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

Calpain-type cysteine protease ADL1 (EC 3.4.22.-) (Phytocalpain ADL1) (Protein ADAXIALIZED LEAF1) (Protein DEFECTIVE KERNEL 1) (OsDEK1) (Protein SHOOTLESS 3)

 DEK1_ORYSJ              Reviewed;        2162 AA.
Q6ZFZ4; Q8RYA5;
18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
30-AUG-2017, entry version 99.
RecName: Full=Calpain-type cysteine protease ADL1;
EC=3.4.22.-;
AltName: Full=Phytocalpain ADL1;
AltName: Full=Protein ADAXIALIZED LEAF1;
AltName: Full=Protein DEFECTIVE KERNEL 1;
Short=OsDEK1;
AltName: Full=Protein SHOOTLESS 3;
Flags: Precursor;
Name=ADL1; Synonyms=DEK1, ODM63, SHL3;
OrderedLocusNames=Os02g0709400, LOC_Os02g47970; ORFNames=OJ1311_H06.4;
Oryza sativa subsp. japonica (Rice).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade;
Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
NCBI_TaxID=39947;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE
SPECIFICITY.
STRAIN=cv. Taichung 65;
PubMed=19665012; DOI=10.1016/j.ydbio.2009.07.042;
Hibara K., Obara M., Hayashida E., Abe M., Ishimaru T., Satoh H.,
Itoh J., Nagato Y.;
"The ADAXIALIZED LEAF1 gene functions in leaf and embryonic pattern
formation in rice.";
Dev. Biol. 334:345-354(2009).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=11929961; DOI=10.1073/pnas.042098799;
Lid S.E., Gruis D., Jung R., Lorentzen J.A., Ananiev E.,
Chamberlin M., Niu X., Meeley R., Nichols S., Olsen O.-A.;
"The defective kernel 1 (dek1) gene required for aleurone cell
development in the endosperm of maize grains encodes a membrane
protein of the calpain gene superfamily.";
Proc. Natl. Acad. Sci. U.S.A. 99:5460-5465(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Nipponbare;
PubMed=16100779; DOI=10.1038/nature03895;
International rice genome sequencing project (IRGSP);
"The map-based sequence of the rice genome.";
Nature 436:793-800(2005).
[4]
GENOME REANNOTATION.
STRAIN=cv. Nipponbare;
PubMed=18089549; DOI=10.1093/nar/gkm978;
The rice annotation project (RAP);
"The rice annotation project database (RAP-DB): 2008 update.";
Nucleic Acids Res. 36:D1028-D1033(2008).
[5]
GENOME REANNOTATION.
STRAIN=cv. Nipponbare;
PubMed=24280374; DOI=10.1186/1939-8433-6-4;
Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H.,
McCombie W.R., Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S.,
Childs K.L., Davidson R.M., Lin H., Quesada-Ocampo L.,
Vaillancourt B., Sakai H., Lee S.S., Kim J., Numa H., Itoh T.,
Buell C.R., Matsumoto T.;
"Improvement of the Oryza sativa Nipponbare reference genome using
next generation sequence and optical map data.";
Rice 6:4-4(2013).
[6]
FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF TRP-1841.
DOI=10.1002/dvg.1020160403;
Hong S.K., Aoki T., Kitano H., Satoh H., Nagato Y.;
"Phenotypic diversity of 188 rice embryo mutants.";
Dev. Genet. 16:298-310(1995).
[7]
FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF SER-1776.
STRAIN=cv. Taichung 65;
PubMed=10409508;
Satoh N., Hong S.-K., Nishimura A., Matsuoka M., Kitano H., Nagato Y.;
"Initiation of shoot apical meristem in rice: characterization of four
SHOOTLESS genes.";
Development 126:3629-3636(1999).
-!- FUNCTION: Essential protein involved in epiderm development.
Required for aleurone cell development in the endosperm probably
by maintaining and restricting the aleurone and embryonic
epidermal L1 cell-layer fates as well as meristems organization.
Involved in the maintenance of adaxial/abaxial axis information in
developing leaves, probably by regulating cell proliferation and
expansion. Does not need calcium ions to be active.
