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Cathepsin E (EC 3.4.23.34) [Cleaved into: Cathepsin E form I; Cathepsin E form II]

 CATE_HUMAN              Reviewed;         396 AA.
P14091; Q5TZ01; Q5TZ02; Q9NY58; Q9UCE3; Q9UCE4;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
28-MAR-2018, sequence version 3.
12-SEP-2018, entry version 197.
RecName: Full=Cathepsin E;
EC=3.4.23.34;
Contains:
RecName: Full=Cathepsin E form I;
Contains:
RecName: Full=Cathepsin E form II;
Flags: Precursor;
Name=CTSE;
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).
TISSUE=Gastric mucosa;
PubMed=2674141;
Azuma T., Pals G., Mohandas T.K., Couvreur J.M., Taggart R.T.;
"Human gastric cathepsin E. Predicted sequence, localization to
chromosome 1, and sequence homology with other aspartic proteinases.";
J. Biol. Chem. 264:16748-16753(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
PubMed=1370478;
Azuma T., Liu W.G., Vander Laan D.J., Bowcock A.M., Taggart R.T.;
"Human gastric cathepsin E gene. Multiple transcripts result from
alternative polyadenylation of the primary transcripts of a single
gene locus at 1q31-q32.";
J. Biol. Chem. 267:1609-1614(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), SUBCELLULAR LOCATION,
AND GLYCOSYLATION.
TISSUE=Intestine;
PubMed=7983070;
Finley E.M., Kornfeld S.;
"Subcellular localization and targeting of cathepsin E.";
J. Biol. Chem. 269:31259-31266(1994).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Gastric adenocarcinoma;
PubMed=12531480; DOI=10.1016/S0167-4781(02)00595-X;
Tatnell P.J., Cook M., Kay J.;
"An alternatively spliced variant of cathepsin E in human gastric
adenocarcinoma cells.";
Biochim. Biophys. Acta 1625:203-206(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Stomach;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
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).
[9]
PROTEIN SEQUENCE OF 20-38 AND 54-76, BIOPHYSICOCHEMICAL PROPERTIES,
AUTOCATALYTIC CLEAVAGE, AND GLYCOSYLATION.
TISSUE=Erythrocyte;
PubMed=8346912; DOI=10.1006/abbi.1993.1361;
Takeda-Ezaki M., Yamamoto K.;
"Isolation and biochemical characterization of procathepsin E from
human erythrocyte membranes.";
Arch. Biochem. Biophys. 304:352-358(1993).
[10]
PROTEIN SEQUENCE OF 54-68; 77-95; 141-154; 275-285 AND 389-396, AND
GLYCOSYLATION.
TISSUE=Gastric mucosa;
PubMed=2334440; DOI=10.1016/0006-291X(90)92403-M;
Athauda S.B.P., Matsuzaki O., Kgeyama T., Takahashi K.;
"Structural evidence for two isozymic forms and the carbohydrate
attachment site of human gastric cathepsin E.";
Biochem. Biophys. Res. Commun. 168:878-885(1990).
[11]
CATALYTIC ACTIVITY, SUBUNIT, DISULFIDE BONDS, AND MUTAGENESIS OF
CYS-60.
PubMed=7789521; DOI=10.1016/0014-5793(95)00501-Y;
Fowler S.D., Kay J., Dunn B.M., Tatnell P.J.;
"Monomeric human cathepsin E.";
FEBS Lett. 366:72-74(1995).
[12]
FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
PubMed=8765029; DOI=10.1002/eji.1830260826;
Sealy L., Mota F., Rayment N., Tatnell P.J., Kay J., Chain B.;
"Regulation of cathepsin E expression during human B cell
differentiation in vitro.";
Eur. J. Immunol. 26:1838-1843(1996).
[13]
TISSUE SPECIFICITY.
PubMed=11322887; DOI=10.1046/j.1432-1327.2001.02159.x;
Cook M., Caswell R.C., Richards R.J., Kay J., Tatnell P.J.;
"Regulation of human and mouse procathepsin E gene expression.";
Eur. J. Biochem. 268:2658-2668(2001).
-!- FUNCTION: May have a role in immune function. Probably involved in
the processing of antigenic peptides during MHC class II-mediated
antigen presentation. May play a role in activation-induced
lymphocyte depletion in the thymus, and in neuronal degeneration
and glial cell activation in the brain.
{ECO:0000269|PubMed:8765029}.
