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Carbonic anhydrase 9 (EC 4.2.1.1) (Carbonate dehydratase IX) (Carbonic anhydrase IX) (CA-IX) (CAIX) (Membrane antigen MN) (P54/58N) (Renal cell carcinoma-associated antigen G250) (RCC-associated antigen G250) (pMW1)

 CAH9_HUMAN              Reviewed;         459 AA.
Q16790; Q5T4R1;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
06-DEC-2005, sequence version 2.
25-OCT-2017, entry version 168.
RecName: Full=Carbonic anhydrase 9;
EC=4.2.1.1;
AltName: Full=Carbonate dehydratase IX;
AltName: Full=Carbonic anhydrase IX;
Short=CA-IX;
Short=CAIX;
AltName: Full=Membrane antigen MN;
AltName: Full=P54/58N;
AltName: Full=Renal cell carcinoma-associated antigen G250;
Short=RCC-associated antigen G250;
AltName: Full=pMW1;
Flags: Precursor;
Name=CA9; Synonyms=G250, MN;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND VARIANT MET-33.
TISSUE=Carcinoma;
PubMed=8084592;
Pastorek J., Pastorekova S., Callebaut I., Mornon J.-P., Zelnik V.,
Opavsky R., Zat'Ovicova M., Liao S., Portetelle D., Stanbridge E.J.,
Zavada J., Burny A., Kettmann R.;
"Cloning and characterization of MN, a human tumor-associated protein
with a domain homologous to carbonic anhydrase and a putative helix-
loop-helix DNA binding segment.";
Oncogene 9:2877-2888(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Renal cell carcinoma;
PubMed=10709109;
DOI=10.1002/(SICI)1097-0215(20000315)85:6<865::AID-IJC21>3.0.CO;2-Q;
Grabmaier K., Vissers J.L.M., De Weijert M.C.A.,
Oosterwijk-Wakka J.C., Van Bokhoven A., Brakenhoff R.H., Noessner E.,
Mulders P.A., Merkx G., Figdor C.G., Adema G.J., Oosterwijk E.;
"Molecular cloning and immunogenicity of renal cell carcinoma-
associated antigen G250.";
Int. J. Cancer 85:865-870(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-33.
TISSUE=Colon;
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]
PROTEIN SEQUENCE OF 38-52.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[7]
CHARACTERIZATION.
PubMed=1312272; DOI=10.1016/0042-6822(92)90464-Z;
Pastorekova S., Zavadova Z., Kostal M., Babusikova O., Zavada J.;
"A novel quasi-viral agent, MaTu, is a two-component system.";
Virology 187:620-626(1992).
[8]
SUBCELLULAR LOCATION.
PubMed=8486430; DOI=10.1002/ijc.2910540218;
Zavada J., Zavadova Z., Pastorekova S., Ciampor F., Pastorek J.,
Zelnik V.;
"Expression of MaTu-MN protein in human tumor cultures and in clinical
specimens.";
Int. J. Cancer 54:268-274(1993).
[9]
PHOSPHORYLATION AT TYR-449.
PubMed=16310354; DOI=10.1016/j.ejca.2005.09.011;
Dorai T., Sawczuk I.S., Pastorek J., Wiernik P.H., Dutcher J.P.;
"The role of carbonic anhydrase IX overexpression in kidney cancer.";
Eur. J. Cancer 41:2935-2947(2005).
[10]
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).
[11]
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).
[12]
FUNCTION, SUBUNIT, INDUCTION, GLYCOSYLATION AT THR-115 AND ASN-346,
AND DISULFIDE BONDS.
PubMed=18703501; DOI=10.1074/jbc.M800938200;
Hilvo M., Baranauskiene L., Salzano A.M., Scaloni A., Matulis D.,
Innocenti A., Scozzafava A., Monti S.M., Di Fiore A., De Simone G.,
Lindfors M., Janis J., Valjakka J., Pastorekova S., Pastorek J.,
Kulomaa M.S., Nordlund H.R., Supuran C.T., Parkkila S.;
"Biochemical characterization of CA IX, one of the most active
carbonic anhydrase isozymes.";
J. Biol. Chem. 283:27799-27809(2008).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
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).
[15]
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).
[16]
X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 83-91 IN COMPLEX WITH
SPECIFIC ANTIBODIES.
