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Carbonic anhydrase 12 (EC 4.2.1.1) (Carbonate dehydratase XII) (Carbonic anhydrase XII) (CA-XII) (Tumor antigen HOM-RCC-3.1.3)

 CAH12_HUMAN             Reviewed;         354 AA.
O43570; B2RE24; Q53YE5; Q9BWG2;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
25-OCT-2017, entry version 170.
RecName: Full=Carbonic anhydrase 12;
EC=4.2.1.1;
AltName: Full=Carbonate dehydratase XII;
AltName: Full=Carbonic anhydrase XII;
Short=CA-XII;
AltName: Full=Tumor antigen HOM-RCC-3.1.3;
Flags: Precursor;
Name=CA12;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHARACTERIZATION.
TISSUE=Renal cell carcinoma;
PubMed=9636197; DOI=10.1073/pnas.95.13.7608;
Tuereci O., Sahin U., Vollmar E., Siemer S., Goettert E., Seitz G.,
Parkkila A.-K., Shah G.N., Grubb J.H., Pfreundschuh M., Sly W.S.;
"Human carbonic anhydrase XII: cDNA cloning, expression, and
chromosomal localization of a carbonic anhydrase gene that is
overexpressed in some renal cell cancers.";
Proc. Natl. Acad. Sci. U.S.A. 95:7608-7613(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Lung;
PubMed=9770531; DOI=10.1073/pnas.95.21.12596;
Ivanov S.V., Kuzmin I., Wei M.-H., Pack S., Geil L., Johnson B.E.,
Stanbridge E.J., Lerman M.I.;
"Down-regulation of transmembrane carbonic anhydrases in renal cell
carcinoma cell lines by wild-type von Hippel-Lindau transgenes.";
Proc. Natl. Acad. Sci. U.S.A. 95:12596-12601(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Eye, and Kidney;
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]
ENZYME REGULATION.
PubMed=17705204; DOI=10.1002/anie.200701189;
Koehler K., Hillebrecht A., Schulze Wischeler J., Innocenti A.,
Heine A., Supuran C.T., Klebe G.;
"Saccharin inhibits carbonic anhydrases: possible explanation for its
unpleasant metallic aftertaste.";
Angew. Chem. Int. Ed. Engl. 46:7697-7699(2007).
[7]
ENZYME REGULATION.
PubMed=17314045; DOI=10.1016/j.bmcl.2007.01.113;
Temperini C., Innocenti A., Guerri A., Scozzafava A., Rusconi S.,
Supuran C.T.;
"Phosph(on)ate as a zinc-binding group in metalloenzyme inhibitors: X-
ray crystal structure of the antiviral drug foscarnet complexed to
human carbonic anhydrase I.";
Bioorg. Med. Chem. Lett. 17:2210-2215(2007).
[8]
ENZYME REGULATION.
PubMed=17407288; DOI=10.1021/ja068359w;
Srivastava D.K., Jude K.M., Banerjee A.L., Haldar M., Manokaran S.,
Kooren J., Mallik S., Christianson D.W.;
"Structural analysis of charge discrimination in the binding of
inhibitors to human carbonic anhydrases I and II.";
J. Am. Chem. Soc. 129:5528-5537(2007).
[9]
ENZYME REGULATION.
PubMed=19186056; DOI=10.1016/j.bmcl.2009.01.038;
Crocetti L., Maresca A., Temperini C., Hall R.A., Scozzafava A.,
Muehlschlegel F.A., Supuran C.T.;
"A thiabendazole sulfonamide shows potent inhibitory activity against
mammalian and nematode alpha-carbonic anhydrases.";
Bioorg. Med. Chem. Lett. 19:1371-1375(2009).
[10]
ENZYME REGULATION.
PubMed=19206230; DOI=10.1021/ja809683v;
Maresca A., Temperini C., Vu H., Pham N.B., Poulsen S.-A.,
Scozzafava A., Quinn R.J., Supuran C.T.;
"Non-zinc mediated inhibition of carbonic anhydrases: coumarins are a
new class of suicide inhibitors.";
J. Am. Chem. Soc. 131:3057-3062(2009).
[11]
BIOPHYSICOCHEMICAL PROPERTIES, AND ENZYME REGULATION.
PubMed=18618712; DOI=10.1002/prot.22144;
Di Fiore A., Monti S.M., Hilvo M., Parkkila S., Romano V., Scaloni A.,
Pedone C., Scozzafava A., Supuran C.T., De Simone G.;
"Crystal structure of human carbonic anhydrase XIII and its complex
with the inhibitor acetazolamide.";
Proteins 74:164-175(2009).
