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Cathepsin Z (EC 3.4.18.1) (Cathepsin P) (Cathepsin X)

 CATZ_HUMAN              Reviewed;         303 AA.
Q9UBR2; B2RC40; O75331; Q9UQV5; Q9UQV6;
24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
20-JUN-2018, entry version 170.
RecName: Full=Cathepsin Z;
EC=3.4.18.1;
AltName: Full=Cathepsin P;
AltName: Full=Cathepsin X;
Flags: Precursor;
Name=CTSZ;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS SER-36 AND ARG-129.
TISSUE=Ovary;
PubMed=9738465; DOI=10.1016/S0014-5793(98)00964-8;
Naegler D.K., Menard R.;
"Human cathepsin X: a novel cysteine protease of the papain family
with a very short proregion and unique insertions.";
FEBS Lett. 434:135-139(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Prostate;
PubMed=9642240; DOI=10.1074/jbc.273.27.16816;
Santamaria I., Velasco G., Pendas A.M., Fueyo A., Lopez-Otin C.;
"Cathepsin Z, a novel human cysteine proteinase with a short
propeptide domain and a unique chromosomal location.";
J. Biol. Chem. 273:16816-16823(1998).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
TISSUE=Blood, and Colon tumor;
PubMed=10760573; DOI=10.1016/S0167-4781(00)00021-X;
Deussing J., von Olshausen I., Peters C.;
"Murine and human cathepsin Z: cDNA-cloning, characterization of the
genes and chromosomal localization.";
Biochim. Biophys. Acta 1491:93-106(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon;
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 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).
[6]
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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pancreas;
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).
[8]
NUCLEOTIDE SEQUENCE OF 11-303.
TISSUE=Ileum;
PubMed=10653162; DOI=10.1007/s004240000112;
Pungercar J., Ivanovski G.;
"Identification and molecular cloning of cathepsin P, a novel human
putative cysteine protease of the papain family.";
Pflugers Arch. 439:R116-R118(2000).
[9]
CATALYTIC ACTIVITY, AND CHARACTERIZATION.
PubMed=10504234; DOI=10.1021/bi991371z;
Naegler D.K., Zhang R., Tam W., Sulea T., Purisima E.O., Menard R.;
"Human cathepsin X: a cysteine protease with unique carboxypeptidase
activity.";
Biochemistry 38:12648-12654(1999).
[10]
TISSUE SPECIFICITY.
PubMed=10653163; DOI=10.1007/s004240000113;
Pungercar J., Viyjak A., Ivanovski G., Krizaj I.;
"Tissue expression and immunolocalization of a novel human cathepsin
P.";
Pflugers Arch. 439:R119-R121(2000).
[11]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-184.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[12]
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).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[15]
X-RAY CRYSTALLOGRAPHY (2.67 ANGSTROMS).
PubMed=10745011; DOI=10.1016/S0969-2126(00)00108-8;
Guncar G., Klemencic I., Turk B., Turk V., Karaoglanovic-Carmona A.,
Juliano L., Turk D.;
"Crystal structure of cathepsin X: a flip-flop of the ring of His23
allows carboxy-monopeptidase and carboxy-dipeptidase activity of the
protease.";
Structure 8:305-313(2000).
-!- FUNCTION: Exhibits carboxy-monopeptidase as well as carboxy-
dipeptidase activity.
-!- CATALYTIC ACTIVITY: Release of C-terminal amino acid residues with
broad specificity, but lacks action on C-terminal proline. Shows
weak endopeptidase activity. {ECO:0000269|PubMed:10504234}.
-!- INTERACTION:
Q6A162:KRT40; NbExp=3; IntAct=EBI-8636823, EBI-10171697;
P26371:KRTAP5-9; NbExp=6; IntAct=EBI-8636823, EBI-3958099;
Q9UJV3-2:MID2; NbExp=5; IntAct=EBI-8636823, EBI-10172526;
Q5JR59:MTUS2; NbExp=3; IntAct=EBI-8636823, EBI-742948;
Q7Z3S9:NOTCH2NL; NbExp=5; IntAct=EBI-8636823, EBI-945833;
O15162:PLSCR1; NbExp=3; IntAct=EBI-8636823, EBI-740019;
-!- SUBCELLULAR LOCATION: Lysosome.
