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Protein bicaudal D homolog 2 (Bic-D 2)

 BICD2_MOUSE             Reviewed;         820 AA.
Q921C5; Q80TU1; Q8BTE3; Q9DCL3;
15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
12-SEP-2018, entry version 129.
RecName: Full=Protein bicaudal D homolog 2;
Short=Bic-D 2;
Name=Bicd2; Synonyms=Kiaa0699;
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), FUNCTION, INTERACTION WITH
DCTN2, SUBCELLULAR LOCATION, AND DOMAIN.
PubMed=11483508; DOI=10.1093/emboj/20.15.4041;
Hoogenraad C.C., Akhmanova A., Howell S.A., Dortland B.R.,
de Zeeuw C.I., Willemsen R., Visser P., Grosveld F., Galjart N.;
"Mammalian Golgi-associated Bicaudal-D2 functions in the dynein-
dynactin pathway by interacting with these complexes.";
EMBO J. 20:4041-4054(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Mammary tumor;
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]
PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
STRAIN=C57BL/6J; TISSUE=Embryo, and Kidney;
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]
FUNCTION, INTERACTION WITH RAB6A, AND SUBCELLULAR LOCATION.
PubMed=12447383; DOI=10.1038/ncb891;
Matanis T., Akhmanova A., Wulf P., Del Nery E., Weide T.,
Stepanova T., Galjart N., Grosveld F., Goud B., De Zeeuw C.I.,
Barnekow A., Hoogenraad C.C.;
"Bicaudal-D regulates COPI-independent Golgi-ER transport by
recruiting the dynein-dynactin motor complex.";
Nat. Cell Biol. 4:986-992(2002).
[6]
INTERACTION WITH CPNE4.
PubMed=12522145; DOI=10.1074/jbc.M212632200;
Tomsig J.L., Snyder S.L., Creutz C.E.;
"Identification of targets for calcium signaling through the copine
family of proteins. Characterization of a coiled-coil copine-binding
motif.";
J. Biol. Chem. 278:10048-10054(2003).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-578, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Kidney, 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).
[9]
FUNCTION, AND INTERACTION WITH RANBP2; RAB6A AND KIF5A.
PubMed=20386726; DOI=10.1371/journal.pbio.1000350;
Splinter D., Tanenbaum M.E., Lindqvist A., Jaarsma D., Flotho A.,
Yu K.L., Grigoriev I., Engelsma D., Haasdijk E.D., Keijzer N.,
Demmers J., Fornerod M., Melchior F., Hoogenraad C.C., Medema R.H.,
Akhmanova A.;
"Bicaudal D2, dynein, and kinesin-1 associate with nuclear pore
complexes and regulate centrosome and nuclear positioning during
mitotic entry.";
PLoS Biol. 8:E1000350-E1000350(2010).
[10]
FUNCTION, AND INTERACTION WITH DYNLL1; DYNC1H1; DYNC1I2; DCTN1 AND
DCTN2.
PubMed=22956769; DOI=10.1091/mbc.E12-03-0210;
Splinter D., Razafsky D.S., Schlager M.A., Serra-Marques A.,
Grigoriev I., Demmers J., Keijzer N., Jiang K., Poser I., Hyman A.A.,
Hoogenraad C.C., King S.J., Akhmanova A.;
"BICD2, dynactin, and LIS1 cooperate in regulating dynein recruitment
to cellular structures.";
Mol. Biol. Cell 23:4226-4241(2012).
[11]
TISSUE SPECIFICITY.
PubMed=23664119; DOI=10.1016/j.ajhg.2013.04.013;
Peeters K., Litvinenko I., Asselbergh B., Almeida-Souza L.,
Chamova T., Geuens T., Ydens E., Zimon M., Irobi J., De Vriendt E.,
De Winter V., Ooms T., Timmerman V., Tournev I., Jordanova A.;
"Molecular defects in the motor adaptor BICD2 cause proximal spinal
muscular atrophy with autosomal-dominant inheritance.";
Am. J. Hum. Genet. 92:955-964(2013).
[12]
FUNCTION, AND COMPLEX FORMATION WITH DYNEIN AND DYNACTIN.
