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

Pro-cathepsin H [Cleaved into: Cathepsin H mini chain; Cathepsin H (EC 3.4.22.16); Cathepsin H heavy chain; Cathepsin H light chain]

 CATH_PIG                Reviewed;         335 AA.
O46427;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
25-OCT-2017, entry version 121.
RecName: Full=Pro-cathepsin H;
Contains:
RecName: Full=Cathepsin H mini chain;
Contains:
RecName: Full=Cathepsin H;
EC=3.4.22.16;
Contains:
RecName: Full=Cathepsin H heavy chain;
Contains:
RecName: Full=Cathepsin H light chain;
Flags: Precursor;
Name=CTSH;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
TISSUE=Peripheral blood, and Spleen;
PubMed=9493267; DOI=10.1016/S0969-2126(98)00007-0;
Guncar G., Podobnik M., Pungercar J., Strukelj B., Turk V., Turk D.;
"Crystal structure of porcine cathepsin H determined at 2.1-A
resolution: location of the mini-chain C-terminal carboxyl group
defines cathepsin H aminopeptidase function.";
Structure 6:51-61(1998).
-!- FUNCTION: Important for the overall degradation of proteins in
lysosomes.
-!- CATALYTIC ACTIVITY: Hydrolysis of proteins, acting as an
aminopeptidase (notably, cleaving Arg-|-Xaa bonds) as well as an
endopeptidase.
-!- SUBUNIT: Composed of cathepsin H and mini chain; disulfide-linked.
Cathepsin H may be split into heavy and light chain. All chains
are held together by disulfide bonds.
-!- SUBCELLULAR LOCATION: Lysosome.
-!- SIMILARITY: Belongs to the peptidase C1 family.
{ECO:0000255|PROSITE-ProRule:PRU10088, ECO:0000255|PROSITE-
ProRule:PRU10089, ECO:0000255|PROSITE-ProRule:PRU10090}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF001169; AAB93957.1; -; mRNA.
RefSeq; NP_999094.1; NM_213929.2.
UniGene; Ssc.3593; -.
PDB; 1NB3; X-ray; 2.80 A; A/B/C/D=116-334, P/R/S/T=98-105.
PDB; 1NB5; X-ray; 2.40 A; A/B/C/D=116-334, P/R/S/T=98-105.
PDB; 8PCH; X-ray; 2.10 A; A=116-334, P=98-105.
PDBsum; 1NB3; -.
PDBsum; 1NB5; -.
PDBsum; 8PCH; -.
ProteinModelPortal; O46427; -.
SMR; O46427; -.
IntAct; O46427; 2.
STRING; 9823.ENSSSCP00000001934; -.
MEROPS; C01.040; -.
PaxDb; O46427; -.
PeptideAtlas; O46427; -.
PRIDE; O46427; -.
Ensembl; ENSSSCT00000001983; ENSSSCP00000001934; ENSSSCG00000001770.
GeneID; 396969; -.
KEGG; ssc:396969; -.
CTD; 1512; -.
eggNOG; KOG1543; Eukaryota.
eggNOG; COG4870; LUCA.
GeneTree; ENSGT00900000140823; -.
HOGENOM; HOG000230774; -.
HOVERGEN; HBG011513; -.
InParanoid; O46427; -.
KO; K01366; -.
OMA; IMGEDTY; -.
OrthoDB; EOG091G0AKT; -.
TreeFam; TF328985; -.
Reactome; R-SSC-5683826; Surfactant metabolism.
Reactome; R-SSC-6798695; Neutrophil degranulation.
SABIO-RK; O46427; -.
EvolutionaryTrace; O46427; -.
Proteomes; UP000008227; Chromosome 7.
Bgee; ENSSSCG00000001770; -.
ExpressionAtlas; O46427; differential.
Genevisible; O46427; SS.
GO; GO:0097208; C:alveolar lamellar body; ISS:UniProtKB.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IEA:Ensembl.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
GO; GO:0005764; C:lysosome; ISS:UniProtKB.
GO; GO:0004177; F:aminopeptidase activity; ISS:UniProtKB.
GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; ISS:UniProtKB.
GO; GO:0004197; F:cysteine-type endopeptidase activity; ISS:UniProtKB.
GO; GO:0008234; F:cysteine-type peptidase activity; ISS:UniProtKB.
GO; GO:0004175; F:endopeptidase activity; ISS:UniProtKB.
GO; GO:0030108; F:HLA-A specific activating MHC class I receptor activity; ISS:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; ISS:UniProtKB.
GO; GO:0070324; F:thyroid hormone binding; ISS:UniProtKB.
GO; GO:0010815; P:bradykinin catabolic process; ISS:UniProtKB.
GO; GO:0097067; P:cellular response to thyroid hormone stimulus; IEA:Ensembl.