[12]
X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 30-291 IN COMPLEX WITH ZINC
ION AND THE INHIBITOR ACETAZOLAMIDE, DISULFIDE BOND, AND SUBUNIT.
PubMed=11493685; DOI=10.1073/pnas.161301298;
Whittington D.A., Waheed A., Ulmasov B., Shah G.N., Grubb J.H.,
Sly W.S., Christianson D.W.;
"Crystal structure of the dimeric extracellular domain of human
carbonic anhydrase XII, a bitopic membrane protein overexpressed in
certain cancer tumor cells.";
Proc. Natl. Acad. Sci. U.S.A. 98:9545-9550(2001).
[13]
VARIANT HCHLH LYS-143.
PubMed=21035102; DOI=10.1016/j.ajhg.2010.10.008;
Feldshtein M., Elkrinawi S., Yerushalmi B., Marcus B., Vullo D.,
Romi H., Ofir R., Landau D., Sivan S., Supuran C.T., Birk O.S.;
"Hyperchlorhidrosis caused by homozygous mutation in CA12, encoding
carbonic anhydrase XII.";
Am. J. Hum. Genet. 87:713-720(2010).
-!- FUNCTION: Reversible hydration of carbon dioxide.
-!- CATALYTIC ACTIVITY: H(2)CO(3) = CO(2) + H(2)O.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:11493685};
-!- ENZYME REGULATION: Inhibited by coumarins, saccharin, sulfonamide
derivatives such as acetazolamide (AZA), benzenesulfonamide and
derivatives (4-carboxyethylbenzene-sulfonamide, 4-
carboxyethylbenzene-sulfonamide ethyl ester, 4-(acetyl-2-
aminoethyl)benzene-sulfonamide, 4-aminoethylbenzene-sulfonamide)
and Foscarnet (phosphonoformate trisodium salt).
{ECO:0000269|PubMed:17314045, ECO:0000269|PubMed:17407288,
ECO:0000269|PubMed:17705204, ECO:0000269|PubMed:18618712,
ECO:0000269|PubMed:19186056, ECO:0000269|PubMed:19206230}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=12.0 mM for CO(2) {ECO:0000269|PubMed:18618712};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11493685}.
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O43570-1; Sequence=Displayed;
Name=2;
IsoId=O43570-2; Sequence=VSP_000772;
-!- TISSUE SPECIFICITY: Highly expressed in colon, kidney, prostate,
intestine and activated lymphocytes. Expressed at much higher
levels in the renal cell cancers than in surrounding normal kidney
tissue. Moderately expressed in pancreas, ovary and testis.
-!- DISEASE: Hyperchlorhidrosis, isolated (HCHLH) [MIM:143860]: A
disorder characterized by excessive sweating and increased sweat
chloride levels. Affected individuals suffer from episodes of
hyponatremic dehydration and report increased amounts of visible
salt precipitates in sweat. {ECO:0000269|PubMed:21035102}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
{ECO:0000305}.
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EMBL; AF051882; AAC39789.1; -; mRNA.
EMBL; AF037335; AAC63952.1; -; mRNA.
EMBL; BT006656; AAP35302.1; -; mRNA.
EMBL; AK315769; BAG38121.1; -; mRNA.
EMBL; BC000278; AAH00278.1; -; mRNA.
EMBL; BC011691; AAH11691.1; -; mRNA.
EMBL; BC023981; AAH23981.1; -; mRNA.
CCDS; CCDS10185.1; -. [O43570-1]
CCDS; CCDS10186.1; -. [O43570-2]
RefSeq; NP_001209.1; NM_001218.4. [O43570-1]
RefSeq; NP_996808.1; NM_206925.2. [O43570-2]
UniGene; Hs.210995; -.
UniGene; Hs.603780; -.
PDB; 1JCZ; X-ray; 1.55 A; A/B=30-291.
PDB; 1JD0; X-ray; 1.50 A; A/B=30-291.
PDB; 4HT2; X-ray; 1.45 A; A/B/C/D=30-291.
PDB; 4KP5; X-ray; 1.45 A; A/B/C/D=30-291.
PDB; 4KP8; X-ray; 1.80 A; A/B/C/D=30-291.
PDB; 4Q0L; X-ray; 2.00 A; A/B/C/D=30-291.