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:10653163}.
-!- SIMILARITY: Belongs to the peptidase C1 family.
{ECO:0000255|PROSITE-ProRule:PRU10090}.
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EMBL; AF073890; AAC61477.1; -; mRNA.
EMBL; AF032906; AAC39839.1; -; mRNA.
EMBL; AF136273; AAF13145.1; -; mRNA.
EMBL; AF136276; AAF13148.1; -; Genomic_DNA.
EMBL; AF136274; AAF13148.1; JOINED; Genomic_DNA.
EMBL; AF136275; AAF13148.1; JOINED; Genomic_DNA.
EMBL; AK314931; BAG37437.1; -; mRNA.
EMBL; AL109840; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471077; EAW75448.1; -; Genomic_DNA.
EMBL; BC042168; AAH42168.1; -; mRNA.
EMBL; AF009923; AAC63141.1; -; mRNA.
CCDS; CCDS13474.1; -.
RefSeq; NP_001327.2; NM_001336.3.
UniGene; Hs.252549; -.
PDB; 1DEU; X-ray; 1.70 A; A/B=27-303.
PDB; 1EF7; X-ray; 2.67 A; A/B=62-303.
PDBsum; 1DEU; -.
PDBsum; 1EF7; -.
ProteinModelPortal; Q9UBR2; -.
SMR; Q9UBR2; -.
BioGrid; 107902; 15.
IntAct; Q9UBR2; 24.
MINT; Q9UBR2; -.
STRING; 9606.ENSP00000217131; -.
BindingDB; Q9UBR2; -.
ChEMBL; CHEMBL4160; -.
GuidetoPHARMACOLOGY; 2354; -.
MEROPS; C01.013; -.
iPTMnet; Q9UBR2; -.
PhosphoSitePlus; Q9UBR2; -.
SwissPalm; Q9UBR2; -.
BioMuta; CTSZ; -.
DMDM; 12643324; -.
EPD; Q9UBR2; -.
MaxQB; Q9UBR2; -.
PaxDb; Q9UBR2; -.
PeptideAtlas; Q9UBR2; -.
PRIDE; Q9UBR2; -.
ProteomicsDB; 84036; -.
DNASU; 1522; -.
Ensembl; ENST00000217131; ENSP00000217131; ENSG00000101160.
GeneID; 1522; -.
KEGG; hsa:1522; -.
UCSC; uc002yai.3; human.
CTD; 1522; -.
DisGeNET; 1522; -.
EuPathDB; HostDB:ENSG00000101160.13; -.
GeneCards; CTSZ; -.
HGNC; HGNC:2547; CTSZ.
HPA; CAB025114; -.
HPA; HPA049876; -.
HPA; HPA053504; -.
MIM; 603169; gene.
neXtProt; NX_Q9UBR2; -.
OpenTargets; ENSG00000101160; -.
PharmGKB; PA27043; -.
eggNOG; KOG1543; Eukaryota.
eggNOG; COG4870; LUCA.
GeneTree; ENSGT00900000140859; -.
HOGENOM; HOG000264454; -.
HOVERGEN; HBG004456; -.
InParanoid; Q9UBR2; -.
KO; K08568; -.
OMA; QCGTCTE; -.
OrthoDB; EOG091G0BNT; -.
PhylomeDB; Q9UBR2; -.
TreeFam; TF313225; -.
BRENDA; 3.4.18.1; 2681.
Reactome; R-HSA-2022377; Metabolism of Angiotensinogen to Angiotensins.
Reactome; R-HSA-204005; COPII-mediated vesicle transport.
Reactome; R-HSA-432720; Lysosome Vesicle Biogenesis.
Reactome; R-HSA-5694530; Cargo concentration in the ER.
Reactome; R-HSA-6798695; Neutrophil degranulation.