PubMed=18041760; DOI=10.1002/prot.21821;
Kral V., Mader P., Collard R., Fabry M., Horejsi M., Rezacova P.,
Kozisek M., Zavada J., Sedlacek J., Rulisek L., Brynda J.;
"Stabilization of antibody structure upon association to a human
carbonic anhydrase IX epitope studied by X-ray crystallography,
microcalorimetry, and molecular dynamics simulations.";
Proteins 71:1275-1287(2008).
[17]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 137-391 IN COMPLEX WITH ZINC
ION AND THE INHIBITOR ACETAZOLAMIDE, GLYCOSYLATION AT ASN-346,
DISULFIDE BOND, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=19805286; DOI=10.1073/pnas.0908301106;
Alterio V., Hilvo M., Di Fiore A., Supuran C.T., Pan P., Parkkila S.,
Scaloni A., Pastorek J., Pastorekova S., Pedone C., Scozzafava A.,
Monti S.M., De Simone G.;
"Crystal structure of the catalytic domain of the tumor-associated
human carbonic anhydrase IX.";
Proc. Natl. Acad. Sci. U.S.A. 106:16233-16238(2009).
-!- FUNCTION: Reversible hydration of carbon dioxide. Participates in
pH regulation. May be involved in the control of cell
proliferation and transformation. Appears to be a novel specific
biomarker for a cervical neoplasia. {ECO:0000269|PubMed:18703501}.
-!- CATALYTIC ACTIVITY: H(2)CO(3) = CO(2) + H(2)O.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:19805286};
-!- ENZYME REGULATION: Inhibited by coumarins, saccharin, sulfonamide
derivatives such as acetazolamide (AZA) and Foscarnet
(phosphonoformate trisodium salt). {ECO:0000269|PubMed:17314045,
ECO:0000269|PubMed:17705204, ECO:0000269|PubMed:19186056,
ECO:0000269|PubMed:19206230}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 6.5. {ECO:0000269|PubMed:19805286};
-!- SUBUNIT: Forms oligomers linked by disulfide bonds.
{ECO:0000269|PubMed:18041760, ECO:0000269|PubMed:18703501,
ECO:0000269|PubMed:19805286}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8486430}.
Nucleus, nucleolus {ECO:0000269|PubMed:8486430}. Cell membrane
{ECO:0000269|PubMed:8486430}; Single-pass type I membrane protein
{ECO:0000269|PubMed:8486430}. Cell projection, microvillus
membrane {ECO:0000269|PubMed:8486430}; Single-pass type I membrane
protein {ECO:0000269|PubMed:8486430}. Note=Found on the surface
microvilli and in the nucleus, particularly in nucleolus.
-!- TISSUE SPECIFICITY: Expressed primarily in carcinoma cells lines.
Expression is restricted to very few normal tissues and the most
abundant expression is found in the epithelial cells of gastric
mucosa.
-!- INDUCTION: By hypoxia. {ECO:0000269|PubMed:18703501}.
-!- PTM: Asn-346 bears high-mannose type glycan structures.
-!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
{ECO:0000305}.
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EMBL; X66839; CAA47315.1; -; mRNA.
EMBL; AJ010588; CAB82444.1; -; mRNA.
EMBL; AL133410; CAI10985.1; -; Genomic_DNA.
EMBL; AL357874; CAI10985.1; JOINED; Genomic_DNA.
EMBL; AL357874; CAI13455.1; -; Genomic_DNA.
EMBL; AL133410; CAI13455.1; JOINED; Genomic_DNA.
EMBL; CH471071; EAW58359.1; -; Genomic_DNA.
EMBL; BC014950; AAH14950.1; -; mRNA.
CCDS; CCDS6585.1; -.
PIR; I38013; I38013.
RefSeq; NP_001207.2; NM_001216.2.
UniGene; Hs.63287; -.
PDB; 2HKF; X-ray; 2.01 A; P=83-91.
PDB; 3IAI; X-ray; 2.20 A; A/B/C/D=137-391.
PDB; 5DVX; X-ray; 1.60 A; A/B=140-399.
PDB; 5FL4; X-ray; 1.82 A; A/B/C/D=137-391.
PDB; 5FL5; X-ray; 2.05 A; A/B/C/D=137-391.
PDB; 5FL6; X-ray; 1.95 A; A/B/C/D=137-391.
PDBsum; 2HKF; -.
PDBsum; 3IAI; -.