{ECO:0000269|PubMed:10409508, ECO:0000269|PubMed:19665012,
ECO:0000269|Ref.6}.
-!- CATALYTIC ACTIVITY: Broad endopeptidase specificity.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass
membrane protein {ECO:0000250}. Endosome membrane {ECO:0000250};
Multi-pass membrane protein {ECO:0000250}.
-!- TISSUE SPECIFICITY: Ubiquitously expressed with higher levels in
embryos, vasculatures, leaf primordia, leaf margins, and shoot
apical meristem (SAM). {ECO:0000269|PubMed:19665012}.
-!- DOMAIN: The transmembrane regions are not required for calpain
activity but may play regulatory roles. {ECO:0000250}.
-!- PTM: Autocatalytic proteolytic cleavage leading to the production
of mainly cytoplasmic localized subproducts of about 85 and 120
kDa. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Abnormal embryos arrested at the globular
stage with an abnormal aleurone layer on the ventral side.
{ECO:0000269|PubMed:10409508, ECO:0000269|PubMed:19665012,
ECO:0000269|Ref.6}.
-!- MISCELLANEOUS: Although homology to other calpains is high within
the protease domain, the lack of calcium-binding sites suggests
that this protein is a protease that may not be activated by
calcium ions. {ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB477099; BAI44850.1; -; mRNA.
EMBL; AY062272; AAL38190.1; -; mRNA.
EMBL; AP004161; BAD07761.1; -; Genomic_DNA.
EMBL; AP008208; BAF09804.1; -; Genomic_DNA.
EMBL; AP014958; -; NOT_ANNOTATED_CDS; Genomic_DNA.
RefSeq; XP_015625425.1; XM_015769939.1.
RefSeq; XP_015625426.1; XM_015769940.1.
UniGene; Os.11709; -.
ProteinModelPortal; Q6ZFZ4; -.
SMR; Q6ZFZ4; -.
STRING; 39947.LOC_Os02g47970.1; -.
MEROPS; C02.019; -.
iPTMnet; Q6ZFZ4; -.
PaxDb; Q6ZFZ4; -.
PRIDE; Q6ZFZ4; -.
GeneID; 4330484; -.
KEGG; osa:4330484; -.
eggNOG; KOG0045; Eukaryota.
eggNOG; ENOG410XP0B; LUCA.
HOGENOM; HOG000030613; -.
InParanoid; Q6ZFZ4; -.
OrthoDB; EOG09360026; -.
Proteomes; UP000059680; Chromosome 2.
Genevisible; Q6ZFZ4; OS.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IBA:GO_Central.
GO; GO:0008234; F:cysteine-type peptidase activity; ISS:UniProtKB.
GO; GO:0009793; P:embryo development ending in seed dormancy; ISS:UniProtKB.
GO; GO:0090628; P:plant epidermal cell fate specification; ISS:UniProtKB.
GO; GO:0006508; P:proteolysis; IBA:GO_Central.
GO; GO:2000011; P:regulation of adaxial/abaxial pattern formation; IMP:UniProtKB.
GO; GO:0001558; P:regulation of cell growth; ISS:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; ISS:UniProtKB.
GO; GO:2000014; P:regulation of endosperm development; ISS:UniProtKB.
GO; GO:2000024; P:regulation of leaf development; IMP:UniProtKB.
GO; GO:0009934; P:regulation of meristem structural organization; IMP:UniProtKB.
GO; GO:0097264; P:self proteolysis; ISS:UniProtKB.
CDD; cd00044; CysPc; 1.
InterPro; IPR022684; Calpain_cysteine_protease.
InterPro; IPR022682; Calpain_domain_III.
InterPro; IPR022683; Calpain_III.
InterPro; IPR013320; ConA-like_dom.
InterPro; IPR000169; Pept_cys_AS.
InterPro; IPR001300; Peptidase_C2_calpain_cat.
Pfam; PF01067; Calpain_III; 1.
Pfam; PF00648; Peptidase_C2; 1.
PRINTS; PR00704; CALPAIN.
SMART; SM00720; calpain_III; 1.