ChiTaRS; CTSZ; human.
EvolutionaryTrace; Q9UBR2; -.
GeneWiki; Cathepsin_Z; -.
GenomeRNAi; 1522; -.
PRO; PR:Q9UBR2; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000101160; -.
CleanEx; HS_CTSZ; -.
Genevisible; Q9UBR2; HS.
GO; GO:0099738; C:cell cortex region; IDA:CAFA.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; TAS:Reactome.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:CAFA.
GO; GO:0005783; C:endoplasmic reticulum; IDA:LIFEdb.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:CAFA.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0000139; C:Golgi membrane; IEA:GOC.
GO; GO:0030426; C:growth cone; IEA:Ensembl.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005764; C:lysosome; IDA:CAFA.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
GO; GO:0004180; F:carboxypeptidase activity; IMP:CAFA.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
GO; GO:0008234; F:cysteine-type peptidase activity; TAS:Reactome.
GO; GO:0002003; P:angiotensin maturation; TAS:Reactome.
GO; GO:0048208; P:COPII vesicle coating; TAS:Reactome.
GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IEA:Ensembl.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; TAS:Reactome.
GO; GO:0010977; P:negative regulation of neuron projection development; IEA:Ensembl.
GO; GO:0010757; P:negative regulation of plasminogen activation; IMP:CAFA.
GO; GO:0032091; P:negative regulation of protein binding; IDA:CAFA.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; IEA:Ensembl.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0006508; P:proteolysis; IMP:CAFA.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IBA:GO_Central.
GO; GO:1901214; P:regulation of neuron death; IGI:CAFA.
InterPro; IPR033157; Cathepsin_X.
InterPro; IPR038765; Papain_like_cys_pep_sf.
InterPro; IPR025661; Pept_asp_AS.
InterPro; IPR013128; Peptidase_C1A.
InterPro; IPR000668; Peptidase_C1A_C.
PANTHER; PTHR12411; PTHR12411; 1.
PANTHER; PTHR12411:SF14; PTHR12411:SF14; 1.
Pfam; PF00112; Peptidase_C1; 1.
PRINTS; PR00705; PAPAIN.
SMART; SM00645; Pept_C1; 1.
SUPFAM; SSF54001; SSF54001; 1.
PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Disulfide bond; Glycoprotein;
Hydrolase; Lysosome; Polymorphism; Protease; Reference proteome;
Signal; Thiol protease; Zymogen.
SIGNAL 1 23 {ECO:0000255}.
PROPEP 24 61 Activation peptide.
/FTId=PRO_0000026285.
CHAIN 62 303 Cathepsin Z.
/FTId=PRO_0000026286.
ACT_SITE 92 92
ACT_SITE 241 241
ACT_SITE 261 261
CARBOHYD 184 184 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 224 224 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 89 132
DISULFID 126 164
DISULFID 154 170
DISULFID 173 179
DISULFID 214 296
VARIANT 36 36 P -> S (in dbSNP:rs778998634).
{ECO:0000269|PubMed:9738465}.
/FTId=VAR_010254.
VARIANT 129 129 A -> R (requires 2 nucleotide
substitutions).
{ECO:0000269|PubMed:9738465}.
/FTId=VAR_010255.
VARIANT 286 286 A -> T (in dbSNP:rs34069356).
/FTId=VAR_033719.
CONFLICT 48 48 S -> T (in Ref. 2; AAC39839).
{ECO:0000305}.
CONFLICT 150 150 P -> S (in Ref. 1; AAC61477).
{ECO:0000305}.
STRAND 40 42 {ECO:0000244|PDB:1DEU}.
HELIX 59 61 {ECO:0000244|PDB:1DEU}.
STRAND 85 87 {ECO:0000244|PDB:1EF7}.
HELIX 92 108 {ECO:0000244|PDB:1DEU}.
TURN 109 111 {ECO:0000244|PDB:1DEU}.
HELIX 120 126 {ECO:0000244|PDB:1DEU}.