-!- CATALYTIC ACTIVITY: Similar to cathepsin D, but slightly broader
specificity. {ECO:0000269|PubMed:7789521,
ECO:0000269|PubMed:8765029}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.06 mM for hemoglobin {ECO:0000269|PubMed:8346912};
KM=0.13 mM for Pro-Pro-Thr-Ile-Phe-Phe(4-NO2)-Arg-Leu
{ECO:0000269|PubMed:8346912};
KM=0.04 mM for Lys-Pro-Ile-Glu-Phe-Phe(4-NO2)-Arg-Leu
{ECO:0000269|PubMed:8346912};
-!- SUBUNIT: Homodimer; disulfide-linked.
{ECO:0000269|PubMed:7789521}.
-!- SUBCELLULAR LOCATION: Endosome {ECO:0000269|PubMed:7983070}.
Note=The proenzyme is localized to the endoplasmic reticulum and
Golgi apparatus, while the mature enzyme is localized to the
endosome.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P14091-1; Sequence=Displayed;
Name=2;
IsoId=P14091-2; Sequence=VSP_059426;
Name=3;
IsoId=P14091-3; Sequence=VSP_059425;
Note=Dubious isoform produced through aberrant splice sites.
{ECO:0000305};
-!- TISSUE SPECIFICITY: Expressed abundantly in the stomach, the Clara
cells of the lung and activated B-lymphocytes, and at lower levels
in lymph nodes, skin and spleen. Not expressed in resting B-
lymphocytes. {ECO:0000269|PubMed:11322887,
ECO:0000269|PubMed:1370478, ECO:0000269|PubMed:8765029}.
-!- PTM: Glycosylated. The nature of the carbohydrate chain varies
between cell types. In fibroblasts, the proenzyme contains a high
mannose-type oligosaccharide, while the mature enzyme contains a
complex-type oligosaccharide. In erythrocyte membranes, both the
proenzyme and mature enzyme contain a complex-type
oligosaccharide. {ECO:0000269|PubMed:2334440,
ECO:0000269|PubMed:7983070, ECO:0000269|PubMed:8346912}.
-!- PTM: Two forms are produced by autocatalytic cleavage, form I
begins at Ile-54, form II begins at Thr-57.
-!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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EMBL; J05036; AAA52130.1; -; mRNA.
EMBL; M84424; AAA52300.1; -; Genomic_DNA.
EMBL; M84413; AAA52300.1; JOINED; Genomic_DNA.
EMBL; M84417; AAA52300.1; JOINED; Genomic_DNA.
EMBL; M84418; AAA52300.1; JOINED; Genomic_DNA.
EMBL; M84419; AAA52300.1; JOINED; Genomic_DNA.
EMBL; M84420; AAA52300.1; JOINED; Genomic_DNA.
EMBL; M84421; AAA52300.1; JOINED; Genomic_DNA.
EMBL; M84422; AAA52300.1; JOINED; Genomic_DNA.
EMBL; AJ250716; CAB82849.1; -; mRNA.
EMBL; AJ250717; CAB82850.1; -; mRNA.
EMBL; AK292057; BAF84746.1; -; mRNA.
EMBL; BX571818; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471067; EAW91592.1; -; Genomic_DNA.
EMBL; CH471067; EAW91593.1; -; Genomic_DNA.
EMBL; BC042537; AAH42537.1; -; mRNA.
CCDS; CCDS73012.1; -. [P14091-2]
CCDS; CCDS73013.1; -. [P14091-1]
PIR; A42038; A34401.
RefSeq; NP_001304260.1; NM_001317331.1.
RefSeq; NP_001901.1; NM_001910.3. [P14091-1]
RefSeq; NP_683865.1; NM_148964.2. [P14091-2]
UniGene; Hs.644082; -.
PDB; 1LCG; Model; -; A=1-396.
PDB; 1TZS; X-ray; 2.35 A; A=54-396, P=19-53.
PDBsum; 1LCG; -.
PDBsum; 1TZS; -.
ProteinModelPortal; P14091; -.
SMR; P14091; -.
BioGrid; 107890; 8.
IntAct; P14091; 2.
STRING; 9606.ENSP00000350911; -.
BindingDB; P14091; -.
ChEMBL; CHEMBL3092; -.
GuidetoPHARMACOLOGY; 2346; -.
MEROPS; A01.010; -.
iPTMnet; P14091; -.
PhosphoSitePlus; P14091; -.