SMART; SM00230; CysPc; 1.
SUPFAM; SSF49758; SSF49758; 1.
SUPFAM; SSF49899; SSF49899; 1.
PROSITE; PS50203; CALPAIN_CAT; 1.
PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Cytoplasm; Developmental protein;
Endoplasmic reticulum; Endosome; Hydrolase; Membrane; Phosphoprotein;
Protease; Reference proteome; Repeat; Signal; Thiol protease;
Transmembrane; Transmembrane helix.
SIGNAL 1 33 {ECO:0000255}.
CHAIN 34 2162 Calpain-type cysteine protease ADL1.
/FTId=PRO_0000423441.
PROPEP 34 ? {ECO:0000250}.
/FTId=PRO_0000423442.
TOPO_DOM 34 70 Extracellular. {ECO:0000255}.
TRANSMEM 71 91 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 92 95 Cytoplasmic. {ECO:0000255}.
TRANSMEM 96 116 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 117 127 Extracellular. {ECO:0000255}.
TRANSMEM 128 148 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 149 164 Cytoplasmic. {ECO:0000255}.
TRANSMEM 165 185 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 186 236 Extracellular. {ECO:0000255}.
TRANSMEM 237 257 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 258 264 Cytoplasmic. {ECO:0000255}.
TRANSMEM 265 285 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 286 294 Extracellular. {ECO:0000255}.
TRANSMEM 295 315 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 316 320 Cytoplasmic. {ECO:0000255}.
TRANSMEM 321 341 Helical; Name=8. {ECO:0000255}.
TOPO_DOM 342 626 Extracellular. {ECO:0000255}.
TRANSMEM 627 647 Helical; Name=9. {ECO:0000255}.
TOPO_DOM 648 663 Cytoplasmic. {ECO:0000255}.
TRANSMEM 664 684 Helical; Name=10. {ECO:0000255}.
TOPO_DOM 685 697 Extracellular. {ECO:0000255}.
TRANSMEM 698 718 Helical; Name=11. {ECO:0000255}.
TOPO_DOM 719 722 Cytoplasmic. {ECO:0000255}.
TRANSMEM 723 743 Helical; Name=12. {ECO:0000255}.
TOPO_DOM 744 773 Extracellular. {ECO:0000255}.
TRANSMEM 774 794 Helical; Name=13. {ECO:0000255}.
TOPO_DOM 795 825 Cytoplasmic. {ECO:0000255}.
TRANSMEM 826 846 Helical; Name=14. {ECO:0000255}.
TOPO_DOM 847 856 Extracellular. {ECO:0000255}.
TRANSMEM 857 877 Helical; Name=15. {ECO:0000255}.
TOPO_DOM 878 890 Cytoplasmic. {ECO:0000255}.
TRANSMEM 891 911 Helical; Name=16. {ECO:0000255}.
TOPO_DOM 912 924 Extracellular. {ECO:0000255}.
TRANSMEM 925 945 Helical; Name=17. {ECO:0000255}.
TOPO_DOM 946 949 Cytoplasmic. {ECO:0000255}.
TRANSMEM 950 970 Helical; Name=18. {ECO:0000255}.
TOPO_DOM 971 984 Extracellular. {ECO:0000255}.
TRANSMEM 985 1005 Helical; Name=19. {ECO:0000255}.
TOPO_DOM 1006 1019 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1020 1040 Helical; Name=20. {ECO:0000255}.
TOPO_DOM 1041 1063 Extracellular. {ECO:0000255}.
TRANSMEM 1064 1084 Helical; Name=21. {ECO:0000255}.
TOPO_DOM 1085 2162 Cytoplasmic. {ECO:0000255}.
DOMAIN 1418 1611 Calpain catalytic 1.
{ECO:0000255|PROSITE-ProRule:PRU00239}.
DOMAIN 1706 2008 Calpain catalytic 2.
{ECO:0000255|PROSITE-ProRule:PRU00239}.
COMPBIAS 1249 1255 Poly-Leu.
ACT_SITE 1772 1772 {ECO:0000250}.
ACT_SITE 1930 1930 {ECO:0000250}.
