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

Adenylyltransferase and sulfurtransferase MOCS3 (Molybdenum cofactor synthesis protein 3) (Molybdopterin synthase sulfurylase) (MPT synthase sulfurylase) [Includes: Molybdopterin-synthase adenylyltransferase (EC 2.7.7.80) (Adenylyltransferase MOCS3) (Sulfur carrier protein MOCS2A adenylyltransferase); Molybdopterin-synthase sulfurtransferase (EC 2.8.1.11) (Sulfur carrier protein MOCS2A sulfurtransferase) (Sulfurtransferase MOCS3)]

 MOCS3_HUMAN             Reviewed;         460 AA.
O95396;
26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
20-JUN-2018, entry version 161.
RecName: Full=Adenylyltransferase and sulfurtransferase MOCS3 {ECO:0000255|HAMAP-Rule:MF_03049};
AltName: Full=Molybdenum cofactor synthesis protein 3 {ECO:0000255|HAMAP-Rule:MF_03049};
AltName: Full=Molybdopterin synthase sulfurylase;
Short=MPT synthase sulfurylase;
Includes:
RecName: Full=Molybdopterin-synthase adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_03049};
EC=2.7.7.80 {ECO:0000255|HAMAP-Rule:MF_03049, ECO:0000269|PubMed:15073332, ECO:0000269|PubMed:17459099, ECO:0000269|PubMed:18650437};
AltName: Full=Adenylyltransferase MOCS3 {ECO:0000255|HAMAP-Rule:MF_03049};
AltName: Full=Sulfur carrier protein MOCS2A adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_03049};
Includes:
RecName: Full=Molybdopterin-synthase sulfurtransferase {ECO:0000255|HAMAP-Rule:MF_03049};
EC=2.8.1.11 {ECO:0000255|HAMAP-Rule:MF_03049, ECO:0000269|PubMed:15073332, ECO:0000269|PubMed:17459099, ECO:0000269|PubMed:18650437};
AltName: Full=Sulfur carrier protein MOCS2A sulfurtransferase {ECO:0000255|HAMAP-Rule:MF_03049};
AltName: Full=Sulfurtransferase MOCS3 {ECO:0000255|HAMAP-Rule:MF_03049};
Name=MOCS3 {ECO:0000255|HAMAP-Rule:MF_03049};
Synonyms=UBA4 {ECO:0000255|HAMAP-Rule:MF_03049};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
FUNCTION IN BIOSYNTHESIS OF THE MOLYBDENUM COFACTOR, CATALYTIC
ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF CYS-239; CYS-316; CYS-324; CYS-365 AND CYS-412.
PubMed=15073332; DOI=10.1073/pnas.0308191101;
Matthies A., Rajagopalan K.V., Mendel R.R., Leimkuehler S.;
"Evidence for the physiological role of a rhodanese-like protein for
the biosynthesis of the molybdenum cofactor in humans.";
Proc. Natl. Acad. Sci. U.S.A. 101:5946-5951(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Uterus;
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]
ACTIVE SITE, AND DISULFIDE BOND.
PubMed=15910006; DOI=10.1021/bi0503448;
Matthies A., Nimtz M., Leimkuehler S.;
"Molybdenum cofactor biosynthesis in humans: identification of a
persulfide group in the rhodanese-like domain of MOCS3 by mass
spectrometry.";
Biochemistry 44:7912-7920(2005).
[5]
ENZYME ACTIVITY, AND MUTAGENESIS OF LYS-413; LEU-414; GLY-415;
ASN-416; ASP-417; PRO-458 AND TYR-460.
PubMed=17459099; DOI=10.1111/j.1742-4658.2007.05811.x;
Krepinsky K., Leimkuehler S.;
"Site-directed mutagenesis of the active site loop of the rhodanese-
like domain of the human molybdopterin synthase sulfurase MOCS3. Major
differences in substrate specificity between eukaryotic and bacterial
homologs.";
FEBS J. 274:2778-2787(2007).
[6]
ENZYME ACTIVITY, AND INTERACTION WITH NFS1.
PubMed=18650437; DOI=10.1074/jbc.M804064200;
Marelja Z., Stoecklein W., Nimtz M., Leimkuehler S.;
"A novel role for human Nfs1 in the cytoplasm: Nfs1 acts as a sulfur
donor for MOCS3, a protein involved in molybdenum cofactor
biosynthesis.";
J. Biol. Chem. 283:25178-25185(2008).
[7]
FUNCTION IN 2-THIOLATION OF TRNA.
