[9]
SUBCELLULAR LOCATION.
PubMed=10444383;
Rothwell W.F., Zhang C.X., Zelano C., Hsieh T.-S., Sullivan W.;
"The Drosophila centrosomal protein Nuf is required for recruiting
Dah, a membrane associated protein, to furrows in the early embryo.";
J. Cell Sci. 112:2885-2893(1999).
[10]
DEVELOPMENTAL STAGE.
PubMed=10751177;
Afshar K., Stuart B., Wasserman S.A.;
"Functional analysis of the Drosophila diaphanous FH protein in early
embryonic development.";
Development 127:1887-1897(2000).
[11]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12134082; DOI=10.1091/mbc.01-12-0589;
Somma M.P., Fasulo B., Cenci G., Cundari E., Gatti M.;
"Molecular dissection of cytokinesis by RNA interference in Drosophila
cultured cells.";
Mol. Biol. Cell 13:2448-2460(2002).
[12]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=12538517; DOI=10.1242/dev.00315;
Mathe E., Inoue Y.H., Palframan W., Brown G., Glover D.M.;
"Orbit/Mast, the CLASP orthologue of Drosophila, is required for
asymmetric stem cell and cystocyte divisions and development of the
polarised microtubule network that interconnects oocyte and nurse
cells during oogenesis.";
Development 130:901-915(2003).
[13]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15380073; DOI=10.1016/j.cub.2004.08.063;
Echard A., Hickson G.R.X., Foley E., O'Farrell P.H.;
"Terminal cytokinesis events uncovered after an RNAi screen.";
Curr. Biol. 14:1685-1693(2004).
[14]
FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
PubMed=14736750; DOI=10.1242/dev.00989;
Thomas J.H., Wieschaus E.;
"src64 and tec29 are required for microfilament contraction during
Drosophila cellularization.";
Development 131:863-871(2004).
[15]
SUBCELLULAR LOCATION.
PubMed=15240570; DOI=10.1083/jcb.200402157;
D'Avino P.P., Savoian M.S., Glover D.M.;
"Mutations in sticky lead to defective organization of the contractile
ring during cytokinesis and are enhanced by Rho and suppressed by
Rac.";
J. Cell Biol. 166:61-71(2004).
[16]
SUBCELLULAR LOCATION.
PubMed=15004238; DOI=10.1091/mbc.E03-08-0603;
Giansanti M.G., Farkas R.M., Bonaccorsi S., Lindsley D.L.,
Wakimoto B.T., Fuller M.T., Gatti M.;
"Genetic dissection of meiotic cytokinesis in Drosophila males.";
Mol. Biol. Cell 15:2509-2522(2004).
[17]
SUBCELLULAR LOCATION.
PubMed=15371536; DOI=10.1091/mbc.E04-06-0536;
Naim V., Imarisio S., Di Cunto F., Gatti M., Bonaccorsi S.;
"Drosophila citron kinase is required for the final steps of
cytokinesis.";
Mol. Biol. Cell 15:5053-5063(2004).
[18]
FUNCTION, SUBCELLULAR LOCATION, AND CHARACTERIZATION OF MUTANTS
ILE-549; SER-1107; ILE-1114; GLU-1121 AND SER-1143.
PubMed=15930114; DOI=10.1242/dev.01843;
Field C.M., Coughlin M., Doberstein S., Marty T., Sullivan W.;
"Characterization of anillin mutants reveals essential roles in septin
localization and plasma membrane integrity.";
Development 132:2849-2860(2005).
[19]
SUBCELLULAR LOCATION.
PubMed=16280552; DOI=10.1242/jcs.02652;
Zavortink M., Contreras N., Addy T., Bejsovec A., Saint R.;
"Tum/RacGAP50C provides a critical link between anaphase microtubules
and the assembly of the contractile ring in Drosophila melanogaster.";
J. Cell Sci. 118:5381-5392(2005).
[20]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15496454; DOI=10.1091/mbc.E04-08-0758;
Straight A.F., Field C.M., Mitchison T.J.;
"Anillin binds nonmuscle myosin II and regulates the contractile
ring.";
Mol. Biol. Cell 16:193-201(2005).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-712; THR-740; SER-744;
SER-754 AND THR-831, 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: Required for cytokinesis. Essential for the structural
integrity of the cleavage furrow and for completion of cleavage
furrow ingression and proper formation of the midbody. Required
during cellularization of syncytial embryos for the proper
formation and function of the furrow canals, the stable inward
folds of the plasma membrane which separate the peripheral nuclei.
