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CLIP-associating protein 1 (Cytoplasmic linker-associated protein 1)

 CLAP1_MOUSE             Reviewed;        1535 AA.
Q80TV8; Q505G6; Q6DI75; Q6PG14; Q8BNS4; Q99JH5; Q99JI2; Q9CVU1;
23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
25-OCT-2017, entry version 112.
RecName: Full=CLIP-associating protein 1;
AltName: Full=Cytoplasmic linker-associated protein 1;
Name=Clasp1; Synonyms=Kiaa0622;
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 GENOMIC DNA].
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-306 (ISOFORMS 1/2), NUCLEOTIDE
SEQUENCE [MRNA] OF 1251-1535 (ISOFORMS 1/2), INTERACTION WITH CLIP2
AND RSN, AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=11290329; DOI=10.1016/S0092-8674(01)00288-4;
Akhmanova A., Hoogenraad C.C., Drabek K., Stepanova T., Dortland B.,
Verkerk T., Vermeulen W., Burgering B.M., de Zeeuw C.I., Grosveld F.,
Galjart N.;
"Clasps are CLIP-115 and -170 associating proteins involved in the
regional regulation of microtubule dynamics in motile fibroblasts.";
Cell 104:923-935(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-393 (ISOFORMS 1/2), AND
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1187-1535 (ISOFORMS 1/2).
STRAIN=C57BL/6J; TISSUE=Embryo, and Testis;
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 MRNA] OF 735-1535 (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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 985-1535 (ISOFORM 1), AND
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 997-1535 (ISOFORM 2).
STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Salivary gland;
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]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic brain;
PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
"Phosphoproteomic analysis of the developing mouse brain.";
Mol. Cell. Proteomics 3:1093-1101(2004).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1220, 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).
[8]
INTERACTION WITH MACF1.
PubMed=18854161; DOI=10.1016/j.cell.2008.07.045;
Wu X., Kodama A., Fuchs E.;
"ACF7 regulates cytoskeletal-focal adhesion dynamics and migration and
has ATPase activity.";
Cell 135:137-148(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246; SER-545; SER-548;
SER-600; SER-636; SER-688; SER-820; SER-1088; THR-1092 AND SER-1110,
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1139 (ISOFORM 2), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, 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: Microtubule plus-end tracking protein that promotes the
stabilization of dynamic microtubules. Involved in the nucleation
of noncentrosomal microtubules originating from the trans-Golgi
network (TGN). Required for the polarization of the cytoplasmic
microtubule arrays in migrating cells towards the leading edge of
the cell. May act at the cell cortex to enhance the frequency of
rescue of depolymerizing microtubules by attaching their plus-ends
to cortical platforms composed of ERC1 and PHLDB2. This cortical
microtubule stabilizing activity is regulated at least in part by
phosphatidylinositol 3-kinase signaling. Also performs a similar
stabilizing function at the kinetochore which is essential for the
bipolar alignment of chromosomes on the mitotic spindle (By
similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with ERC1, MAPRE1, MAPRE3, microtubules, and
PHLDB2. The interaction with ERC1 may be mediated by PHLDB2.
Interacts with GCC2; recruits CLASP1 to Golgi membranes (By
similarity). Interacts with CLIP2 and RSN. Interacts with MACF1.
{ECO:0000250, ECO:0000269|PubMed:11290329,
ECO:0000269|PubMed:18854161}.
-!- INTERACTION:
O55156:Clip2 (xeno); NbExp=3; IntAct=EBI-908322, EBI-349416;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
{ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}.
Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Golgi apparatus,
trans-Golgi network {ECO:0000250}. Note=Localizes to microtubule
plus ends. Localizes to centrosomes, kinetochores and the mitotic
spindle from prometaphase. Subsequently localizes to the spindle
midzone from anaphase and to the midbody from telophase. In
migrating cells localizes to the plus ends of microtubules within
the cell body and to the entire microtubule lattice within the
lamella. Localizes to the cell cortex and this requires ERC1 and
PHLDB2. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q80TV8-1; Sequence=Displayed;
Name=2;
IsoId=Q80TV8-2; Sequence=VSP_022390, VSP_022391, VSP_022392;
Note=No experimental confirmation available. Contains a
phosphoserine at position 1139. {ECO:0000244|PubMed:21183079};
-!- TISSUE SPECIFICITY: Highly expressed in brain and heart and at
lower levels in kidney, lung, skeletal muscle and testis.