PDB; 4QJ0; X-ray; 1.55 A; A/B/C/D=30-291.
PDB; 4QJO; X-ray; 1.80 A; A/B/C/D=30-291.
PDB; 4QJW; X-ray; 1.55 A; A/B/C/D=30-291.
PDB; 4WW8; X-ray; 1.42 A; A/B/C/D=30-291.
PDB; 5LL5; X-ray; 1.42 A; A/B/C/D=30-291.
PDB; 5LL9; X-ray; 1.45 A; A/B/C/D=30-291.
PDB; 5LLO; X-ray; 1.60 A; A/B/C/D=30-291.
PDB; 5LLP; X-ray; 1.48 A; A/B/C/D=30-291.
PDBsum; 1JCZ; -.
PDBsum; 1JD0; -.
PDBsum; 4HT2; -.
PDBsum; 4KP5; -.
PDBsum; 4KP8; -.
PDBsum; 4Q0L; -.
PDBsum; 4QJ0; -.
PDBsum; 4QJO; -.
PDBsum; 4QJW; -.
PDBsum; 4WW8; -.
PDBsum; 5LL5; -.
PDBsum; 5LL9; -.
PDBsum; 5LLO; -.
PDBsum; 5LLP; -.
ProteinModelPortal; O43570; -.
SMR; O43570; -.
BioGrid; 107225; 8.
IntAct; O43570; 10.
MINT; MINT-1392387; -.
STRING; 9606.ENSP00000178638; -.
BindingDB; O43570; -.
ChEMBL; CHEMBL3242; -.
DrugBank; DB00562; Benzthiazide.
DrugBank; DB08846; Ellagic Acid.
DrugBank; DB00999; Hydrochlorothiazide.
DrugBank; DB00774; Hydroflumethiazide.
DrugBank; DB00909; Zonisamide.
GuidetoPHARMACOLOGY; 2747; -.
iPTMnet; O43570; -.
PhosphoSitePlus; O43570; -.
BioMuta; CA12; -.
MaxQB; O43570; -.
PaxDb; O43570; -.
PeptideAtlas; O43570; -.
PRIDE; O43570; -.
DNASU; 771; -.
Ensembl; ENST00000178638; ENSP00000178638; ENSG00000074410. [O43570-1]
Ensembl; ENST00000344366; ENSP00000343088; ENSG00000074410. [O43570-2]
GeneID; 771; -.
KEGG; hsa:771; -.
UCSC; uc002amc.4; human. [O43570-1]
CTD; 771; -.
DisGeNET; 771; -.
EuPathDB; HostDB:ENSG00000074410.13; -.
GeneCards; CA12; -.
HGNC; HGNC:1371; CA12.
HPA; CAB025181; -.
HPA; CAB062549; -.
HPA; CAB068179; -.
HPA; HPA008773; -.
HPA; HPA073203; -.
MalaCards; CA12; -.
MIM; 143860; phenotype.
MIM; 603263; gene.
neXtProt; NX_O43570; -.
OpenTargets; ENSG00000074410; -.
PharmGKB; PA25987; -.
eggNOG; KOG0382; Eukaryota.
eggNOG; COG3338; LUCA.
GeneTree; ENSGT00760000118915; -.
HOGENOM; HOG000112637; -.
HOVERGEN; HBG002837; -.
InParanoid; O43570; -.
KO; K01672; -.
OMA; HLHWGNR; -.
OrthoDB; EOG091G0XFM; -.
PhylomeDB; O43570; -.
TreeFam; TF316425; -.
BRENDA; 4.2.1.1; 2681.
Reactome; R-HSA-1475029; Reversible hydration of carbon dioxide.
ChiTaRS; CA12; human.
EvolutionaryTrace; O43570; -.
GeneWiki; CA12; -.
GenomeRNAi; 771; -.
PRO; PR:O43570; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000074410; -.
CleanEx; HS_CA12; -.
ExpressionAtlas; O43570; baseline and differential.
Genevisible; O43570; HS.
GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0004089; F:carbonate dehydratase activity; TAS:Reactome.
GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
GO; GO:0015701; P:bicarbonate transport; TAS:Reactome.
GO; GO:0055064; P:chloride ion homeostasis; IMP:UniProtKB.
GO; GO:0006730; P:one-carbon metabolic process; IEA:InterPro.
Gene3D; 3.10.200.10; -; 1.