Also required for the formation of the pole cells, the progenitors
of the adult germline which are formed by cytokinesis of the
cytoplasmic buds at the posterior pole of the syncytial embryo.
Essential for embryonic viability. {ECO:0000269|PubMed:12134082,
ECO:0000269|PubMed:14736750, ECO:0000269|PubMed:15380073,
ECO:0000269|PubMed:15496454, ECO:0000269|PubMed:15930114}.
-!- SUBUNIT: Interacts with and bundles F-actin.
{ECO:0000269|PubMed:7559773}.
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton. Cytoplasm,
cell cortex. Note=Mainly found in the nucleus during interphase.
Colocalizes with cortical F-actin upon nuclear envelope breakdown
in mitosis and subsequently concentrates in the area of the
prospective contractile ring in anaphase. This pattern persists
until telophase, when the protein becomes concentrated in the
midbody. Accumulates in the nucleus of newly divided cells in a
diffuse staining pattern, thereby restarting the cycle.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=B;
IsoId=Q9V4P1-1; Sequence=Displayed;
Name=A;
IsoId=Q9V4P1-2; Sequence=VSP_017618;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Accumulates in the ring canals that
interconnect cells of the germline cysts in males and the ovarian
follicles in females. These structures develop from arrested
contractile rings after a specialized cytokinesis in which the
closing of the invaginating plasma membrane is incomplete. Also
concentrates in the arrested cleavage furrows that initially link
the oocyte to its 15 nurse cells in the early egg chamber and is
subsequently lost from these furrows as germline cell division is
completed. {ECO:0000269|PubMed:10381388,
ECO:0000269|PubMed:12538517, ECO:0000269|PubMed:9013326,
ECO:0000269|PubMed:9655801}.
-!- DEVELOPMENTAL STAGE: Expressed throughout development and at
reduced levels late in embryogenesis. Localizes to the embryonic
cortex and to the metaphase furrows which separate mitotic nuclei
in the syncytial embryo prior to cellularization. Concentrates in
the leading edges of the furrow canals at the onset of
cellularization. {ECO:0000269|PubMed:10751177,
ECO:0000269|PubMed:14736750, ECO:0000269|PubMed:7559773}.
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EMBL; X89858; CAA61954.1; -; mRNA.
EMBL; AE013599; AAF59225.3; -; Genomic_DNA.
EMBL; AE013599; AAM71099.1; -; Genomic_DNA.
EMBL; AY069520; AAL39665.1; -; mRNA.
PIR; A57369; A57369.
RefSeq; NP_724582.1; NM_165543.2. [Q9V4P1-1]
RefSeq; NP_724583.1; NM_165544.2. [Q9V4P1-2]
UniGene; Dm.508; -.
ProteinModelPortal; Q9V4P1; -.
SMR; Q9V4P1; -.
BioGrid; 61572; 32.
IntAct; Q9V4P1; 9.
STRING; 7227.FBpp0087986; -.
iPTMnet; Q9V4P1; -.
PaxDb; Q9V4P1; -.
PRIDE; Q9V4P1; -.
EnsemblMetazoa; FBtr0088911; FBpp0087985; FBgn0261385. [Q9V4P1-2]
EnsemblMetazoa; FBtr0088912; FBpp0087986; FBgn0261385. [Q9V4P1-1]
GeneID; 35696; -.
KEGG; dme:Dmel_CG2092; -.
CTD; 35696; -.
FlyBase; FBgn0261385; scra.
eggNOG; KOG3640; Eukaryota.
eggNOG; ENOG4110J5Z; LUCA.
GeneTree; ENSGT00390000008749; -.
HOGENOM; HOG000270273; -.
InParanoid; Q9V4P1; -.
KO; K18621; -.
OMA; EIQRTSW; -.
OrthoDB; EOG091G01HH; -.
PhylomeDB; Q9V4P1; -.
GenomeRNAi; 35696; -.
PRO; PR:Q9V4P1; -.