{ECO:0000269|PubMed:11290329}.
-!- SIMILARITY: Belongs to the CLASP family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB24639.2; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAC38020.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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EMBL; AC109294; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC131804; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC136636; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AJ276962; CAC35162.1; -; mRNA.
EMBL; AJ288061; CAC35163.1; -; mRNA.
EMBL; AK006534; BAB24639.2; ALT_INIT; mRNA.
EMBL; AK080782; BAC38020.1; ALT_SEQ; mRNA.
EMBL; AK122330; BAC65612.1; -; mRNA.
EMBL; BC057312; AAH57312.1; -; mRNA.
EMBL; BC075708; AAH75708.1; -; mRNA.
EMBL; BC094554; AAH94554.1; -; mRNA.
RefSeq; NP_001280229.1; NM_001293300.1.
RefSeq; NP_001280230.1; NM_001293301.1.
RefSeq; NP_083985.2; NM_029709.2.
UniGene; Mm.138740; -.
ProteinModelPortal; Q80TV8; -.
SMR; Q80TV8; -.
BioGrid; 218270; 5.
IntAct; Q80TV8; 7.
MINT; MINT-4123448; -.
STRING; 10090.ENSMUSP00000042266; -.
iPTMnet; Q80TV8; -.
PhosphoSitePlus; Q80TV8; -.
EPD; Q80TV8; -.
PaxDb; Q80TV8; -.
PeptideAtlas; Q80TV8; -.
PRIDE; Q80TV8; -.
GeneID; 76707; -.
KEGG; mmu:76707; -.
CTD; 23332; -.
MGI; MGI:1923957; Clasp1.
eggNOG; KOG2956; Eukaryota.
eggNOG; ENOG410ZMY0; LUCA.
HOVERGEN; HBG079692; -.
InParanoid; Q80TV8; -.
KO; K16578; -.
PhylomeDB; Q80TV8; -.
PRO; PR:Q80TV8; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_CLASP1; -.
GO; GO:0045180; C:basal cortex; ISO:MGI.
GO; GO:0005938; C:cell cortex; ISO:MGI.
GO; GO:0031592; C:centrosomal corona; ISO:MGI.
GO; GO:0005813; C:centrosome; ISO:MGI.
GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
GO; GO:0030981; C:cortical microtubule cytoskeleton; ISO:MGI.
GO; GO:0005881; C:cytoplasmic microtubule; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0000776; C:kinetochore; ISO:MGI.
GO; GO:0005828; C:kinetochore microtubule; IEA:InterPro.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0005876; C:spindle microtubule; ISO:MGI.
GO; GO:0002162; F:dystroglycan binding; ISO:MGI.
GO; GO:0043515; F:kinetochore binding; ISO:MGI.
GO; GO:0008017; F:microtubule binding; IDA:MGI.
GO; GO:0051010; F:microtubule plus-end binding; ISO:MGI.
GO; GO:0030953; P:astral microtubule organization; ISO:MGI.
GO; GO:0051301; P:cell division; ISO:MGI.
GO; GO:0040001; P:establishment of mitotic spindle localization; ISO:MGI.
GO; GO:0051294; P:establishment of spindle orientation; ISO:MGI.
GO; GO:0010458; P:exit from mitosis; ISO:MGI.
GO; GO:0007030; P:Golgi organization; ISO:MGI.
GO; GO:0034453; P:microtubule anchoring; ISS:UniProtKB.
GO; GO:0001578; P:microtubule bundle formation; ISO:MGI.
GO; GO:0000226; P:microtubule cytoskeleton organization; ISO:MGI.
GO; GO:0007020; P:microtubule nucleation; ISS:UniProtKB.
GO; GO:0031023; P:microtubule organizing center organization; ISS:UniProtKB.
GO; GO:0007052; P:mitotic spindle organization; ISO:MGI.
GO; GO:0007026; P:negative regulation of microtubule depolymerization; IDA:MGI.
GO; GO:0031111; P:negative regulation of microtubule polymerization or depolymerization; ISO:MGI.
GO; GO:0051497; P:negative regulation of stress fiber assembly; ISO:MGI.
GO; GO:1903690; P:negative regulation of wound healing, spreading of epidermal cells; ISO:MGI.
