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Furin (EC 3.4.21.75) (Dibasic-processing enzyme) (Paired basic amino acid residue-cleaving enzyme) (PACE) (Prohormone convertase 3)

 FURIN_MOUSE             Reviewed;         793 AA.
P23188; Q6GTN6;
01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
22-NOV-2017, entry version 178.
RecName: Full=Furin;
EC=3.4.21.75 {ECO:0000250|UniProtKB:P09958};
AltName: Full=Dibasic-processing enzyme;
AltName: Full=Paired basic amino acid residue-cleaving enzyme;
Short=PACE;
AltName: Full=Prohormone convertase 3;
Flags: Precursor;
Name=Furin; Synonyms=Fur, Pcsk3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
PubMed=2266110;
Hatsuzawa K., Hosaka M., Nakagawa T., Nagase M., Shoda A.,
Murakami K., Nakayama K.;
"Structure and expression of mouse furin, a yeast Kex2-related
protease. Lack of processing of coexpressed prorenin in GH4C1 cells.";
J. Biol. Chem. 265:22075-22078(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
Creemers J.W.M., Roebroek A.J.M., van den Ouweland A.M.W.,
van Duijnhoven H.L.P., van de Ven W.J.M.;
"Cloning and functional expression of a 4.3 kbp mouse fur cDNA:
evidence for differential expression.";
Life Sci. Adv. (Mol. Biol.) 11:127-138(1992).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye;
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).
[5]
INTERACTION WITH FLNA.
PubMed=9412467; DOI=10.1083/jcb.139.7.1719;
Liu G., Thomas L., Warren R.A., Enns C.A., Cunningham C.C.,
Hartwig J.H., Thomas G.;
"Cytoskeletal protein ABP-280 directs the intracellular trafficking of
furin and modulates proprotein processing in the endocytic pathway.";
J. Cell Biol. 139:1719-1733(1997).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 108-578 IN COMPLEX WITH
CALCIUM AND INHIBITOR, GLYCOSYLATION AT ASN-387 AND ASN-440, AND
DISULFIDE BONDS.
PubMed=12794637; DOI=10.1038/nsb941;
Henrich S., Cameron A., Bourenkov G.P., Kiefersauer R., Huber R.,
Lindberg I., Bode W., Than M.E.;
"The crystal structure of the proprotein processing proteinase furin
explains its stringent specificity.";
Nat. Struct. Biol. 10:520-526(2003).
-!- FUNCTION: Furin is likely to represent the ubiquitous endoprotease
activity within constitutive secretory pathways and capable of
cleavage at the RX(K/R)R consensus motif.
{ECO:0000250|UniProtKB:P09958}.
-!- CATALYTIC ACTIVITY: Release of mature proteins from their
proproteins by cleavage of -Arg-Xaa-Yaa-Arg-|-Zaa- bonds, where
Xaa can be any amino acid and Yaa is Arg or Lys. Releases albumin,
complement component C3 and von Willebrand factor from their
respective precursors. {ECO:0000250|UniProtKB:P09958}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:12794637};
Note=Binds 3 calcium ions per subunit.
{ECO:0000250|UniProtKB:P09958};
-!- ENZYME REGULATION: Inhibited by the not secondly cleaved
propeptide. Inhibited by m-guanidinomethyl-phenylacetyl-Arg-Val-
Arg-(amidomethyl)-benzamidine (m-guanidinomethyl-Phac-RVR-Amb) and
4-guanidinomethyl-phenylacteyl-Arg-Tle-Arg-4-amidinobenzylamide
(MI-1148). {ECO:0000250|UniProtKB:P09958}.
-!- SUBUNIT: Interacts with FLNA (PubMed:9412467). Binds to PACS1
which mediates TGN localization and connection to clathrin
adapters (By similarity). {ECO:0000250|UniProtKB:P09958,
ECO:0000269|PubMed:9412467}.
-!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
membrane {ECO:0000250|UniProtKB:P09958}; Single-pass type I
membrane protein {ECO:0000305}. Cell membrane
{ECO:0000250|UniProtKB:P09958}; Single-pass type I membrane
protein {ECO:0000305}. Secreted {ECO:0000250|UniProtKB:Q28193}.
Endosome membrane {ECO:0000250|UniProtKB:P09958}; Single-pass type
I membrane protein {ECO:0000305}. Note=Shuttles between the trans-
Golgi network and the cell surface. Propeptide cleavage is a
prerequisite for exit of furin molecules out of the endoplasmic
reticulum (ER). A second cleavage within the propeptide occurs in
the trans Golgi network (TGN), followed by the release of the
propeptide and the activation of furin.
{ECO:0000250|UniProtKB:P09958}.
-!- TISSUE SPECIFICITY: Seems to be expressed ubiquitously.
{ECO:0000269|PubMed:2266110}.
-!- DOMAIN: Contains a cytoplasmic domain responsible for its TGN
localization and recycling from the cell surface.
{ECO:0000250|UniProtKB:P09958}.
-!- PTM: The inhibition peptide, which plays the role of an
intramolecular chaperone, is autocatalytically removed in the
endoplasmic reticulum (ER) and remains non-covalently bound to
furin as a potent autoinhibitor. Following transport to the trans
Golgi, a second cleavage within the inhibition propeptide results
in propeptide dissociation and furin activation.
{ECO:0000250|UniProtKB:P09958}.
-!- PTM: Phosphorylation is required for TGN localization of the
endoprotease. In vivo, exists as di-, mono- and non-phosphorylated
forms. {ECO:0000250|UniProtKB:P09958}.
-!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
{ECO:0000305}.