ACT_SITE 1950 1950 {ECO:0000250}.
MOD_RES 1372 1372 Phosphoserine. {ECO:0000250}.
MOD_RES 1377 1377 Phosphoserine. {ECO:0000250}.
MOD_RES 1668 1668 Phosphoserine. {ECO:0000250}.
MUTAGEN 1776 1776 S->N: In adl1-s1 and shl3-1; deletion of
the apical region including the shoot
apical meristem (SAM), coleoptile, and
scutellum in embryos, and no clear root
organization.
{ECO:0000269|PubMed:10409508}.
MUTAGEN 1777 1777 A->V: In adl1-2; abaxially rolled leaves
covered with bulliform-like cells, which
are normally distributed only on the
adaxial surface; this adaxialization
concerns both epidermal and mesophyll
tissues. Larger L1 cells in shoot apical
meristems (SAM).
MUTAGEN 1841 1841 W->R: In adl1-g1 and odm-63; abnormal
embryos arrested at the globular stage
with an abnormal aleurone layer on the
ventral side. {ECO:0000269|Ref.6}.
MUTAGEN 2110 2110 G->R: In adl1-1; abaxially rolled leaves
covered with bulliform-like cells, which
are normally distributed only on the
adaxial surface; this adaxialization
concerns both epidermal and mesophyll
tissues. Larger L1 cells in shoot apical
meristems (SAM).
CONFLICT 42 42 Y -> F (in Ref. 2; AAL38190).
{ECO:0000305}.
CONFLICT 713 713 L -> F (in Ref. 2; AAL38190).
{ECO:0000305}.
SEQUENCE 2162 AA; 239859 MW; 9FF44A8AE2B23F0B CRC64;
MEEEEHRGVV LVCSICGFLF AVLGPLSFWI LWAVNWRPWR LYSWIYARKW PAYVQGPQLS
TLCSFFTLFA WLVVVSPITV LLVWGGILIA LLERNIIGLA VIMVGVALLL SFYSIMLWWR
TQWQSSKAVA YLLLLAVGLL CAYEFCAVYV TTGASASELN SPSGFFFGVS AISLAINMLF
ISKILFNGSG FDVDEYVRRL YKFAYSDCVE VAPVSCSPDP PDPSELYMTK SSRVLHLGLL
YLCSLMVLVV YSILYGLTSK EARWLGALTS VAVVILDWNL GLCSFRFELL KSRMIALFVA
GTSRVFLICF GVHYWYLGHC ISYAFVASVL LAAAVSCWLS ISNPSVARID ALRSTVIKLR
EGFRRKGQTS SSNSSDGCGS SVKRSSGSVE AGPHGNATDS MYRSNSQSDC VNWNNVPFDR
SNSCQEGQSS DKNIDSGRAS LAHRSNSCLS AVAVQDPETA VVSADRHGDP TASLVVCSSS
GLESQGCESS GSATASGNQQ LLDLNLAAIF QDRLNDPRIT SMLKRNGGLG DVELANLLQD
KGLDPNFSYM MKDKVMDPRI LALLQRSSLD ADREHQDDVD VTGTDSDRLD TTIANQISLS
EELRRSGLEN WLNLSRLMFH QVAGSPIRAF VVFTLIFIIE TVTVAVHRPK PIKVINATHE
QFEFGFSILL LSPVVCSIMA FIWSLCAEEM TMTSKPRKYG FIAWLLSTCV GLLLSFLSKS
SVILGLSLTV PLMVACLSFA IPIWMRNGYR FWIPGGELDS RENIRQAPGK KERALFAISI
TVFTASVIGL GAIVSAKPLD ALGYKGWDAD KKSFYSPYAT SMYLGWALSS TIAVLATGVI
PIVAWFATYR FSPSSAICVG LFATVLVSFC GVSYWGVVNS RQDGVPLKAD FLAALLPLLC
IPAVFSLFTG MYKWKDDDWK ISRGVYLFVG MGVLLLLGAI SAVIVTIRPW TVGVACLLVI
LFLVFAIGVI HYWTSNNFYL TRTQMLLVCS LAFLLALAAF LMGLFQEKPF VGASIGYFSF
LFLLTGRALT VLLSPPIVVY SPRVLPVYVY DAHADSAKNV SYAFLILYGI ALATEVWGVI
ASLILNPPFI GAAISAITLV IAFSFAVSRP CLTLKMLEDA VHFLSKDTVV QAMSRSANKT
RNAISGTYSA PQRSASSAAL LVGDPAITLD RAGNFVLPRA DVMKLRDRLR NEEITAGSFF