GO; GO:1904261; P:positive regulation of basement membrane assembly involved in embryonic body morphogenesis; ISO:MGI.
GO; GO:0010634; P:positive regulation of epithelial cell migration; ISO:MGI.
GO; GO:0045921; P:positive regulation of exocytosis; ISO:MGI.
GO; GO:0090091; P:positive regulation of extracellular matrix disassembly; ISO:MGI.
GO; GO:0010717; P:regulation of epithelial to mesenchymal transition; ISO:MGI.
GO; GO:0051893; P:regulation of focal adhesion assembly; ISO:MGI.
GO; GO:0010470; P:regulation of gastrulation; ISO:MGI.
GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; ISO:MGI.
GO; GO:0006903; P:vesicle targeting; ISO:MGI.
Gene3D; 1.25.10.10; -; 3.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR028399; CLASP_1.
InterPro; IPR024395; CLASP_N_dom.
InterPro; IPR021133; HEAT_type_2.
InterPro; IPR034085; TOG.
PANTHER; PTHR21567:SF28; PTHR21567:SF28; 1.
Pfam; PF12348; CLASP_N; 2.
SMART; SM01349; TOG; 4.
SUPFAM; SSF48371; SSF48371; 5.
PROSITE; PS50077; HEAT_REPEAT; 1.
1: Evidence at protein level;
Alternative splicing; Cell cycle; Cell division; Centromere;
Chromosome; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton;
Golgi apparatus; Kinetochore; Microtubule; Mitosis; Phosphoprotein;
Reference proteome; Repeat.
CHAIN 1 1535 CLIP-associating protein 1.
/FTId=PRO_0000272274.
REPEAT 87 124 HEAT 1.
REPEAT 163 200 HEAT 2.
REPEAT 405 440 HEAT 3.
REPEAT 441 477 HEAT 4.
REPEAT 971 1008 HEAT 5.
REPEAT 1339 1376 HEAT 6.
REPEAT 1457 1494 HEAT 7.
REGION 662 782 Interaction with microtubules, MAPRE1 and
MAPRE3. {ECO:0000250}.
REGION 1251 1535 Interaction with CLIP2 and RSN.
{ECO:0000269|PubMed:11290329}.
REGION 1251 1535 Interaction with PHLDB2. {ECO:0000250}.
REGION 1253 1535 Localization to kinetochores.
{ECO:0000250}.
COILED 1296 1327 {ECO:0000255}.
COMPBIAS 530 762 Ser-rich.
MOD_RES 246 246 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 545 545 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 548 548 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 558 558 Phosphoserine.
{ECO:0000250|UniProtKB:Q7Z460}.
MOD_RES 559 559 Phosphoserine.
{ECO:0000250|UniProtKB:Q7Z460}.
MOD_RES 568 568 Phosphoserine.
{ECO:0000250|UniProtKB:Q7Z460}.
MOD_RES 600 600 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 636 636 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 646 646 Phosphoserine.
{ECO:0000250|UniProtKB:Q7Z460}.
MOD_RES 647 647 Phosphoserine.
{ECO:0000250|UniProtKB:Q7Z460}.
MOD_RES 649 649 Phosphoserine.
{ECO:0000250|UniProtKB:Q7Z460}.
MOD_RES 656 656 Phosphothreonine.
{ECO:0000250|UniProtKB:Q7Z460}.
MOD_RES 684 684 Phosphoserine.
{ECO:0000250|UniProtKB:Q7Z460}.
MOD_RES 688 688 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 695 695 Phosphoserine.
{ECO:0000250|UniProtKB:Q7Z460}.
MOD_RES 702 702 Phosphoserine.
{ECO:0000250|UniProtKB:Q7Z460}.
MOD_RES 708 708 Phosphothreonine.
{ECO:0000250|UniProtKB:Q7Z460}.
MOD_RES 711 711 Phosphoserine.
{ECO:0000250|UniProtKB:Q7Z460}.
MOD_RES 784 784 Phosphoserine.
{ECO:0000250|UniProtKB:Q7Z460}.
MOD_RES 794 794 Phosphoserine.
{ECO:0000250|UniProtKB:Q7Z460}.
MOD_RES 820 820 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1088 1088 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1092 1092 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1096 1096 Phosphothreonine.
{ECO:0000250|UniProtKB:Q7Z460}.
MOD_RES 1110 1110 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1193 1193 Phosphoserine.