PubMed=24986880; DOI=10.15252/embj.201488792;
Schlager M.A., Hoang H.T., Urnavicius L., Bullock S.L., Carter A.P.;
"In vitro reconstitution of a highly processive recombinant human
dynein complex.";
EMBO J. 33:1855-1868(2014).
[13]
FUNCTION.
PubMed=25035494; DOI=10.1126/science.1254198;
McKenney R.J., Huynh W., Tanenbaum M.E., Bhabha G., Vale R.D.;
"Activation of cytoplasmic dynein motility by dynactin-cargo adapter
complexes.";
Science 345:337-341(2014).
[14]
FUNCTION, INTERACTION WITH RAB6A, AND SUBCELLULAR LOCATION.
PubMed=25962623; DOI=10.1016/j.bbamcr.2015.05.005;
Matsuto M., Kano F., Murata M.;
"Reconstitution of the targeting of Rab6A to the Golgi apparatus in
semi-intact HeLa cells: A role of BICD2 in stabilizing Rab6A on Golgi
membranes and a concerted role of Rab6A/BICD2 interactions in Golgi-
to-ER retrograde transport.";
Biochim. Biophys. Acta 1853:2592-2609(2015).
[15]
ASSOCIATION WITH MICROTUBULES.
PubMed=26968983; DOI=10.15252/embj.201593071;
McKenney R.J., Huynh W., Vale R.D., Sirajuddin M.;
"Tyrosination of alpha-tubulin controls the initiation of processive
dynein-dynactin motility.";
EMBO J. 35:1175-1185(2016).
-!- FUNCTION: Acts as an adapter protein linking the dynein motor
complex to various cargos and converts dynein from a non-
processive to a highly processive motor in the presence of
dynactin. Facilitates and stabilizes the interaction between
dynein and dynactin and activates dynein processivity (the ability
to move along a microtubule for a long distance without falling
off the track) (PubMed:11483508, PubMed:25035494, PubMed:24986880,
PubMed:22956769). Facilitates the binding of RAB6A to the Golgi by
stabilizing its GTP-bound form (PubMed:25962623). Regulates coat
complex coatomer protein I (COPI)-independent Golgi-endoplasmic
reticulum transport via its interaction with RAB6A and recruitment
of the dynein-dynactin motor complex (PubMed:12447383,
PubMed:25962623). Contributes to nuclear and centrosomal
positioning prior to mitotic entry through regulation of both
dynein and kinesin-1. During G2 phase of the cell cycle,
associates with RANBP2 at the nuclear pores and recruits dynein
and dynactin to the nuclear envelope to ensure proper positioning
of the nucleus relative to centrosomes prior to the onset of
mitosis (PubMed:20386726). {ECO:0000269|PubMed:11483508,
ECO:0000269|PubMed:12447383, ECO:0000269|PubMed:20386726,
ECO:0000269|PubMed:22956769, ECO:0000269|PubMed:24986880,
ECO:0000269|PubMed:25035494, ECO:0000269|PubMed:25962623}.
-!- SUBUNIT: Interacts with CPNE4 (via VWFA domain) (PubMed:12522145).
Interacts with NEK9 (By similarity). Interacts with DCTN2
(PubMed:11483508, PubMed:22956769). Interacts with RAB6A
(PubMed:12447383, PubMed:25962623). Interacts with DNAI1 (By
similarity). Interacts with DYNLL1, DYNC1H1, DYNC1I2 and DCTN1
(PubMed:22956769). Forms a complex with dynein and dynactin
(PubMed:24986880). The dynein-dynactin-BICD2 ternary complex (DDB)
binds preferentially to tyrosinated microtubules than to
detyrosinated microtubules (PubMed:26968983). Interacts with
RANBP2, RAB6A and KIF5A (PubMed:20386726). Interacts with KIF1C
(By similarity). {ECO:0000250|UniProtKB:Q8TD16,
ECO:0000269|PubMed:11483508, ECO:0000269|PubMed:12447383,
ECO:0000269|PubMed:12522145, ECO:0000269|PubMed:20386726,
ECO:0000269|PubMed:22956769, ECO:0000269|PubMed:24986880,
ECO:0000269|PubMed:25035494, ECO:0000269|PubMed:25962623,
ECO:0000269|PubMed:26968983}.