PubMed=19017811; DOI=10.1073/pnas.0808756105;
Schlieker C.D., Van der Veen A.G., Damon J.R., Spooner E.,
Ploegh H.L.;
"A functional proteomics approach links the ubiquitin-related modifier
Urm1 to a tRNA modification pathway.";
Proc. Natl. Acad. Sci. U.S.A. 105:18255-18260(2008).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[9]
X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 335-460.
Structural genomics consortium (SGC);
"Crystal structure of the human MOCS3 rhodanese-like domain.";
Submitted (JUL-2009) to the PDB data bank.
-!- FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at
tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and
tRNA(Gln). Also essential during biosynthesis of the molybdenum
cofactor. Acts by mediating the C-terminal thiocarboxylation of
sulfur carriers URM1 and MOCS2A. Its N-terminus first activates
URM1 and MOCS2A as acyl-adenylates (-COAMP), then the persulfide
sulfur on the catalytic cysteine is transferred to URM1 and MOCS2A
to form thiocarboxylation (-COSH) of their C-terminus. The
reaction probably involves hydrogen sulfide that is generated from
the persulfide intermediate and that acts as nucleophile towards
URM1 and MOCS2A. Subsequently, a transient disulfide bond is
formed. Does not use thiosulfate as sulfur donor; NFS1 probably
acting as a sulfur donor for thiocarboxylation reactions.
{ECO:0000255|HAMAP-Rule:MF_03049, ECO:0000269|PubMed:15073332,
ECO:0000269|PubMed:19017811}.
-!- CATALYTIC ACTIVITY: ATP + [molybdopterin-synthase sulfur-carrier
protein]-Gly-Gly = diphosphate + [molybdopterin-synthase sulfur-
carrier protein]-Gly-Gly-AMP. {ECO:0000255|HAMAP-Rule:MF_03049,
ECO:0000269|PubMed:15073332, ECO:0000269|PubMed:17459099,
ECO:0000269|PubMed:18650437}.
-!- CATALYTIC ACTIVITY: [Molybdopterin-synthase sulfur-carrier
protein]-Gly-Gly-AMP + [cysteine desulfurase]-S-sulfanyl-L-
cysteine + reduced acceptor = AMP + [molybdopterin-synthase
sulfur-carrier protein]-Gly-NH-CH(2)-C(O)SH + [cysteine
desulfurase] + oxidized acceptor. {ECO:0000255|HAMAP-
Rule:MF_03049, ECO:0000269|PubMed:15073332,
ECO:0000269|PubMed:17459099, ECO:0000269|PubMed:18650437}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000255|HAMAP-Rule:MF_03049};
Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-
Rule:MF_03049};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.25 mM for thiosulfate {ECO:0000269|PubMed:15073332};
KM=0.28 mM for cyanide {ECO:0000269|PubMed:15073332};
-!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-
tRNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03049}.
-!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
{ECO:0000255|HAMAP-Rule:MF_03049}.
-!- SUBUNIT: Interacts with NFS1. {ECO:0000255|HAMAP-Rule:MF_03049,
ECO:0000269|PubMed:18650437}.
-!- INTERACTION:
Q9BTM9:URM1; NbExp=4; IntAct=EBI-373206, EBI-714589;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03049,
ECO:0000269|PubMed:15073332}.
-!- SIMILARITY: In the N-terminal section; belongs to the
HesA/MoeB/ThiF family. UBA4 subfamily. {ECO:0000255|HAMAP-
Rule:MF_03049}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF102544; AAC72412.1; -; mRNA.
EMBL; AL034553; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC015939; AAH15939.1; -; mRNA.
CCDS; CCDS13435.1; -.
RefSeq; NP_055299.1; NM_014484.4.
UniGene; Hs.159410; -.
UniGene; Hs.736268; -.
PDB; 3I2V; X-ray; 1.25 A; A=335-460.
PDBsum; 3I2V; -.
ProteinModelPortal; O95396; -.
SMR; O95396; -.
BioGrid; 118127; 22.
DIP; DIP-31168N; -.
IntAct; O95396; 2.
STRING; 9606.ENSP00000244051; -.
iPTMnet; O95396; -.
PhosphoSitePlus; O95396; -.
EPD; O95396; -.
MaxQB; O95396; -.
PaxDb; O95396; -.
PeptideAtlas; O95396; -.
PRIDE; O95396; -.
ProteomicsDB; 50847; -.
DNASU; 27304; -.
Ensembl; ENST00000244051; ENSP00000244051; ENSG00000124217.
GeneID; 27304; -.
KEGG; hsa:27304; -.
UCSC; uc002xvy.3; human.
CTD; 27304; -.
EuPathDB; HostDB:ENSG00000124217.4; -.