CGVKNCLMIG SPVDVDYRRN MCAHARILAL EEAIDTEWVY MWDKFGGYLL LLLGLTAKAE
QIQDEVRLRL FLDSIGLSDL SAKEIKKWMP EDRRHFELIQ ESYIREKEME EEVLMQRREE
EGKGRERRKA LLEREERKWK ELEISLLSSI PNAGSRDAAA MAAAVRAVGG DSALEDSFAR
DRVSSIARHI RKAQLARRAE QTGIPDTVCI LDDEPRSTGR HCGEIDLCLC ESKKVSFSIA
VMVQPVSGPV CLFGTEFQKK VCWEILVAGS EQGMEAGQVG LRLVTKGERM TTVAKEWNIG
ASSIADGRWH LVTVTIDADL GEATSFIDGV YDGYQNALPL PRNNGIWEPG TDIWVGARPP
TDLDAFGRSD SEGSDSKMQI MDAFLWGRCL TEDEVAMLHT AICSAEYGLF DLAAEDAWHG
SYSARVDDWE SEEANFELYD QEDVEWDGQY SSGRKRHARD SVAIDIDSFA RRPRKPRFET
REEVNQRMLS VERAVREALI AKGERNFTDQ EFPPDDRSLF VDPMNPSLKL QVVSEWMRPS
DIAKEVSISS QPCLFSGSVN SSDVCQGRLG DCWFLSAVAV LTEMARISEV IITPEYNEEG
IYTVRFCIQG EWVAVVVDDW IPCESPGKPA FATSRKQNEL WVSILEKAYA KLHGSYEALE
GGLVQDALVD LTGGAGEEID MRSPQAQIDL ASGRLWSQLL HFKQEGFLLG AGSPSGSDAH
ISSSGIVQGH AYSILQVREV DGHKLVQIRN PWANEVEWNG PWSDSSQEWT ERMKHKLKHV
PQSKNGVFWM SWQDFQIHFR SIYVCRVYPP EMRYSVHGQW RGYSAGGCQD YDSWHQNPQY
RLRVTGRDAL YPVHVFITLT QGVGFSRKTN GFRNYQSSHD SSMFYIGMRI LKTRGCRAAY
NIYMHESVGG TDYVNSREIS CELVLEPYPK GYTIVPTTIH PGEEAPFVLS VFTKAPIKLE
AV


Related products :

Catalog number Product name Quantity
EIAAB10617 DCN1-like protein 1,DCUN1 domain-containing protein 1,Dcun1d1,Dcun1l1,Defective in cullin neddylation protein 1-like protein 1,Mouse,Mus musculus,Rp42,Tes3,Testis-specific protein 3
EIAAB09655 Cardiac LIM protein,CLP,CRP3,CSRP3,Cysteine and glycine-rich protein 3,Cysteine-rich protein 3,Homo sapiens,Human,LIM domain protein, cardiac,MLP,Muscle LIM protein
EIAAB09656 Clp,CRP3,Csrp3,Cysteine and glycine-rich protein 3,Cysteine-rich protein 3,LIM domain protein, cardiac,Mlp,Mouse,Mus musculus,Muscle LIM protein
EIAAB09658 Clp,CRP3,Csrp3,Cysteine and glycine-rich protein 3,Cysteine-rich protein 3,LIM domain protein, cardiac,Mlp,Muscle LIM protein,Rat,Rattus norvegicus
orb80283 Human Pro-NGF protein Pro NGF is the pro-form of the neurotrophin NGF. Like the mature protein pro NGF is characterized by the cysteine knot motif consisting of three cysteine bridges. The protein pre 2
EIAAB10624 DCN1-like protein 4,DCUN1 domain-containing protein 4,Dcun1d4,Defective in cullin neddylation protein 1-like protein 4,Mouse,Mus musculus
EIAAB10628 DCN1-like protein 5,DCUN1 domain-containing protein 5,Dcun1d5,Defective in cullin neddylation protein 1-like protein 5,Rat,Rattus norvegicus
EIAAB10626 Bos taurus,Bovine,DCN1-like protein 5,DCUN1 domain-containing protein 5,DCUN1D5,Defective in cullin neddylation protein 1-like protein 5
EIAAB10627 DCN1-like protein 5,DCUN1 domain-containing protein 5,Dcun1d5,Defective in cullin neddylation protein 1-like protein 5,Mouse,Mus musculus