-!- INTERACTION:
P35279:Rab6a; NbExp=3; IntAct=EBI-642984, EBI-444674;
P49792:RANBP2 (xeno); NbExp=4; IntAct=EBI-642995, EBI-973138;
-!- SUBCELLULAR LOCATION: Golgi apparatus
{ECO:0000269|PubMed:11483508, ECO:0000269|PubMed:12447383,
ECO:0000269|PubMed:25962623}. Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:11483508}. Cytoplasm
{ECO:0000250|UniProtKB:Q8TD16}. Nucleus, nuclear pore complex
{ECO:0000250|UniProtKB:Q8TD16}. Nucleus envelope
{ECO:0000250|UniProtKB:Q8TD16}. Note=In interphase cells mainly
localizes to the Golgi complex and colocalizes with dynactin at
microtubule plus ends (PubMed:11483508). Localizes to the nuclear
envelope and cytoplasmic stacks of nuclear pore complex known as
annulate lamellae in a RANBP2-dependent manner during G2 phase of
the cell cycle (By similarity). {ECO:0000250|UniProtKB:Q8TD16,
ECO:0000269|PubMed:11483508}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q921C5-1; Sequence=Displayed;
Name=2;
IsoId=Q921C5-2; Sequence=VSP_007970;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q921C5-3; Sequence=VSP_007971, VSP_007972;
Note=Ref.4 (BAB22282) sequence differs from that shown due to a
frameshift in position 70. No experimental confirmation
available. {ECO:0000305};
-!- TISSUE SPECIFICITY: Ubiquitously expressed with high expression in
the spinal cord. {ECO:0000269|PubMed:23664119}.
-!- DOMAIN: The fourth coiled coil region is involved in Golgi
targeting and in the interaction with DCTN2.
{ECO:0000269|PubMed:11483508}.
-!- PTM: Phosphorylated by NEK9 in vitro.
{ECO:0000250|UniProtKB:Q8TD16}.
-!- SIMILARITY: Belongs to the BicD family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAC65630.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AJ250106; CAC51393.1; -; mRNA.
EMBL; AK122348; BAC65630.1; ALT_INIT; mRNA.
EMBL; BC032198; AAH32198.1; -; mRNA.
EMBL; AK002683; BAB22282.1; ALT_FRAME; mRNA.
EMBL; AK003456; BAC25035.1; -; mRNA.
CCDS; CCDS36656.1; -. [Q921C5-1]
CCDS; CCDS36657.1; -. [Q921C5-2]
RefSeq; NP_001034268.1; NM_001039179.2. [Q921C5-2]
RefSeq; NP_001034269.1; NM_001039180.2.
RefSeq; NP_084067.1; NM_029791.4. [Q921C5-1]
UniGene; Mm.197387; -.
ProteinModelPortal; Q921C5; -.
SMR; Q921C5; -.
BioGrid; 218383; 7.
DIP; DIP-49453N; -.
IntAct; Q921C5; 18.
MINT; Q921C5; -.
STRING; 10090.ENSMUSP00000039394; -.
iPTMnet; Q921C5; -.
PhosphoSitePlus; Q921C5; -.
PaxDb; Q921C5; -.
PeptideAtlas; Q921C5; -.
PRIDE; Q921C5; -.
Ensembl; ENSMUST00000048544; ENSMUSP00000039394; ENSMUSG00000037933. [Q921C5-2]
Ensembl; ENSMUST00000110085; ENSMUSP00000105712; ENSMUSG00000037933. [Q921C5-1]
GeneID; 76895; -.
KEGG; mmu:76895; -.
UCSC; uc007qjg.2; mouse. [Q921C5-1]
UCSC; uc007qji.2; mouse. [Q921C5-2]
CTD; 23299; -.
MGI; MGI:1924145; Bicd2.
eggNOG; KOG0999; Eukaryota.
eggNOG; ENOG410XR47; LUCA.
GeneTree; ENSGT00390000004114; -.
HOGENOM; HOG000261658; -.
HOVERGEN; HBG050686; -.
InParanoid; Q921C5; -.
KO; K18739; -.
OMA; DRDSHED; -.
OrthoDB; EOG091G01P4; -.
PhylomeDB; Q921C5; -.
TreeFam; TF323833; -.
Reactome; R-MMU-6811436; COPI-independent Golgi-to-ER retrograde traffic.
ChiTaRS; Bicd2; mouse.
PRO; PR:Q921C5; -.