GO; GO:0060448; P:dichotomous subdivision of terminal units involved in lung branching; ISS:UniProtKB.
GO; GO:0070371; P:ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0006955; P:immune response; IBA:GO_Central.
GO; GO:0002764; P:immune response-regulating signaling pathway; ISS:UniProtKB.
GO; GO:0033619; P:membrane protein proteolysis; ISS:UniProtKB.
GO; GO:0001656; P:metanephros development; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0010813; P:neuropeptide catabolic process; ISS:UniProtKB.
GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IBA:GO_Central.
GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0010634; P:positive regulation of epithelial cell migration; ISS:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
GO; GO:0010952; P:positive regulation of peptidase activity; ISS:UniProtKB.
GO; GO:0031648; P:protein destabilization; ISS:UniProtKB.
GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IBA:GO_Central.
GO; GO:0032526; P:response to retinoic acid; ISS:UniProtKB.
GO; GO:0043129; P:surfactant homeostasis; ISS:UniProtKB.
GO; GO:0001913; P:T cell mediated cytotoxicity; ISS:UniProtKB.
GO; GO:0031638; P:zymogen activation; ISS:UniProtKB.
InterPro; IPR025661; Pept_asp_AS.
InterPro; IPR000169; Pept_cys_AS.
InterPro; IPR025660; Pept_his_AS.
InterPro; IPR013128; Peptidase_C1A.
InterPro; IPR000668; Peptidase_C1A_C.
InterPro; IPR013201; Prot_inhib_I29.
PANTHER; PTHR12411; PTHR12411; 1.
Pfam; PF08246; Inhibitor_I29; 1.
Pfam; PF00112; Peptidase_C1; 1.
PRINTS; PR00705; PAPAIN.
SMART; SM00848; Inhibitor_I29; 1.
SMART; SM00645; Pept_C1; 1.
PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Disulfide bond; Glycoprotein;
Hydrolase; Lysosome; Protease; Reference proteome; Signal;
Thiol protease; Zymogen.
SIGNAL 1 22 {ECO:0000255}.
PROPEP 23 97 {ECO:0000255}.
/FTId=PRO_0000026218.
PEPTIDE 98 105 Cathepsin H mini chain.
/FTId=PRO_0000026219.
PROPEP 107 115
/FTId=PRO_0000026220.
CHAIN 116 335 Cathepsin H.
/FTId=PRO_0000026221.
CHAIN 116 292 Cathepsin H heavy chain. {ECO:0000250}.
/FTId=PRO_0000026222.
CHAIN 293 335 Cathepsin H light chain. {ECO:0000250}.
/FTId=PRO_0000026223.
ACT_SITE 141 141
ACT_SITE 281 281
ACT_SITE 301 301
CARBOHYD 72 72 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 101 101 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 230 230 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 102 327
DISULFID 138 181
DISULFID 172 214
DISULFID 272 322
HELIX 122 125 {ECO:0000244|PDB:8PCH}.
HELIX 141 158 {ECO:0000244|PDB:8PCH}.
HELIX 166 172 {ECO:0000244|PDB:8PCH}.
HELIX 173 176 {ECO:0000244|PDB:8PCH}.
HELIX 180 182 {ECO:0000244|PDB:8PCH}.
HELIX 186 196 {ECO:0000244|PDB:8PCH}.
STRAND 199 201 {ECO:0000244|PDB:8PCH}.
TURN 202 204 {ECO:0000244|PDB:8PCH}.
HELIX 218 220 {ECO:0000244|PDB:8PCH}.
STRAND 221 223 {ECO:0000244|PDB:8PCH}.
STRAND 225 230 {ECO:0000244|PDB:8PCH}.
HELIX 236 245 {ECO:0000244|PDB:8PCH}.
STRAND 249 253 {ECO:0000244|PDB:8PCH}.
HELIX 257 260 {ECO:0000244|PDB:8PCH}.
STRAND 264 267 {ECO:0000244|PDB:8PCH}.
STRAND 270 272 {ECO:0000244|PDB:1NB5}.
TURN 276 278 {ECO:0000244|PDB:8PCH}.
STRAND 281 291 {ECO:0000244|PDB:8PCH}.
STRAND 294 300 {ECO:0000244|PDB:8PCH}.
STRAND 312 316 {ECO:0000244|PDB:8PCH}.
TURN 317 320 {ECO:0000244|PDB:1NB3}.
HELIX 321 323 {ECO:0000244|PDB:8PCH}.
STRAND 329 333 {ECO:0000244|PDB:8PCH}.
SEQUENCE 335 AA; 37455 MW; F728EB45292C3B55 CRC64;
MWAVLSLLCA GAWLLGPPAC GASNLAVSSF EKLHFKSWMV QHQKKYSLEE YHHRLQVFVS
NWRKINAHNA GNHTFKLGLN QFSDMSFDEI RHKYLWSEPQ NCSATKGNYL RGTGPYPPSM
DWRKKGNFVS PVKNQGSCGS CWTFSTTGAL ESAVAIATGK MLSLAEQQLV DCAQNFNNHG
CQGGLPSQAF EYIRYNKGIM GEDTYPYKGQ DDHCKFQPDK AIAFVKDVAN ITMNDEEAMV
EAVALYNPVS FAFEVTNDFL MYRKGIYSST SCHKTPDKVN HAVLAVGYGE ENGIPYWIVK
NSWGPQWGMN GYFLIERGKN MCGLAACASY PIPLV