{ECO:0000250|UniProtKB:Q7Z460}.
MOD_RES 1220 1220 Phosphoserine.
{ECO:0000244|PubMed:16452087}.
VAR_SEQ 770 770 L -> LASRRHSRSTSALSTAESVGQS (in isoform
2). {ECO:0000303|PubMed:12693553,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_022390.
VAR_SEQ 805 805 L -> LLLGDARSK (in isoform 2).
{ECO:0000303|PubMed:12693553,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_022391.
VAR_SEQ 1120 1158 Missing (in isoform 2).
{ECO:0000303|PubMed:12693553,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_022392.
CONFLICT 1231 1231 I -> K (in Ref. 3; BAB24639).
{ECO:0000305}.
CONFLICT 1417 1417 P -> S (in Ref. 5; AAH75708).
{ECO:0000305}.
SEQUENCE 1535 AA; 169227 MW; 5EE40CCE493C64D2 CRC64;
MEPRMESCLA QVLQKDVGKR LQVGQELIDY FSDRQKSADL EHDQTLLDKL VDGLATSWVN
SSNYKVVLLG MDILSALVTR LQDRFKAQIG TVLPSLIDRL GDAKDSVREQ DQTLLLKIMD
QAANPQYVWD RMLGGFKHKN FRTREGICLC LIATLNASGA QTLTLSKIVP HICNLLGDPN
SQVRDAAINS LVEIYRHVGE RVRADLSKKG LPQSRLNVIF TKFDEVQKSG NMIQSANEKN
FDDEDSVDGN RPSSASSSSS KAPSSSRRNV NLGTTRRLMS SSLGSKSSAA KEGAGAVDEE
DFIKAFDDVP VVQIYSSRDL EESINKIREI LSDDKHDWEQ RVNALKKIRS LLLAGAAEYD
NFFQHLRLLD GAFKLSAKDL RSQVVREACI TLGHLSSVLG NKFDHGAEAI MPTIFNLIPN
SAKIMATSGV VAVRLIIRHT HIPRLIPVIT SNCTSKSVAV RRRCFEFLDL LLQEWQTHSL
ERHISVLAET IKKGIHDADS EARIEARKCY WGFHSHFSRE AEHLYHTLES SYQKALQSHL
KNSDSIVSLP QSDRSSSSSQ ESLNRPLSAK RSPTGSTASR GSTVSTKSVS TTGSLQRSRS
DIDVNAAASA KSKVSSSSGS PAFSSAAALP PGSYASLGRI RTRRQSSGST TNVASTPDSR
GRSRAKVVSQ SQRSRSANPA GAGSRSSSPG KLLGSGLAGG SSRGPPVTPS SEKRSKIPRS
QGCSRETSPN RIGLARSSRI PRPSMSQGCS RDTSRESSRD TSPARGFTPL DRFGLGQSGR
IPGSVNAMRV LSTSTDLEAA VADALKKPVR RRYEPYGMYS DDDANSDASS VCSERSYGSR
NGGIPHYLRQ TEDVAEVLNH CASSNWSERK EGLLGLQNLL KSQRTLSRVE LKRLCEIFTR
MFADPHSKRV FSMFLETLVD FIIIHKDDLQ DWLFVLLTQL LKKMGADLLG SVQAKVQKAL
DVTRDSFPFD QQFNILMRFI VDQTQTPNLK VKVAILKYIE SLARQMDPTD FVNSSETRLA
VSRIITWTTE PKSSDVRKAA QIVLISLFEL NTPEFTMLLG ALPKTFQDGA TKLLHNHLKN
SSNTGVGSPS NTIGRTPSRH PSSRTSPLTS PTNCSHGGLS PSRLWGWSAD GLSKPPPPFS
QPNSIPTAPS HKTLRRSYSP SMLDYDTENL NSEEIYSSLR GVTEAIEKFS FRSQEDLNEP
IKRDGKKDCD IVSRDGGAAS PATEGRGGSE IEGGRMALDN KTSLLNTQPP RAFPGPRARE
YNPYPYSDTI NTYDKTALKE AVFDDDMEQL RDVPIDHSDL VADLLKELSN HNERVEERKG
ALLELLKITR EDSLGVWEEH FKTILLLLLE TLGDKDHSIR ALALRVLREI LRNQPARFKN
YAELTIMKTL EAHKDSHKEV VRAAEEAAST LASSIHPEQC IKVLCPIIQT ADYPINLAAI
KMQTKVVERI TKESLLQLLV DIIPGLLQGY DNTESSVRKA SVFCLVAIYS VIGEDLKPHL
AQLTGSKMKL LNLYIKRAQT TNSNSSSSSD VSTHS


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Catalog number Product name Quantity
EIAAB07688 Clasp2,CLIP-associating protein 2,Cytoplasmic linker-associated protein 2,Rat,Rattus norvegicus