Proteomes; UP000000589; Chromosome 13.
Bgee; ENSMUSG00000037933; Expressed in 291 organ(s), highest expression level in rostral migratory stream.
CleanEx; MM_BICD2; -.
ExpressionAtlas; Q921C5; baseline and differential.
Genevisible; Q921C5; MM.
GO; GO:0005642; C:annulate lamellae; ISS:UniProtKB.
GO; GO:0005813; C:centrosome; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
GO; GO:0005643; C:nuclear pore; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0008093; F:cytoskeletal adaptor activity; IEA:InterPro.
GO; GO:0034452; F:dynactin binding; IDA:UniProtKB.
GO; GO:0070840; F:dynein complex binding; IDA:UniProtKB.
GO; GO:0051959; F:dynein light intermediate chain binding; IPI:FlyBase.
GO; GO:0017137; F:Rab GTPase binding; IPI:BHF-UCL.
GO; GO:0051642; P:centrosome localization; ISS:UniProtKB.
GO; GO:0072393; P:microtubule anchoring at microtubule organizing center; IMP:BHF-UCL.
GO; GO:0007018; P:microtubule-based movement; IDA:MGI.
GO; GO:0072385; P:minus-end-directed organelle transport along microtubule; IMP:BHF-UCL.
GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
GO; GO:0034067; P:protein localization to Golgi apparatus; IMP:UniProtKB.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; ISO:MGI.
GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; IMP:UniProtKB.
InterPro; IPR018477; BICD.
PANTHER; PTHR31233; PTHR31233; 1.
Pfam; PF09730; BicD; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Coiled coil; Complete proteome;
Cytoplasm; Cytoskeleton; Golgi apparatus; mRNA transport;
Nuclear pore complex; Nucleus; Phosphoprotein; Protein transport;
Reference proteome; Translocation; Transport.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q8TD16}.
CHAIN 2 820 Protein bicaudal D homolog 2.
/FTId=PRO_0000205360.
REGION 25 400 Interaction with DYNLL1, DYNC1H1,
DYNC1I2, DCTN1 and DCTN2.
{ECO:0000269|PubMed:22956769}.
REGION 336 595 Interaction with KIF5A.
{ECO:0000269|PubMed:20386726}.
REGION 586 820 Interaction with RANBP2.
{ECO:0000269|PubMed:20386726}.
REGION 662 810 Interaction with RAB6A.
{ECO:0000269|PubMed:12447383,
ECO:0000269|PubMed:20386726,
ECO:0000269|PubMed:25962623}.
COILED 20 270 {ECO:0000255}.
COILED 340 539 {ECO:0000255}.
COILED 662 804 {ECO:0000255}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:Q8TD16}.
MOD_RES 190 190 Phosphoserine.
{ECO:0000250|UniProtKB:Q8TD16}.
MOD_RES 224 224 Phosphoserine.
{ECO:0000250|UniProtKB:Q8TD16}.
MOD_RES 320 320 Phosphoserine.
{ECO:0000250|UniProtKB:Q8TD16}.
MOD_RES 321 321 Phosphothreonine.
{ECO:0000250|UniProtKB:Q8TD16}.
MOD_RES 345 345 Phosphoserine.
{ECO:0000250|UniProtKB:Q8TD16}.
MOD_RES 397 397 Phosphoserine.
{ECO:0000250|UniProtKB:Q8TD16}.
MOD_RES 570 570 Phosphoserine.
{ECO:0000250|UniProtKB:Q8TD16}.
MOD_RES 578 578 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 598 598 Phosphothreonine.
{ECO:0000250|UniProtKB:Q8TD16}.
MOD_RES 819 819 Phosphoserine.
{ECO:0000250|UniProtKB:Q8TD16}.
VAR_SEQ 328 338 APPSPSLVSDL -> VHPLHALCLTV (in isoform
3). {ECO:0000305}.
/FTId=VSP_007971.
VAR_SEQ 339 820 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_007972.
VAR_SEQ 820 820 L -> VSHTCACASERAEGAGLANQVFCSEKHSIYCD (in
isoform 2).
{ECO:0000303|PubMed:12693553}.
/FTId=VSP_007970.