BioMuta; CTSE; -.
DMDM; 46397366; -.
PaxDb; P14091; -.
PeptideAtlas; P14091; -.
PRIDE; P14091; -.
ProteomicsDB; 53019; -.
ProteomicsDB; 53020; -. [P14091-1]
ProteomicsDB; 53021; -. [P14091-2]
DNASU; 1510; -.
Ensembl; ENST00000358184; ENSP00000350911; ENSG00000196188. [P14091-1]
Ensembl; ENST00000360218; ENSP00000353350; ENSG00000196188. [P14091-2]
GeneID; 1510; -.
KEGG; hsa:1510; -.
UCSC; uc001hdu.3; human. [P14091-1]
CTD; 1510; -.
DisGeNET; 1510; -.
EuPathDB; HostDB:ENSG00000196188.10; -.
GeneCards; CTSE; -.
HGNC; HGNC:2530; CTSE.
HPA; CAB032687; -.
HPA; HPA012940; -.
MIM; 116890; gene.
neXtProt; NX_P14091; -.
OpenTargets; ENSG00000196188; -.
PharmGKB; PA27030; -.
eggNOG; KOG1339; Eukaryota.
eggNOG; ENOG410XNV7; LUCA.
GeneTree; ENSGT00760000118929; -.
HOGENOM; HOG000197681; -.
HOVERGEN; HBG000482; -.
InParanoid; P14091; -.
KO; K01382; -.
OMA; KEPGQTF; -.
OrthoDB; EOG091G0JP7; -.
PhylomeDB; P14091; -.
TreeFam; TF314990; -.
BRENDA; 3.4.23.34; 2681.
Reactome; R-HSA-2132295; MHC class II antigen presentation.
SABIO-RK; P14091; -.
EvolutionaryTrace; P14091; -.
GeneWiki; Cathepsin_E; -.
GenomeRNAi; 1510; -.
PMAP-CutDB; P14091; -.
PRO; PR:P14091; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000196188; Expressed in 96 organ(s), highest expression level in duodenum.
CleanEx; HS_CTSE; -.
Genevisible; P14091; HS.
GO; GO:0005768; C:endosome; IDA:UniProtKB.
GO; GO:0004190; F:aspartic-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IDA:UniProtKB.
GO; GO:0016540; P:protein autoprocessing; IEA:Ensembl.
GO; GO:0030163; P:protein catabolic process; IBA:GO_Central.
Gene3D; 2.40.70.10; -; 2.
InterPro; IPR001461; Aspartic_peptidase_A1.
InterPro; IPR001969; Aspartic_peptidase_AS.
InterPro; IPR012848; Aspartic_peptidase_N.
InterPro; IPR033145; Cathepsin_E.
InterPro; IPR033121; PEPTIDASE_A1.
InterPro; IPR021109; Peptidase_aspartic_dom_sf.
PANTHER; PTHR13683; PTHR13683; 1.
PANTHER; PTHR13683:SF81; PTHR13683:SF81; 1.
Pfam; PF07966; A1_Propeptide; 1.
Pfam; PF00026; Asp; 1.
PRINTS; PR00792; PEPSIN.
SUPFAM; SSF50630; SSF50630; 1.
PROSITE; PS00141; ASP_PROTEASE; 2.
PROSITE; PS51767; PEPTIDASE_A1; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Aspartyl protease;
Autocatalytic cleavage; Complete proteome; Direct protein sequencing;
Disulfide bond; Endosome; Glycoprotein; Hydrolase; Polymorphism;
Protease; Reference proteome; Signal; Zymogen.
SIGNAL 1 19 {ECO:0000269|PubMed:8346912}.
PROPEP 20 53 Activation peptide.
{ECO:0000269|PubMed:2334440,
ECO:0000269|PubMed:8346912}.
/FTId=PRO_0000025974.
CHAIN 54 396 Cathepsin E form I.
/FTId=PRO_0000025975.
CHAIN 57 396 Cathepsin E form II.
/FTId=PRO_0000354668.
DOMAIN 78 396 Peptidase A1. {ECO:0000255|PROSITE-
ProRule:PRU01103}.
ACT_SITE 96 96 {ECO:0000255|PROSITE-ProRule:PRU10094}.
ACT_SITE 281 281 {ECO:0000255|PROSITE-ProRule:PRU10094}.
CARBOHYD 90 90 N-linked (GlcNAc...) asparagine.