EIAAB07687 Clasp1,CLIP-associating protein 1,Cytoplasmic linker-associated protein 1,Kiaa0622,Mouse,Mus musculus
EIAAB07689 Clasp2,CLIP-associating protein 2,Cytoplasmic linker-associated protein 2,Kiaa0627,Mouse,Mus musculus
EIAAB07690 CLASP2,CLIP-associating protein 2,Cytoplasmic linker-associated protein 2,Homo sapiens,hOrbit2,Human,KIAA0627,Protein Orbit homolog 2
EIAAB07910 CAP-Gly domain-containing linker protein 1,CLIP1,CLIP-170,CYLN1,Cytoplasmic linker protein 1,Cytoplasmic linker protein 170 alpha-2,Homo sapiens,Human,Reed-Sternberg intermediate filament-associated p
EIAAB07913 CAP-Gly domain-containing linker protein 2,CLIP-115,CLIP2,CYLN2,Cytoplasmic linker protein 115,Cytoplasmic linker protein 2,Homo sapiens,Human,KIAA0291,WBSCR3,WBSCR4,Williams-Beuren syndrome chromosom
EIAAB07912 CAP-Gly domain-containing linker protein 2,CLIP-115,Clip2,Cyln2,Cytoplasmic linker protein 115,Cytoplasmic linker protein 2,Kiaa0291,Mouse,Mus musculus
EIAAB07686 CLASP1,CLIP-associating protein 1,Cytoplasmic linker-associated protein 1,Homo sapiens,hOrbit1,Human,KIAA0622,MAST1,Multiple asters homolog 1,Protein Orbit homolog 1
EIAAB07911 CAP-Gly domain-containing linker protein 2,CLIP-115,Clip2,Cyln2,Cytoplasmic linker protein 115,Cytoplasmic linker protein 2,Rat,Rattus norvegicus
EIAAB07914 CAP-Gly domain-containing linker protein 3,CLIP-170-related 59 kDa protein,CLIP3,CLIPR59,CLIPR-59,Cytoplasmic linker protein 170-related 59 kDa protein,Homo sapiens,Human
EIAAB07908 CAP-Gly domain-containing linker protein 1,Chicken,CLIP1,CLIP-170,Cytoplasmic linker protein 170,Gallus gallus,Restin,RSN
E1094m Human ELISA Kit FOR CLIP-associating protein 2 96T
CSB-EL005472RA Rat CLIP-associating protein 2(CLASP2) ELISA kit 96T
CLAP2_MOUSE Mouse ELISA Kit FOR CLIP-associating protein 2 96T
E11134r Mouse ELISA Kit FOR CLIP-associating protein 1 96T
CSB-EL005471MO Mouse CLIP-associating protein 1(CLASP1) ELISA kit 96T
CSB-EL005472MO Mouse CLIP-associating protein 2(CLASP2) ELISA kit 96T
CSB-EL005471HU Human CLIP-associating protein 1(CLASP1) ELISA kit 96T
CSB-EL005472HU Human CLIP-associating protein 2(CLASP2) ELISA kit 96T
CSB-EL005472RA Rat CLIP-associating protein 2(CLASP2) ELISA kit SpeciesRat 96T
CSB-EL005472MO Mouse CLIP-associating protein 2(CLASP2) ELISA kit SpeciesMouse 96T
CSB-EL005472HU Human CLIP-associating protein 2(CLASP2) ELISA kit SpeciesHuman 96T
CSB-EL005471HU Human CLIP-associating protein 1(CLASP1) ELISA kit SpeciesHuman 96T
CSB-EL005471MO Mouse CLIP-associating protein 1(CLASP1) ELISA kit SpeciesMouse 96T
CLAP1_HUMAN ELISA Kit FOR CLIP-associating protein 1; organism: Human; gene name: CLASP1 96T


 

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