SEQUENCE 820 AA; 93391 MW; 0C1A1754CD74DDE1 CRC64;
MSAPSEEEEY ARLVMEAQPE WLRAEVKRLS HELAETTREK IQAAEYGLAV LEEKHQLKLQ
FEELEVDYEA IRSEMEQLKE AFGQAHTNHK KVAADGESRE ESLIQESASK EQYYVRKVLE
LQTELKQLRN VLTNTQSENE RLTSVAQELK EINQNVEIQR GRLRDDIKEY KFREARLLQD
YSELEEENIS LQKQVSVLRQ NQVEFEGLKH EIKRLEEETE YLNSQLEDAI RLKEISERQL
EEALETLKTE REQKNNLRKE LSHYMSINDS FYTSHLQVSL DGLKFSDDTV TAEPNNDAEA
LVNGFEHSGL VKSSLDNKTS TPRKDGLAPP SPSLVSDLLS ELHISEIQKL KQQLVQMERE
KVGLLATLQD TQKQLEQARG TLSEQHEKVN RLTENLSALR RLQAGKERQT SLDNEKDRDS
HEDGDYYEVD INGPEILACK YHVAVAEAGE LREQLKALRS THEAREAQHA EEKGRYEAEG
QALTEKISLL EKASHQDREL LAHLEKELKK VSDVAGETQG SLNVAQDELV TFSEELANLY
HHVCMCNNET PNRVMLDYYR EGQGKAGRTS PEGRGRRSPV LLPKGLLATE VGRADGGTGD
NSPSPSSSLP SPLSDPRREP MNIYNLIAII RDQIKHLQAA VDRTTELSRQ RIASQELGPA
VDKDKEALME EILKLKSLLS TKREQITTLR TVLKANKQTA EVALANLKSK YENEKAMVTE
TMMKLRNELK ALKEDAATFS SLRAMFATRC DEYITQLDEM QRQLAAAEDE KKTLNSLLRM
AIQQKLALTQ RLELLELDHE QTRRGRSKAA SKAKPASPSL


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G2471 Protein bicaudal C homolog 1 (BICC1), Mouse, ELISA Kit 96T
CSB-EL002695MO Mouse Protein bicaudal C homolog 1(BICC1) ELISA kit 96T
G2474 Protein bicaudal D homolog 2 (BICD2), Human, ELISA Kit 96T
CSB-EL002696MO Mouse Protein bicaudal D homolog 1(BICD1) ELISA kit 96T
G2475 Protein bicaudal D homolog 2 (BICD2), Mouse, ELISA Kit 96T
CSB-EL002697HU Human Protein bicaudal D homolog 2(BICD2) ELISA kit 96T
G2470 Protein bicaudal C homolog 1 (BICC1), Human, ELISA Kit 96T
CSB-EL002696HU Human Protein bicaudal D homolog 1(BICD1) ELISA kit 96T
CSB-EL002695HU Human Protein bicaudal C homolog 1(BICC1) ELISA kit 96T
G2473 Protein bicaudal D homolog 1 (BICD1), Mouse, ELISA Kit 96T
CSB-EL002695HU Human Protein bicaudal C homolog 1(BICC1) ELISA kit SpeciesHuman 96T
CSB-EL002696MO Mouse Protein bicaudal D homolog 1(BICD1) ELISA kit SpeciesMouse 96T
CSB-EL002696HU Human Protein bicaudal D homolog 1(BICD1) ELISA kit SpeciesHuman 96T
CSB-EL002697HU Human Protein bicaudal D homolog 2(BICD2) ELISA kit SpeciesHuman 96T
CSB-EL002697MO Mouse Protein bicaudal D homolog 2(BICD2) ELISA kit SpeciesMouse 96T
CSB-EL002695MO Mouse Protein bicaudal C homolog 1(BICC1) ELISA kit SpeciesMouse 96T
BICD1_HUMAN ELISA Kit FOR Protein bicaudal D homolog 1; organism: Human; gene name: BICD1 96T
BICC1_MOUSE ELISA Kit FOR Protein bicaudal C homolog 1; organism: Mouse; gene name: Bicc1 96T
BICD1_MOUSE ELISA Kit FOR Protein bicaudal D homolog 1; organism: Mouse; gene name: Bicd1 96T
BICD2_HUMAN ELISA Kit FOR Protein bicaudal D homolog 2; organism: Human; gene name: BICD2 96T


 

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