InterPro; IPR001148; Carbonic_anhydrase_a.
InterPro; IPR023561; Carbonic_anhydrase_a-class.
InterPro; IPR018338; Carbonic_anhydrase_a-class_CS.
InterPro; IPR036398; Carbonic_anhydrase_a_sf.
InterPro; IPR018430; Carbonic_anhydrase_CA12.
PANTHER; PTHR18952; PTHR18952; 1.
PANTHER; PTHR18952:SF19; PTHR18952:SF19; 1.
Pfam; PF00194; Carb_anhydrase; 1.
SMART; SM01057; Carb_anhydrase; 1.
SUPFAM; SSF51069; SSF51069; 1.
PROSITE; PS00162; ALPHA_CA_1; 1.
PROSITE; PS51144; ALPHA_CA_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Disease mutation; Disulfide bond; Glycoprotein; Lyase; Membrane;
Metal-binding; Reference proteome; Signal; Transmembrane;
Transmembrane helix; Zinc.
SIGNAL 1 24 {ECO:0000255}.
CHAIN 25 354 Carbonic anhydrase 12.
/FTId=PRO_0000004248.
TOPO_DOM 25 301 Extracellular. {ECO:0000255}.
TRANSMEM 302 322 Helical. {ECO:0000255}.
TOPO_DOM 323 354 Cytoplasmic. {ECO:0000255}.
DOMAIN 30 289 Alpha-carbonic anhydrase.
{ECO:0000255|PROSITE-ProRule:PRU01134}.
REGION 226 227 Substrate binding.
{ECO:0000250|UniProtKB:P00918}.
ACT_SITE 94 94 Proton acceptor.
{ECO:0000250|UniProtKB:P00918}.
ACT_SITE 154 154 {ECO:0000250|UniProtKB:P00918}.
METAL 119 119 Zinc; catalytic.
{ECO:0000269|PubMed:11493685}.
METAL 121 121 Zinc; catalytic.
{ECO:0000269|PubMed:11493685}.
METAL 145 145 Zinc; catalytic.
{ECO:0000269|PubMed:11493685}.
CARBOHYD 28 28 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 80 80 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 162 162 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 50 230 {ECO:0000269|PubMed:11493685}.
VAR_SEQ 292 302 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.3}.
/FTId=VSP_000772.
VARIANT 143 143 E -> K (in HCHLH; mild reduction of
activity; mutant enzyme is highly
inhibited by acetazolamide and shows
higher sensitivity to inhibition by
anions compared to wild-type; the
mutation affects the chloride-mediated
negative feedback regulation of the
enzyme leading to excessive chloride
secretion in sweat; dbSNP:rs267606694).
{ECO:0000269|PubMed:21035102}.
/FTId=VAR_065292.
CONFLICT 305 305 I -> T (in Ref. 4; BAG38121).
{ECO:0000305}.
HELIX 36 38 {ECO:0000244|PDB:4WW8}.
HELIX 40 42 {ECO:0000244|PDB:4WW8}.
TURN 43 46 {ECO:0000244|PDB:4WW8}.
HELIX 48 51 {ECO:0000244|PDB:4WW8}.
STRAND 52 54 {ECO:0000244|PDB:4WW8}.
HELIX 62 64 {ECO:0000244|PDB:4WW8}.
STRAND 65 67 {ECO:0000244|PDB:4WW8}.
STRAND 75 78 {ECO:0000244|PDB:4WW8}.
STRAND 85 91 {ECO:0000244|PDB:4WW8}.
STRAND 93 99 {ECO:0000244|PDB:4WW8}.
STRAND 105 111 {ECO:0000244|PDB:4WW8}.
STRAND 113 122 {ECO:0000244|PDB:4WW8}.
STRAND 132 135 {ECO:0000244|PDB:4WW8}.
STRAND 141 150 {ECO:0000244|PDB:4WW8}.
TURN 151 153 {ECO:0000244|PDB:4WW8}.
HELIX 157 160 {ECO:0000244|PDB:4WW8}.
STRAND 167 176 {ECO:0000244|PDB:4WW8}.
HELIX 181 187 {ECO:0000244|PDB:4WW8}.
HELIX 188 193 {ECO:0000244|PDB:4WW8}.
STRAND 199 203 {ECO:0000244|PDB:4WW8}.
HELIX 207 210 {ECO:0000244|PDB:4WW8}.
TURN 213 216 {ECO:0000244|PDB:4Q0L}.