DISULFID 60 60 Interchain. {ECO:0000269|PubMed:7789521}.
DISULFID 109 114 {ECO:0000250}.
DISULFID 272 276 {ECO:0000250}.
DISULFID 314 351 {ECO:0000250}.
VAR_SEQ 154 154 S -> SAFATQ (in isoform 3).
{ECO:0000303|PubMed:7983070}.
/FTId=VSP_059425.
VAR_SEQ 263 395 IQVGGTVMFCSEGCQAIVDTGTSLITGPSDKIKQLQNAIGA
APVDGEYAVECANLNVMPDVTFTINGVPYTLSPTAYTLLDF
VDGMQFCSSGFQGLDIHPPAGPLWILGDVFIRQFYSVFDRG
NNRVGLAPAV -> MLWSVPTLTSCRMSPSPLTESPIPSAQ
LPTPYWTSWMECSSAAVAFKDLTSTLQLGPSGSWGMSSFDS
FTQSLTVGITVWDWPQQSPKEGPCVCACLSDR (in
isoform 2).
{ECO:0000303|PubMed:12531480}.
/FTId=VSP_059426.
VARIANT 82 82 I -> V (in dbSNP:rs57621203).
/FTId=VAR_061731.
VARIANT 324 324 T -> I (in dbSNP:rs6503).
/FTId=VAR_014572.
MUTAGEN 60 60 C->A: Abolishes homodimerization.
{ECO:0000269|PubMed:7789521}.
STRAND 22 25 {ECO:0000244|PDB:1TZS}.
HELIX 71 73 {ECO:0000244|PDB:1TZS}.
STRAND 74 76 {ECO:0000244|PDB:1TZS}.
STRAND 79 84 {ECO:0000244|PDB:1TZS}.
TURN 85 88 {ECO:0000244|PDB:1TZS}.
STRAND 89 96 {ECO:0000244|PDB:1TZS}.
STRAND 102 106 {ECO:0000244|PDB:1TZS}.
HELIX 112 114 {ECO:0000244|PDB:1TZS}.
HELIX 122 124 {ECO:0000244|PDB:1TZS}.
STRAND 134 141 {ECO:0000244|PDB:1TZS}.
STRAND 143 155 {ECO:0000244|PDB:1TZS}.
STRAND 158 168 {ECO:0000244|PDB:1TZS}.
HELIX 174 178 {ECO:0000244|PDB:1TZS}.
STRAND 182 186 {ECO:0000244|PDB:1TZS}.
HELIX 190 192 {ECO:0000244|PDB:1TZS}.
HELIX 194 196 {ECO:0000244|PDB:1TZS}.
HELIX 200 206 {ECO:0000244|PDB:1TZS}.
STRAND 211 218 {ECO:0000244|PDB:1TZS}.
STRAND 230 233 {ECO:0000244|PDB:1TZS}.
HELIX 238 240 {ECO:0000244|PDB:1TZS}.
STRAND 246 249 {ECO:0000244|PDB:1TZS}.
TURN 253 256 {ECO:0000244|PDB:1TZS}.
STRAND 257 265 {ECO:0000244|PDB:1TZS}.
STRAND 268 271 {ECO:0000244|PDB:1TZS}.
STRAND 276 280 {ECO:0000244|PDB:1TZS}.
STRAND 285 289 {ECO:0000244|PDB:1TZS}.
HELIX 291 301 {ECO:0000244|PDB:1TZS}.
STRAND 307 312 {ECO:0000244|PDB:1TZS}.
HELIX 314 319 {ECO:0000244|PDB:1TZS}.
STRAND 323 327 {ECO:0000244|PDB:1TZS}.
STRAND 330 334 {ECO:0000244|PDB:1TZS}.
TURN 336 338 {ECO:0000244|PDB:1TZS}.
STRAND 339 341 {ECO:0000244|PDB:1TZS}.
STRAND 351 357 {ECO:0000244|PDB:1TZS}.
TURN 362 364 {ECO:0000244|PDB:1TZS}.
STRAND 368 370 {ECO:0000244|PDB:1TZS}.
HELIX 372 377 {ECO:0000244|PDB:1TZS}.
STRAND 378 383 {ECO:0000244|PDB:1TZS}.
TURN 384 387 {ECO:0000244|PDB:1TZS}.
STRAND 388 394 {ECO:0000244|PDB:1TZS}.