PDBsum; 5DVX; -.
PDBsum; 5FL4; -.
PDBsum; 5FL5; -.
PDBsum; 5FL6; -.
ProteinModelPortal; Q16790; -.
SMR; Q16790; -.
BioGrid; 107223; 30.
DIP; DIP-48973N; -.
IntAct; Q16790; 1.
STRING; 9606.ENSP00000367608; -.
BindingDB; Q16790; -.
ChEMBL; CHEMBL3594; -.
DrugBank; DB00562; Benzthiazide.
DrugBank; DB08846; Ellagic Acid.
DrugBank; DB00999; Hydrochlorothiazide.
DrugBank; DB00774; Hydroflumethiazide.
DrugBank; DB09460; Sodium carbonate.
DrugBank; DB05304; WX-G250.
DrugBank; DB00909; Zonisamide.
iPTMnet; Q16790; -.
PhosphoSitePlus; Q16790; -.
BioMuta; CA9; -.
DMDM; 83300925; -.
MaxQB; Q16790; -.
PaxDb; Q16790; -.
PeptideAtlas; Q16790; -.
PRIDE; Q16790; -.
DNASU; 768; -.
Ensembl; ENST00000378357; ENSP00000367608; ENSG00000107159.
GeneID; 768; -.
KEGG; hsa:768; -.
UCSC; uc003zxo.5; human.
CTD; 768; -.
DisGeNET; 768; -.
EuPathDB; HostDB:ENSG00000107159.12; -.
GeneCards; CA9; -.
H-InvDB; HIX0008019; -.
HGNC; HGNC:1383; CA9.
HPA; CAB005100; -.
HPA; CAB017107; -.
HPA; HPA055207; -.
MIM; 603179; gene.
neXtProt; NX_Q16790; -.
OpenTargets; ENSG00000107159; -.
PharmGKB; PA25998; -.
eggNOG; KOG0382; Eukaryota.
eggNOG; COG3338; LUCA.
GeneTree; ENSGT00760000118915; -.
HOGENOM; HOG000112637; -.
HOVERGEN; HBG002837; -.
InParanoid; Q16790; -.
KO; K01672; -.
OMA; SRYFRYE; -.
OrthoDB; EOG091G0XFM; -.
PhylomeDB; Q16790; -.
TreeFam; TF316425; -.
BRENDA; 4.2.1.1; 2681.
Reactome; R-HSA-1234158; Regulation of gene expression by Hypoxia-inducible Factor.
Reactome; R-HSA-1475029; Reversible hydration of carbon dioxide.
SIGNOR; Q16790; -.
EvolutionaryTrace; Q16790; -.
GeneWiki; Carbonic_anhydrase_9; -.
GenomeRNAi; 768; -.
PRO; PR:Q16790; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000107159; -.
CleanEx; HS_CA9; -.
ExpressionAtlas; Q16790; baseline and differential.
Genevisible; Q16790; HS.
GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
GO; GO:0031528; C:microvillus membrane; IEA:UniProtKB-SubCell.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0004089; F:carbonate dehydratase activity; TAS:Reactome.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0015701; P:bicarbonate transport; TAS:Reactome.
GO; GO:0002009; P:morphogenesis of an epithelium; IEA:Ensembl.
GO; GO:0006730; P:one-carbon metabolic process; IEA:InterPro.
GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0033574; P:response to testosterone; IEA:Ensembl.
GO; GO:0046903; P:secretion; IEA:Ensembl.
Gene3D; 3.10.200.10; -; 1.
InterPro; IPR018429; CA9.
InterPro; IPR001148; Carbonic_anhydrase_a.
InterPro; IPR023561; Carbonic_anhydrase_a-class.
InterPro; IPR018338; Carbonic_anhydrase_a-class_CS.
InterPro; IPR036398; Carbonic_anhydrase_a_sf.
PANTHER; PTHR18952; PTHR18952; 1.
PANTHER; PTHR18952:SF18; PTHR18952:SF18; 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; Cell membrane; Cell projection; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein; Lyase;
Membrane; Metal-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Signal; Transmembrane; Transmembrane helix; Zinc.
SIGNAL 1 37 {ECO:0000269|PubMed:15340161}.
CHAIN 38 459 Carbonic anhydrase 9.
/FTId=PRO_0000004243.
TOPO_DOM 38 414 Extracellular.