STRAND 218 223 {ECO:0000244|PDB:4WW8}.
STRAND 234 241 {ECO:0000244|PDB:4WW8}.
STRAND 243 245 {ECO:0000244|PDB:4WW8}.
HELIX 247 255 {ECO:0000244|PDB:4WW8}.
STRAND 258 260 {ECO:0000244|PDB:4WW8}.
STRAND 285 288 {ECO:0000244|PDB:4WW8}.
SEQUENCE 354 AA; 39451 MW; 9016216BF2CA6C0C CRC64;
MPRRSLHAAA VLLLVILKEQ PSSPAPVNGS KWTYFGPDGE NSWSKKYPSC GGLLQSPIDL
HSDILQYDAS LTPLEFQGYN LSANKQFLLT NNGHSVKLNL PSDMHIQGLQ SRYSATQLHL
HWGNPNDPHG SEHTVSGQHF AAELHIVHYN SDLYPDASTA SNKSEGLAVL AVLIEMGSFN
PSYDKIFSHL QHVKYKGQEA FVPGFNIEEL LPERTAEYYR YRGSLTTPPC NPTVLWTVFR
NPVQISQEQL LALETALYCT HMDDPSPREM INNFRQVQKF DERLVYTSFS QVQVCTAAGL
SLGIILSLAL AGILGICIVV VVSIWLFRRK SIKKGDNKGV IYKPATKMET EAHA


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EIAAB05183 Ca9,CAIX,CA-IX,Car9,Carbonate dehydratase IX,Carbonic anhydrase 9,Carbonic anhydrase IX,Membrane antigen MN homolog,Mouse,Mus musculus
EIAAB05184 CA9,CAIX,CA-IX,Carbonate dehydratase IX,Carbonic anhydrase 9,Carbonic anhydrase IX,G250,Homo sapiens,Human,Membrane antigen MN,MN,P54_58N,pMW1,RCC-associated antigen G250,Renal cell carcinoma-associat
EIAAB05170 CA Y,Ca5,Ca5a,Car5,Car5a,Carbonate dehydratase VA,Carbonic anhydrase 5A, mitochondrial,Carbonic anhydrase VA,CA-VA,Mouse,Mus musculus
EIAAB05169 CA5,CA5A,Carbonate dehydratase VA,Carbonic anhydrase 5A, mitochondrial,Carbonic anhydrase VA,CA-VA,Homo sapiens,Human
EIAAB05171 Ca5b,Car5b,Carbonate dehydratase VB,Carbonic anhydrase 5B, mitochondrial,Carbonic anhydrase VB,CA-VB,Mouse,Mus musculus
EIAAB05155 Ca14,Car14,Carbonate dehydratase XIV,Carbonic anhydrase 14,Carbonic anhydrase XIV,Catm,CA-XIV,Mouse,Mus musculus
EIAAB05173 CA5B,Carbonate dehydratase VB,Carbonic anhydrase 5B, mitochondrial,Carbonic anhydrase VB,CA-VB,Homo sapiens,Human
EIAAB05156 CA14,Carbonate dehydratase XIV,Carbonic anhydrase 14,Carbonic anhydrase XIV,CA-XIV,Homo sapiens,Human,UNQ690_PRO1335
EIAAB05172 Ca5b,Car5b,Carbonate dehydratase VB,Carbonic anhydrase 5B, mitochondrial,Carbonic anhydrase VB,CA-VB,Rat,Rattus norvegicus
EIAAB05157 Ca15,Car15,Carbonate dehydratase XV,Carbonic anhydrase 15,Carbonic anhydrase XV,CA-XV,Mouse,Mus musculus
E0782Rb ELISA CA2,CA-II,Carbonate dehydratase II,Carbonic anhydrase 2,Carbonic anhydrase II,Oryctolagus cuniculus,Rabbit 96T
E1799Rb ELISA kit CA1,CA-I,Carbonate dehydratase I,Carbonic anhydrase 1,Carbonic anhydrase I,Oryctolagus cuniculus,Rabbit 96T
U1799r CLIA Ca1,CA-I,Car1,Carbonate dehydratase I,Carbonic anhydrase 1,Carbonic anhydrase I,Rat,Rattus norvegicus 96T
E0782m ELISA Ca2,CA-II,Car2,Carbonate dehydratase II,Carbonic anhydrase 2,Carbonic anhydrase II,Mouse,Mus musculus 96T


 

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