Proteomes; UP000000803; Chromosome 2R.
Bgee; FBgn0261385; -.
ExpressionAtlas; Q9V4P1; baseline and differential.
Genevisible; Q9V4P1; DM.
GO; GO:0005826; C:actomyosin contractile ring; IDA:UniProtKB.
GO; GO:0032154; C:cleavage furrow; IDA:FlyBase.
GO; GO:0070938; C:contractile ring; IDA:FlyBase.
GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
GO; GO:0045172; C:germline ring canal; IDA:UniProtKB.
GO; GO:0035323; C:male germline ring canal; IDA:FlyBase.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003779; F:actin binding; IDA:FlyBase.
GO; GO:0051015; F:actin filament binding; IDA:WormBase.
GO; GO:0008017; F:microtubule binding; IDA:FlyBase.
GO; GO:0017022; F:myosin binding; IDA:UniProtKB.
GO; GO:0000915; P:actomyosin contractile ring assembly; IMP:UniProtKB.
GO; GO:0008356; P:asymmetric cell division; IMP:FlyBase.
GO; GO:0007349; P:cellularization; IMP:FlyBase.
GO; GO:0043063; P:intercellular bridge organization; IMP:FlyBase.
GO; GO:0032189; P:maintenance of actomyosin contractile ring localization; IMP:FlyBase.
GO; GO:0030726; P:male germline ring canal formation; IMP:UniProtKB.
GO; GO:0007112; P:male meiosis cytokinesis; IMP:FlyBase.
GO; GO:0000281; P:mitotic cytokinesis; IMP:UniProtKB.
GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
GO; GO:0007009; P:plasma membrane organization; IMP:UniProtKB.
GO; GO:0007279; P:pole cell formation; IMP:UniProtKB.
GO; GO:0008104; P:protein localization; IMP:UniProtKB.
GO; GO:0032465; P:regulation of cytokinesis; IMP:FlyBase.
GO; GO:0007423; P:sensory organ development; IMP:FlyBase.
GO; GO:0045035; P:sensory organ precursor cell division; IMP:FlyBase.
GO; GO:0031106; P:septin ring organization; IMP:FlyBase.
CDD; cd01263; PH_anillin; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR012966; AHD.
InterPro; IPR031970; Anillin_N.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR037840; PH_Anillin.
InterPro; IPR001849; PH_domain.
Pfam; PF08174; Anillin; 1.
Pfam; PF16018; Anillin_N; 1.
Pfam; PF00169; PH; 1.
SMART; SM00233; PH; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
1: Evidence at protein level;
Actin-binding; Alternative splicing; Cell cycle; Cell division;
Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton;
Developmental protein; Differentiation; Meiosis; Mitosis; Nucleus;
Oogenesis; Phosphoprotein; Reference proteome; Spermatogenesis.
CHAIN 1 1239 Anillin.
/FTId=PRO_0000227968.
DOMAIN 1106 1230 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
REGION 126 371 Interaction with and bundling of F-actin.
COILED 834 861 {ECO:0000255}.
MOD_RES 712 712 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 740 740 Phosphothreonine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 744 744 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 754 754 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 831 831 Phosphothreonine.
{ECO:0000269|PubMed:18327897}.
VAR_SEQ 272 298 Missing (in isoform A).
{ECO:0000303|PubMed:7559773}.
/FTId=VSP_017618.
MUTAGEN 549 549 T->I: In allele scra3. Weak maternal
effect allele; abrogates separation of
pole cells.
MUTAGEN 1107 1107 V->S: In alleles scra1; scra3; scra4; and
scra5.
MUTAGEN 1114 1114 T->I: In allele scra5. Strong maternal
effect allele; abrogates cellularization
of syncytial embryos.
MUTAGEN 1121 1121 G->E: In allele scra1. Strong maternal
effect allele; abrogates cellularization
of syncytial embryos.
MUTAGEN 1143 1143 P->S: In allele scra4. Strong maternal
effect allele; abrogates cellularization
of syncytial embryos.
CONFLICT 38 40 Missing (in Ref. 1; CAA61954).
{ECO:0000305}.
CONFLICT 50 60 LAPRSRSPGGQ -> PAP (in Ref. 1; CAA61954).