EIAAB10621 Bos taurus,Bovine,DCN1-like protein 3,DCUN1 domain-containing protein 3,DCUN1D3,Defective in cullin neddylation protein 1-like protein 3
EIAAB10620 DCN1-like protein 3,DCUN1 domain-containing protein 3,Dcun1d3,Defective in cullin neddylation protein 1-like protein 3,Rat,Rattus norvegicus
EIAAB10623 DCN1-like protein 3,DCUN1 domain-containing protein 3,Dcun1d3,Defective in cullin neddylation protein 1-like protein 3,Mouse,Mus musculus
EIAAB10622 DCN1-like protein 3,DCUN1 domain-containing protein 3,DCUN1D3,Defective in cullin neddylation protein 1-like protein 3,Homo sapiens,Human
EIAAB10619 DCN1-like protein 2,DCUN1 domain-containing protein 2,Dcun1d2,Dcun1l2,Defective in cullin neddylation protein 1-like protein 2,Mouse,Mus musculus
EIAAB10629 DCN1-like protein 5,DCUN1 domain-containing protein 5,DCUN1D5,Defective in cullin neddylation protein 1-like protein 5,Homo sapiens,Human
15-288-21280 Cysteine and glycine-rich protein 2 - Cysteine-rich protein 2; CRP2; Smooth muscle cell LIM protein; SmLIM; LIM-only protein 5 Polyclonal 0.05 mg
15-288-21280 Cysteine and glycine-rich protein 2 - Cysteine-rich protein 2; CRP2; Smooth muscle cell LIM protein; SmLIM; LIM-only protein 5 Polyclonal 0.1 mg
EIAAB10625 DCN1-like protein 4,DCUN1 domain-containing protein 4,DCUN1D4,Defective in cullin neddylation protein 1-like protein 4,Homo sapiens,Human,KIAA0276
EIAAB10618 C13orf17,DCN1-like protein 2,DCUN1 domain-containing protein 2,DCUN1D2,DCUN1L2,Defective in cullin neddylation protein 1-like protein 2,Homo sapiens,Human
18-003-42492 Cysteine and glycine-rich protein 3 - Cysteine-rich protein 3; CRP3; LIM domain protein. cardiac; Muscle LIM protein Polyclonal 0.05 mg Aff Pur
18-003-43112 Cysteine and glycine-rich protein 3 - Cysteine-rich protein 3; CRP3; LIM domain protein. cardiac; Muscle LIM protein Polyclonal 0.1 mg Protein A
18-003-42491 Cysteine and glycine-rich protein 3 - Cysteine-rich protein 3; CRP3; LIM domain protein. cardiac; Muscle LIM protein Polyclonal 0.05 mg Aff Pur
15-288-22036F Cysteine and glycine-rich protein 3 - Cysteine-rich protein 3; CRP3; LIM domain protein. cardiac; Muscle LIM protein Polyclonal 0.1 mg
18-003-43112 Cysteine and glycine-rich protein 3 - Cysteine-rich protein 3; CRP3; LIM domain protein. cardiac; Muscle LIM protein Polyclonal 0.05 mg Aff Pur
15-288-22036F Cysteine and glycine-rich protein 3 - Cysteine-rich protein 3; CRP3; LIM domain protein. cardiac; Muscle LIM protein Polyclonal 0.05 mg


 

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