TRANSMEM 415 435 Helical. {ECO:0000255}.
TOPO_DOM 436 459 Cytoplasmic.
DOMAIN 139 390 Alpha-carbonic anhydrase.
{ECO:0000255|PROSITE-ProRule:PRU01134}.
REGION 38 112 Proteoglycan-like (PG).
REGION 113 414 Catalytic.
REGION 332 333 Substrate binding.
{ECO:0000250|UniProtKB:P00918}.
ACT_SITE 200 200 Proton acceptor.
{ECO:0000250|UniProtKB:P00918}.
METAL 226 226 Zinc; catalytic.
{ECO:0000269|PubMed:19805286}.
METAL 228 228 Zinc; catalytic.
{ECO:0000269|PubMed:19805286}.
METAL 251 251 Zinc; catalytic.
{ECO:0000269|PubMed:19805286}.
MOD_RES 449 449 Phosphotyrosine.
{ECO:0000269|PubMed:16310354}.
CARBOHYD 115 115 O-linked (GlcNAc...) threonine.
{ECO:0000269|PubMed:18703501}.
CARBOHYD 346 346 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:18703501,
ECO:0000269|PubMed:19805286}.
DISULFID 156 336 {ECO:0000269|PubMed:19805286}.
DISULFID 174 174 Interchain.
{ECO:0000305|PubMed:19805286}.
VARIANT 33 33 V -> M (in dbSNP:rs2071676).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:8084592}.
/FTId=VAR_010787.
VARIANT 326 326 Q -> R (in dbSNP:rs3829078).
/FTId=VAR_020049.
TURN 137 139 {ECO:0000244|PDB:3IAI}.
STRAND 145 147 {ECO:0000244|PDB:5FL4}.
HELIX 149 152 {ECO:0000244|PDB:5DVX}.
HELIX 154 157 {ECO:0000244|PDB:5DVX}.
HELIX 168 170 {ECO:0000244|PDB:5DVX}.
STRAND 171 173 {ECO:0000244|PDB:5FL6}.
STRAND 181 184 {ECO:0000244|PDB:5DVX}.
STRAND 193 197 {ECO:0000244|PDB:5DVX}.
STRAND 202 205 {ECO:0000244|PDB:5DVX}.
STRAND 211 215 {ECO:0000244|PDB:5DVX}.
STRAND 218 229 {ECO:0000244|PDB:5DVX}.
STRAND 238 241 {ECO:0000244|PDB:5DVX}.
STRAND 247 256 {ECO:0000244|PDB:5DVX}.
HELIX 262 265 {ECO:0000244|PDB:5DVX}.
STRAND 271 281 {ECO:0000244|PDB:5DVX}.
HELIX 287 293 {ECO:0000244|PDB:5DVX}.
TURN 294 296 {ECO:0000244|PDB:5FL4}.
HELIX 297 299 {ECO:0000244|PDB:5DVX}.
STRAND 305 308 {ECO:0000244|PDB:5DVX}.
HELIX 313 316 {ECO:0000244|PDB:5DVX}.
STRAND 324 330 {ECO:0000244|PDB:5DVX}.
STRAND 338 347 {ECO:0000244|PDB:5DVX}.
STRAND 349 351 {ECO:0000244|PDB:5DVX}.
HELIX 353 361 {ECO:0000244|PDB:5DVX}.
STRAND 387 390 {ECO:0000244|PDB:5DVX}.