Related products :

Catalog number Product name Quantity
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
U0267h CLIA Cathepsin K,Cathepsin O,Cathepsin O2,Cathepsin X,CTSK,CTSO,CTSO2,Homo sapiens,Human 96T
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
3741BP-50 Cathepsin L (Cleaved) Blocking Peptide Cathepsin 50 μg
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
3741BP-50 Cathepsin L (Cleaved) Blocking Peptide target: Cathepsin L (Cleaved) 50 μg
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 1 mg
10-663-45680 Procathepsin K Human - EC 3.4.22.38; Cathepsin O; Cathepsin X; Cathepsin O2 N_A 0.01 mg
BM773 Cathepsin D (167_181 heavy chain) 0.2 mg
BM773 Cathepsin D (167_181 heavy chain) 0.2 mg
BM773 Cathepsin D (167_181 heavy chain) 0.2 mg
NB100-62441 Cathepsin D (167_181 heavy chain) 0.2 mg
NB100-62441 Cathepsin D (167_181 heavy chain) 0.2 mg
18-272-196838 Cathepsin B - Sheep polyclonal to Cathepsin B; EC 3.4.22.1; Cathepsin B1; APP secretase; APPS Polyclonal 1 ml
20-783-73093 MOUSE ANTI HUMAN CATHEPSIN D HEAVY CHAIN - EC 3.4.23.5 Monoclonal 0.2 mg
6205 Cathepsin H (Human Liver), purified cathepsin and related proteases 25
6206 Cathepsin L (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


 

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