SEQUENCE 396 AA; 42794 MW; 40B643C5FB01521E CRC64;
MKTLLLLLLV LLELGEAQGS LHRVPLRRHP SLKKKLRARS QLSEFWKSHN LDMIQFTESC
SMDQSAKEPL INYLDMEYFG TISIGSPPQN FTVIFDTGSS NLWVPSVYCT SPACKTHSRF
QPSQSSTYSQ PGQSFSIQYG TGSLSGIIGA DQVSVEGLTV VGQQFGESVT EPGQTFVDAE
FDGILGLGYP SLAVGGVTPV FDNMMAQNLV DLPMFSVYMS SNPEGGAGSE LIFGGYDHSH
FSGSLNWVPV TKQAYWQIAL DNIQVGGTVM FCSEGCQAIV DTGTSLITGP SDKIKQLQNA
IGAAPVDGEY AVECANLNVM PDVTFTINGV PYTLSPTAYT LLDFVDGMQF CSSGFQGLDI
HPPAGPLWIL GDVFIRQFYS VFDRGNNRVG LAPAVP


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Catalog number Product name Quantity
U0267h CLIA Cathepsin K,Cathepsin O,Cathepsin O2,Cathepsin X,CTSK,CTSO,CTSO2,Homo sapiens,Human 96T
E0267h ELISA Cathepsin K,Cathepsin O,Cathepsin O2,Cathepsin X,CTSK,CTSO,CTSO2,Homo sapiens,Human 96T
E0267h ELISA kit Cathepsin K,Cathepsin O,Cathepsin O2,Cathepsin X,CTSK,CTSO,CTSO2,Homo sapiens,Human 96T
3741BP-50 Cathepsin L (Cleaved) Blocking Peptide target: Cathepsin L (Cleaved) 50 μg
3741BP-50 Cathepsin L (Cleaved) Blocking Peptide Cathepsin 50 μg
EIAAB05436 Cathepsin L2,Cathepsin U,Cathepsin V,CATL2,CTSL2,CTSU,CTSV,Homo sapiens,Human,UNQ268_PRO305
EIAAB05434 Cathepsin J,Cathepsin L-related protein,Cathepsin P,Catlrp-p,Ctsj,Ctsp,Mouse,Mus musculus
EIAAB05433 Cathepsin J,Cathepsin L-related protein,Cathepsin P,Catlrp-p,Ctsj,Ctsp,Rat,Rattus norvegicus
EIAAB05448 Cathepsin P,Cathepsin X,Cathepsin Z,CTSZ,Homo sapiens,Human
EIAAB05431 Cathepsin B3,Cathepsin BA,Ctsh,Mouse,Mus musculus,Pro-cathepsin H
orb90060 Human Cathepsin L protein Cathepsin Human Recombinant (aa 1-87) expressed in E.coli, shows 38 kDa band on SDS-PAGE.The Cathepsin is purified by proprietary chromatographic techniques. For research use 2
10-663-45680 Procathepsin K Human - EC 3.4.22.38; Cathepsin O; Cathepsin X; Cathepsin O2 N_A 0.002 mg
10-663-45680 Procathepsin K Human - EC 3.4.22.38; Cathepsin O; Cathepsin X; Cathepsin O2 N_A 0.01 mg
10-663-45680 Procathepsin K Human - EC 3.4.22.38; Cathepsin O; Cathepsin X; Cathepsin O2 N_A 1 mg
BMDV2111 Cathepsin D, precursor & activated form, Rabbit anti_Human 0.5 ml.
18-272-196838 Cathepsin B - Sheep polyclonal to Cathepsin B; EC 3.4.22.1; Cathepsin B1; APP secretase; APPS Polyclonal 1 ml
6205 Cathepsin H (Human Liver), purified cathepsin and related proteases 25
6202 Cathepsin B (Human Liver), purified cathepsin and related proteases 25
6204 Cathepsin G (Human Neutrophil), purified cathepsin and related proteases 100
6203 Cathepsin D (Human Liver), purified cathepsin and related proteases 25
6206 Cathepsin L (Human Liver), purified cathepsin and related proteases 25
E0405h ELISA kit 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
U0405h CLIA APP secretase,APPS,Cathepsin B,Cathepsin B1,CPSB,CTSB,Homo sapiens,Human 96T
20-002-35038 Cathepsin D (anti-human Cathepsin D. clone 4G2) - EC 3.4.23.5 Monoclonal 0.05 ml


 

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