GeneCards; MOCS3; -.
HGNC; HGNC:15765; MOCS3.
MIM; 609277; gene.
neXtProt; NX_O95396; -.
OpenTargets; ENSG00000124217; -.
PharmGKB; PA30904; -.
eggNOG; KOG2017; Eukaryota.
eggNOG; COG0476; LUCA.
eggNOG; COG0607; LUCA.
GeneTree; ENSGT00920000149174; -.
HOGENOM; HOG000281219; -.
HOVERGEN; HBG052491; -.
InParanoid; O95396; -.
KO; K11996; -.
OMA; MAWAAKI; -.
OrthoDB; EOG091G0EQP; -.
PhylomeDB; O95396; -.
TreeFam; TF106103; -.
BioCyc; MetaCyc:HS04742-MONOMER; -.
BRENDA; 2.7.7.80; 2681.
BRENDA; 2.8.1.11; 2681.
Reactome; R-HSA-947581; Molybdenum cofactor biosynthesis.
UniPathway; UPA00344; -.
UniPathway; UPA00988; -.
EvolutionaryTrace; O95396; -.
GeneWiki; MOCS3; -.
GenomeRNAi; 27304; -.
PRO; PR:O95396; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000124217; -.
CleanEx; HS_MOCS3; -.
Genevisible; O95396; HS.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0061605; F:molybdopterin-synthase adenylyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0061604; F:molybdopterin-synthase sulfurtransferase activity; IEA:UniProtKB-EC.
GO; GO:0016779; F:nucleotidyltransferase activity; IDA:UniProtKB.
GO; GO:0016783; F:sulfurtransferase activity; IDA:UniProtKB.
GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IMP:UniProtKB.
GO; GO:0042292; F:URM1 activating enzyme activity; IDA:UniProtKB.
GO; GO:0018192; P:enzyme active site formation via cysteine modification to L-cysteine persulfide; IDA:UniProtKB.
GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IDA:UniProtKB.
GO; GO:0032324; P:molybdopterin cofactor biosynthetic process; TAS:Reactome.
GO; GO:0032447; P:protein urmylation; IBA:GO_Central.
GO; GO:0034227; P:tRNA thio-modification; IDA:UniProtKB.
GO; GO:0002143; P:tRNA wobble position uridine thiolation; IBA:GO_Central.
GO; GO:0002098; P:tRNA wobble uridine modification; IDA:UniProtKB.
Gene3D; 3.40.250.10; -; 1.
HAMAP; MF_03049; MOCS3_Uba4; 1.
InterPro; IPR028885; MOCS3/Uba4.
InterPro; IPR001763; Rhodanese-like_dom.
InterPro; IPR036873; Rhodanese-like_dom_sf.
InterPro; IPR000594; ThiF_NAD_FAD-bd.
InterPro; IPR035985; Ubiquitin-activating_enz.
Pfam; PF00581; Rhodanese; 1.
Pfam; PF00899; ThiF; 1.
SMART; SM00450; RHOD; 1.
SUPFAM; SSF69572; SSF69572; 1.
PROSITE; PS50206; RHODANESE_3; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Complete proteome; Cytoplasm;
Disulfide bond; Metal-binding; Molybdenum cofactor biosynthesis;
Multifunctional enzyme; Nucleotide-binding; Polymorphism;
Reference proteome; Transferase; tRNA processing; Zinc.
CHAIN 1 460 Adenylyltransferase and sulfurtransferase
MOCS3.
/FTId=PRO_0000120583.
DOMAIN 347 458 Rhodanese. {ECO:0000255|HAMAP-
Rule:MF_03049}.
NP_BIND 120 124 ATP. {ECO:0000255|HAMAP-Rule:MF_03049}.
NP_BIND 181 182 ATP. {ECO:0000255|HAMAP-Rule:MF_03049}.
ACT_SITE 239 239 Glycyl thioester intermediate; for
adenylyltransferase activity.
{ECO:0000255|HAMAP-Rule:MF_03049}.
ACT_SITE 412 412 Cysteine persulfide intermediate; for
sulfurtransferase activity.
{ECO:0000255|HAMAP-Rule:MF_03049,
ECO:0000269|PubMed:15910006}.
METAL 222 222 Zinc. {ECO:0000255|HAMAP-Rule:MF_03049}.
METAL 225 225 Zinc. {ECO:0000255|HAMAP-Rule:MF_03049}.
METAL 297 297 Zinc. {ECO:0000255|HAMAP-Rule:MF_03049}.
METAL 300 300 Zinc. {ECO:0000255|HAMAP-Rule:MF_03049}.
BINDING 92 92 ATP; via amide nitrogen.