{ECO:0000305}.
CONFLICT 228 228 L -> P (in Ref. 1; CAA61954).
{ECO:0000305}.
CONFLICT 394 394 G -> A (in Ref. 1; CAA61954).
{ECO:0000305}.
CONFLICT 426 426 M -> V (in Ref. 1; CAA61954).
{ECO:0000305}.
CONFLICT 689 689 D -> E (in Ref. 1; CAA61954).
{ECO:0000305}.
SEQUENCE 1239 AA; 136033 MW; EAA58335AE139A24 CRC64;
MDPFTQHMLE KAEQRSRALG ISNASKFPLV ECSVPSSSAT SASGGDAGVL APRSRSPGGQ
SAASGGGKVV TLGKATLEAS PAKPLRHYTA VNKENLDMGI EINITTDKPI GVQVEIQEQE
VTDDEEQAEG GALNPLLEAE PVNQPLARLR DTSRSRLQRM GALYSNTDDL SSPIHRTEGQ
FHVTTGEEED CGNRSSRQPK QRLGKLAALA DTINQWEDDT SHHEVHRLLE APPPKPHLSS
RRAEKGPAPL PPKKDEVDEA SRTKQLKWDP KVLSSLEAQG FQRRESSTIK HTYDYAKQEE
AAPASKVEDA VLTAKPPVPQ KSTTVSQVAK NFASSAPAPK PAPAPAVSVK SGLVSGRAAL
FENKGTGGQS QGLRNQKDPC ELSLKERMKL FETGNNKAML PMAPIGSAPS ITQIRAEEVK
QHLAAMHPVT AAAATTVVAA TKPKQENKLR DKVAALVANA QSSAETRIKD IDRQRQEDMQ
IISNRFNKQK ELFDNQPSDS SVAAQARPPA PAPSRVVRPM PPPPPPPIAA LSPGLASSKR
RSPGDAPTTD EDSKRARKSH SDRLYPALSD LDSSGDNCCA AETASATDDS HQQDEEETES
CMDESDDQSQ TEDSSAGMCN GSLGREIMSA VQRNEVEMQQ QQTGKKTVRY ADQDMYYDDS
SLNSSQVSAG IDDYLDEALV EDYGSTQDDQ SDSGDEQNAS RLSLGSKGTT ASNSFSFRKN
PASICTPIEE HHEMEMDLQT PLLSGAQPVK SELSVNQDND NLVTLVHTVS FYRRQQSANS
SNSTPVRKIC REQQVMRSAL AGDCHAKHRL EYDSPQQSDY VAAATDIADQ TDEDDEEMQN
AREVNDASQA QDKIKKLLSE VCKQQQVIGQ ASQALNLCAA TVEFSGSTES VEGERYLLLA
THRRQACLDE VQRLRVENSI RPVGAPKEKG LLTVKDITIP LRQEYVRKMA SNNINGHHLV
CLLKYNEHVL ATKTVPTMPG LLSVKFPDVL QLNNVYADFR ITLEIYGMLA QRDQLPHELK
YHINLNKKGG IKTPKKKGGE NRLVMPPVQS PAGPHVVRTP QLVQYGFAIF SLREIQRTTW
TLTQVLGVSP LEGVVHMKVN CELSVSVEYK GFLTMFEDIS GFGAWHRRWC YLNGSVINYW
KYPDDEKRKT PMGSIDLNSC TSQKVTTAPR DICARLNTML LECERPALET DQESLIIVPN
GRTTTVRHLL SADTKEEREE WCAYLNKALT LLRAWGTTH


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CA18411-100 Antibodies: ANILLIN _ Scraps (internal) HOST: Goat Clonality: pAb 100
ER-14-0145 Goat Anti-ANILLIN _ Scraps, Mid-molecule, with HRP-conjugated secondary antibody 100
EIAAB46506 Beta-xin,Cardiomyopathy-associated protein 3,Cmya3,L-NAME-induced actin cytoskeletal protein,Rat,Rattus norvegicus,Xin actin-binding repeat-containing protein 2,Xin2,Xirp2
ER-14-0144 Goat Anti-Human ANILLIN _ Scraps (C Terminus), (C Terminus) Antibodies 100 μg


 

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