SEQUENCE 459 AA; 49698 MW; BA67195483F0F5CE CRC64;
MAPLCPSPWL PLLIPAPAPG LTVQLLLSLL LLVPVHPQRL PRMQEDSPLG GGSSGEDDPL
GEEDLPSEED SPREEDPPGE EDLPGEEDLP GEEDLPEVKP KSEEEGSLKL EDLPTVEAPG
DPQEPQNNAH RDKEGDDQSH WRYGGDPPWP RVSPACAGRF QSPVDIRPQL AAFCPALRPL
ELLGFQLPPL PELRLRNNGH SVQLTLPPGL EMALGPGREY RALQLHLHWG AAGRPGSEHT
VEGHRFPAEI HVVHLSTAFA RVDEALGRPG GLAVLAAFLE EGPEENSAYE QLLSRLEEIA
EEGSETQVPG LDISALLPSD FSRYFQYEGS LTTPPCAQGV IWTVFNQTVM LSAKQLHTLS
DTLWGPGDSR LQLNFRATQP LNGRVIEASF PAGVDSSPRA AEPVQLNSCL AAGDILALVF
GLLFAVTSVA FLVQMRRQHR RGTKGGVSYR PAEVAETGA


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EIAAB05150 CA12,Carbonate dehydratase XII,Carbonic anhydrase 12,Carbonic anhydrase XII,CA-XII,Homo sapiens,Human,Tumor antigen HOM-RCC-3.1.3
EIAAB05176 Ca6,Car6,Carbonate dehydratase VI,Carbonic anhydrase 6,Carbonic anhydrase VI,CA-VI,Mouse,Mus musculus,Salivary carbonic anhydrase,Secreted carbonic anhydrase
EIAAB05175 CA6,Carbonate dehydratase VI,Carbonic anhydrase 6,Carbonic anhydrase VI,CA-VI,Homo sapiens,Human,Salivary carbonic anhydrase,Secreted carbonic anhydrase
EIAAB05177 Bos taurus,Bovine,CA6,Carbonate dehydratase VI,Carbonic anhydrase 6,Carbonic anhydrase VI,CA-VI,Salivary carbonic anhydrase,Secreted carbonic anhydrase
U1799h CLIA CA1,CAB,CA-I,Carbonate dehydratase I,Carbonic anhydrase 1,Carbonic anhydrase B,Carbonic anhydrase I,Homo sapiens,Human 96T
E1799h ELISA kit CA1,CAB,CA-I,Carbonate dehydratase I,Carbonic anhydrase 1,Carbonic anhydrase B,Carbonic anhydrase I,Homo sapiens,Human 96T
E0782h ELISA CA2,CAC,CA-II,Carbonate dehydratase II,Carbonic anhydrase 2,Carbonic anhydrase C,Carbonic anhydrase II,Homo sapiens,Human 96T
U1799h CLIA kit CA1,CAB,CA-I,Carbonate dehydratase I,Carbonic anhydrase 1,Carbonic anhydrase B,Carbonic anhydrase I,Homo sapiens,Human 96T
E0782h ELISA kit CA2,CAC,CA-II,Carbonate dehydratase II,Carbonic anhydrase 2,Carbonic anhydrase C,Carbonic anhydrase II,Homo sapiens,Human 96T
U0782h CLIA CA2,CAC,CA-II,Carbonate dehydratase II,Carbonic anhydrase 2,Carbonic anhydrase C,Carbonic anhydrase II,Homo sapiens,Human 96T
E1799h ELISA CA1,CAB,CA-I,Carbonate dehydratase I,Carbonic anhydrase 1,Carbonic anhydrase B,Carbonic anhydrase I,Homo sapiens,Human 96T
EIAAB05170 CA Y,Ca5,Ca5a,Car5,Car5a,Carbonate dehydratase VA,Carbonic anhydrase 5A, mitochondrial,Carbonic anhydrase VA,CA-VA,Mouse,Mus musculus
EIAAB05155 Ca14,Car14,Carbonate dehydratase XIV,Carbonic anhydrase 14,Carbonic anhydrase XIV,Catm,CA-XIV,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
EIAAB05172 Ca5b,Car5b,Carbonate dehydratase VB,Carbonic anhydrase 5B, mitochondrial,Carbonic anhydrase VB,CA-VB,Rat,Rattus norvegicus
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
E1799r ELISA kit Ca1,CA-I,Car1,Carbonate dehydratase I,Carbonic anhydrase 1,Carbonic anhydrase I,Rat,Rattus norvegicus 96T
EIAAB05157 Ca15,Car15,Carbonate dehydratase XV,Carbonic anhydrase 15,Carbonic anhydrase XV,CA-XV,Mouse,Mus musculus
U1799m CLIA Ca1,CA-I,Car1,Carbonate dehydratase I,Carbonic anhydrase 1,Carbonic anhydrase I,Mouse,Mus musculus 96T
EIAAB05152 Ca12,Car12,Carbonate dehydratase XII,Carbonic anhydrase 12,Carbonic anhydrase XII,CA-XII,Mouse,Mus musculus
U1799r CLIA Ca1,CA-I,Car1,Carbonate dehydratase I,Carbonic anhydrase 1,Carbonic anhydrase I,Rat,Rattus norvegicus 96T


 

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