{ECO:0000255|HAMAP-Rule:MF_03049}.
BINDING 113 113 ATP. {ECO:0000255|HAMAP-Rule:MF_03049}.
BINDING 137 137 ATP. {ECO:0000255|HAMAP-Rule:MF_03049}.
DISULFID 316 324 {ECO:0000269|PubMed:15910006}.
VARIANT 429 429 S -> A (in dbSNP:rs7269297).
/FTId=VAR_049349.
MUTAGEN 239 239 C->A: Impairs sulfurtransferase activity.
{ECO:0000269|PubMed:15073332}.
MUTAGEN 316 316 C->A: Does not affect sulfurtransferase
activity. {ECO:0000269|PubMed:15073332}.
MUTAGEN 324 324 C->A: Does not affect sulfurtransferase
activity. {ECO:0000269|PubMed:15073332}.
MUTAGEN 365 365 C->A: Does not affect sulfurtransferase
activity. {ECO:0000269|PubMed:15073332}.
MUTAGEN 412 412 C->A: Abolishes sulfurtransferase
activity. {ECO:0000269|PubMed:15073332}.
MUTAGEN 413 413 K->R: Does not affect sulfurtransferase
specificity and activity.
{ECO:0000269|PubMed:17459099}.
MUTAGEN 414 414 L->K: Does not affect sulfurtransferase
specificity and activity.
{ECO:0000269|PubMed:17459099}.
MUTAGEN 415 415 G->A: Does not affect sulfurtransferase
specificity and activity.
{ECO:0000269|PubMed:17459099}.
MUTAGEN 416 416 N->V: Does not affect sulfurtransferase
specificity and activity.
{ECO:0000269|PubMed:17459099}.
MUTAGEN 417 417 D->R: Results in 470-fold increased
activity. {ECO:0000269|PubMed:17459099}.
MUTAGEN 417 417 D->T: Results in 90-fold increased
activity. {ECO:0000269|PubMed:17459099}.
MUTAGEN 458 458 P->G: Does not affect sulfurtransferase
specificity and activity.
{ECO:0000269|PubMed:17459099}.
MUTAGEN 460 460 Y->A: Does not affect sulfurtransferase
specificity and activity.
{ECO:0000269|PubMed:17459099}.
HELIX 338 347 {ECO:0000244|PDB:3I2V}.
STRAND 352 355 {ECO:0000244|PDB:3I2V}.
HELIX 359 364 {ECO:0000244|PDB:3I2V}.
STRAND 370 372 {ECO:0000244|PDB:3I2V}.
HELIX 375 379 {ECO:0000244|PDB:3I2V}.
HELIX 383 397 {ECO:0000244|PDB:3I2V}.
STRAND 406 411 {ECO:0000244|PDB:3I2V}.
STRAND 413 416 {ECO:0000244|PDB:3I2V}.
HELIX 417 430 {ECO:0000244|PDB:3I2V}.
STRAND 433 435 {ECO:0000244|PDB:3I2V}.
STRAND 437 442 {ECO:0000244|PDB:3I2V}.
HELIX 445 452 {ECO:0000244|PDB:3I2V}.
SEQUENCE 460 AA; 49669 MW; 299A4E755173E324 CRC64;
MASREEVLAL QAEVAQREEE LNSLKQKLAS ALLAEQEPQP ERLVPVSPLP PKAALSRDEI
LRYSRQLVLP ELGVHGQLRL GTACVLIVGC GGLGCPLAQY LAAAGVGRLG LVDYDVVEMS
NLARQVLHGE ALAGQAKAFS AAASLRRLNS AVECVPYTQA LTPATALDLV RRYDVVADCS
DNVPTRYLVN DACVLAGRPL VSASALRFEG QITVYHYDGG PCYRCIFPQP PPAETVTNCA
DGGVLGVVTG VLGCLQALEV LKIAAGLGPS YSGSLLLFDA LRGHFRSIRL RSRRLDCAAC
GERPTVTDLL DYEAFCGSSA TDKCRSLQLL SPEERVSVTD YKRLLDSGAF HLLLDVRPQV
EVDICRLPHA LHIPLKHLER RDAESLKLLK EAIWEEKQGT QEGAAVPIYV ICKLGNDSQK
AVKILQSLSA AQELDPLTVR DVVGGLMAWA AKIDGTFPQY


Related products :

Catalog number Product name Quantity
EIAAB25090 Adenylyltransferase and sulfurtransferase MOCS3,Homo sapiens,Human,MOCS3,Molybdenum cofactor synthesis protein 3,Molybdopterin synthase sulfurylase,MPT synthase sulfurylase,UBA4
EIAAB25092 Adenylyltransferase and sulfurtransferase MOCS3,MOCS3,Molybdenum cofactor synthesis protein 3,Pig,Sus scrofa,UBA4