STRAND 127 131 {ECO:0000244|PDB:1DEU}.
STRAND 133 135 {ECO:0000244|PDB:1DEU}.
HELIX 137 146 {ECO:0000244|PDB:1DEU}.
STRAND 149 151 {ECO:0000244|PDB:1EF7}.
HELIX 152 154 {ECO:0000244|PDB:1DEU}.
HELIX 166 169 {ECO:0000244|PDB:1DEU}.
STRAND 170 175 {ECO:0000244|PDB:1DEU}.
STRAND 178 181 {ECO:0000244|PDB:1DEU}.
STRAND 190 196 {ECO:0000244|PDB:1DEU}.
HELIX 199 209 {ECO:0000244|PDB:1DEU}.
STRAND 212 216 {ECO:0000244|PDB:1DEU}.
HELIX 220 223 {ECO:0000244|PDB:1DEU}.
STRAND 227 230 {ECO:0000244|PDB:1DEU}.
STRAND 241 251 {ECO:0000244|PDB:1DEU}.
STRAND 254 260 {ECO:0000244|PDB:1DEU}.
STRAND 272 276 {ECO:0000244|PDB:1DEU}.
HELIX 280 283 {ECO:0000244|PDB:1DEU}.
HELIX 285 287 {ECO:0000244|PDB:1DEU}.
TURN 290 293 {ECO:0000244|PDB:1DEU}.
STRAND 296 301 {ECO:0000244|PDB:1DEU}.
SEQUENCE 303 AA; 33868 MW; 6274FD1974D0EBDC CRC64;
MARRGPGWRP LLLLVLLAGA AQGGLYFRRG QTCYRPLRGD GLAPLGRSTY PRPHEYLSPA
DLPKSWDWRN VDGVNYASIT RNQHIPQYCG SCWAHASTSA MADRINIKRK GAWPSTLLSV
QNVIDCGNAG SCEGGNDLSV WDYAHQHGIP DETCNNYQAK DQECDKFNQC GTCNEFKECH
AIRNYTLWRV GDYGSLSGRE KMMAEIYANG PISCGIMATE RLANYTGGIY AEYQDTTYIN
HVVSVAGWGI SDGTEYWIVR NSWGEPWGER GWLRIVTSTY KDGKGARYNL AIEEHCTFGD
PIV


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10-663-45680 Procathepsin K Human - EC 3.4.22.38; Cathepsin O; Cathepsin X; Cathepsin O2 N_A 1 mg
18-272-196838 Cathepsin B - Sheep polyclonal to Cathepsin B; EC 3.4.22.1; Cathepsin B1; APP secretase; APPS Polyclonal 1 ml
6206 Cathepsin L (Human Liver), purified cathepsin and related proteases 25
6205 Cathepsin H (Human Liver), purified cathepsin and related proteases 25
6204 Cathepsin G (Human Neutrophil), purified cathepsin and related proteases 100
6202 Cathepsin B (Human Liver), purified cathepsin and related proteases 25
6203 Cathepsin D (Human Liver), purified cathepsin and related proteases 25
U0405h CLIA APP secretase,APPS,Cathepsin B,Cathepsin B1,CPSB,CTSB,Homo sapiens,Human 96T
E0405h ELISA APP secretase,APPS,Cathepsin B,Cathepsin B1,CPSB,CTSB,Homo sapiens,Human 96T
E0405h ELISA kit APP secretase,APPS,Cathepsin B,Cathepsin B1,CPSB,CTSB,Homo sapiens,Human 96T
CNB-2795549 Recombinant Proteins; Human Cathepsin V _ Cathepsin L2 Protein (His Tag) 100
3192BP-50 Cathepsin L Blocking Peptide target: Cathepsin L (for 3192-100) 50 μg
20-002-35009 Cathepsin H (anti-human Cathepsin H. clone 3G8) - EC 3.4.22.16 Monoclonal 0.1 ml
U0405m CLIA Cathepsin B,Cathepsin B1,Ctsb,Mouse,Mus musculus 96T


 

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