EIAAB25093 Adenylyltransferase and sulfurtransferase MOCS3,Mocs3,Molybdenum cofactor synthesis protein 3,Mouse,Mus musculus,Uba4
EIAAB25091 Adenylyltransferase and sulfurtransferase MOCS3,Bos taurus,Bovine,MOCS3,Molybdenum cofactor synthesis protein 3,UBA4
EIAAB25078 Homo sapiens,Human,MOCO1,MOCO1-A,MOCS2,MOCS2A,Molybdenum cofactor synthesis protein 2 small subunit,Molybdenum cofactor synthesis protein 2A,Molybdopterin synthase sulfur carrier subunit,Molybdopterin
EIAAB25079 Mocs2,MOCS2A,Molybdenum cofactor synthesis protein 2 small subunit,Molybdenum cofactor synthesis protein 2A,Molybdopterin synthase sulfur carrier subunit,Mouse,Mus musculus,Sulfur carrier protein MOCS
MOCS3_BOVIN ELISA Kit FOR Adenylyltransferase and sulfurtransferase MOCS3; organism: Bovine; gene name: MOCS3 96T
CSB-EL014707HU Human Adenylyltransferase and sulfurtransferase MOCS3(MOCS3) ELISA kit SpeciesHuman 96T
CSB-EL014707MO Mouse Adenylyltransferase and sulfurtransferase MOCS3(MOCS3) ELISA kit SpeciesMouse 96T
CSB-EL014707BO Bovine Adenylyltransferase and sulfurtransferase MOCS3(MOCS3) ELISA kit SpeciesBovine 96T
CSB-EL014707PI Pig Adenylyltransferase and sulfurtransferase MOCS3(MOCS3) ELISA kit SpeciesPig 96T
CSB-EL014707BO Bovine Adenylyltransferase and sulfurtransferase MOCS3(MOCS3) ELISA kit 96T
CSB-EL014707MO Mouse Adenylyltransferase and sulfurtransferase MOCS3(MOCS3) ELISA kit 96T
CSB-EL014707HU Human Adenylyltransferase and sulfurtransferase MOCS3(MOCS3) ELISA kit 96T
E0536m Mouse ELISA Kit FOR Adenylyltransferase and sulfurtransferase MOCS3 96T
MOCS3_BOVIN Bovine ELISA Kit FOR Adenylyltransferase and sulfurtransferase MOCS3 96T
PTHD1_HUMAN Mouse ELISA Kit FOR Adenylyltransferase and sulfurtransferase MOCS3 96T
MOC2A_MOUSE ELISA Kit FOR Molybdopterin synthase sulfur carrier subunit; organism: Mouse; gene name: Mocs2 96T
EIAAB25083 Bos taurus,Bovine,MOCS2,MOCS2B,Molybdenum cofactor synthesis protein 2 large subunit,Molybdenum cofactor synthesis protein 2B,Molybdopterin synthase catalytic subunit
EIAAB25080 Mocs2,MOCS2B,Molybdenum cofactor synthesis protein 2 large subunit,Molybdenum cofactor synthesis protein 2B,Molybdopterin synthase catalytic subunit,Rat,Rattus norvegicus
EIAAB25082 Mocs2,MOCS2B,Molybdenum cofactor synthesis protein 2 large subunit,Molybdenum cofactor synthesis protein 2B,Molybdopterin synthase catalytic subunit,Mouse,Mus musculus
CSB-EL009716RA Rat Gephyrin [Includes: Molybdopterin adenylyltransferase(GPHN) ELISA kit 96T
EIAAB27400 Kiaa0479,Mouse,Mus musculus,NaMN adenylyltransferase 1,Nicotinamide mononucleotide adenylyltransferase 2,Nicotinate-nucleotide adenylyltransferase 1,NMN adenylyltransferase 2,Nmnat2
EIAAB27398 D4Cole1e,Mouse,Mus musculus,NaMN adenylyltransferase 1,Nicotinamide mononucleotide adenylyltransferase 1,Nicotinate-nucleotide adenylyltransferase 1,NMN adenylyltransferase 1,Nmnat,Nmnat1
EIAAB27397 Homo sapiens,Human,NaMN adenylyltransferase 1,Nicotinamide mononucleotide adenylyltransferase 1,Nicotinate-nucleotide adenylyltransferase 1,NMN adenylyltransferase 1,NMNAT,NMNAT1


 

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