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EMBL; X54056; CAA37988.1; -; mRNA.
EMBL; L26489; AAA37643.1; -; mRNA.
EMBL; CH466543; EDL06988.1; -; Genomic_DNA.
EMBL; BC048234; AAH48234.1; -; mRNA.
CCDS; CCDS21397.1; -.
PIR; A23679; KXMSF.
RefSeq; NP_001074923.1; NM_001081454.2.
RefSeq; NP_035176.1; NM_011046.3.
UniGene; Mm.5241; -.
PDB; 1P8J; X-ray; 2.60 A; A/B/C/D/E/F/G/H=108-578.
PDBsum; 1P8J; -.
ProteinModelPortal; P23188; -.
SMR; P23188; -.
ELM; P23188; -.
STRING; 10090.ENSMUSP00000102985; -.
MEROPS; S08.071; -.
iPTMnet; P23188; -.
PhosphoSitePlus; P23188; -.
EPD; P23188; -.
MaxQB; P23188; -.
PaxDb; P23188; -.
PeptideAtlas; P23188; -.
PRIDE; P23188; -.
Ensembl; ENSMUST00000107362; ENSMUSP00000102985; ENSMUSG00000030530.
Ensembl; ENSMUST00000120753; ENSMUSP00000113793; ENSMUSG00000030530.
Ensembl; ENSMUST00000122232; ENSMUSP00000113370; ENSMUSG00000030530.
GeneID; 18550; -.
KEGG; mmu:18550; -.
UCSC; uc009iau.1; mouse.
CTD; 5045; -.
MGI; MGI:97513; Furin.
eggNOG; KOG3525; Eukaryota.
eggNOG; COG1404; LUCA.
eggNOG; COG4935; LUCA.
GeneTree; ENSGT00750000117358; -.
HOGENOM; HOG000192536; -.
HOVERGEN; HBG008705; -.
InParanoid; P23188; -.
KO; K01349; -.
OMA; PRPHDYS; -.
OrthoDB; EOG091G05HI; -.
TreeFam; TF314277; -.
Reactome; R-MMU-1442490; Collagen degradation.
Reactome; R-MMU-1566948; Elastic fibre formation.
Reactome; R-MMU-1592389; Activation of Matrix Metalloproteinases.
Reactome; R-MMU-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
Reactome; R-MMU-167060; NGF processing.
Reactome; R-MMU-186797; Signaling by PDGF.
Reactome; R-MMU-1912420; Pre-NOTCH Processing in Golgi.
Reactome; R-MMU-2173789; TGF-beta receptor signaling activates SMADs.
Reactome; R-MMU-6809371; Formation of the cornified envelope.
Reactome; R-MMU-8963889; Assembly of active LPL and LIPC lipase complexes.
EvolutionaryTrace; P23188; -.
PMAP-CutDB; Q6GTN6; -.
PRO; PR:P23188; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000030530; -.
CleanEx; MM_FURIN; -.
ExpressionAtlas; P23188; baseline and differential.
Genevisible; P23188; MM.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0005769; C:early endosome; TAS:MGI.
GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0000139; C:Golgi membrane; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; TAS:MGI.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0045121; C:membrane raft; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
GO; GO:0030140; C:trans-Golgi network transport vesicle; ISO:MGI.
GO; GO:0012510; C:trans-Golgi network transport vesicle membrane; TAS:MGI.
GO; GO:0004175; F:endopeptidase activity; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0048406; F:nerve growth factor binding; ISO:MGI.
GO; GO:0008233; F:peptidase activity; ISO:MGI.
GO; GO:0042277; F:peptide binding; ISO:MGI.
GO; GO:0002020; F:protease binding; ISO:MGI.
GO; GO:0004252; F:serine-type endopeptidase activity; EXP:Reactome.
GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; ISO:MGI.
GO; GO:0008283; P:cell proliferation; ISO:MGI.
GO; GO:0030574; P:collagen catabolic process; TAS:Reactome.
GO; GO:0090472; P:dibasic protein processing; ISO:MGI.
GO; GO:0032804; P:negative regulation of low-density lipoprotein particle receptor catabolic process; ISO:MGI.
GO; GO:0032911; P:negative regulation of transforming growth factor beta1 production; ISO:MGI.
GO; GO:0032455; P:nerve growth factor processing; TAS:Reactome.
GO; GO:0032902; P:nerve growth factor production; ISO:MGI.
GO; GO:0043043; P:peptide biosynthetic process; ISO:MGI.
GO; GO:0016486; P:peptide hormone processing; ISO:MGI.
GO; GO:0016485; P:protein processing; IDA:MGI.
GO; GO:0052548; P:regulation of endopeptidase activity; ISO:MGI.
GO; GO:0045714; P:regulation of low-density lipoprotein particle receptor biosynthetic process; IMP:MGI.
GO; GO:0042176; P:regulation of protein catabolic process; ISO:MGI.
GO; GO:0009966; P:regulation of signal transduction; IDA:MGI.
GO; GO:0032940; P:secretion by cell; ISO:MGI.
GO; GO:0006465; P:signal peptide processing; ISO:MGI.
GO; GO:0019058; P:viral life cycle; IEA:Ensembl.
GO; GO:0031638; P:zymogen activation; ISO:MGI.
CDD; cd04059; Peptidases_S8_Protein_converta; 1.
Gene3D; 2.60.120.260; -; 1.
Gene3D; 3.40.50.200; -; 1.
InterPro; IPR006212; Furin_repeat.
InterPro; IPR008979; Galactose-bd-like_sf.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR034182; Kexin/furin.
InterPro; IPR009020; Peptidase/Inhibitor_I9.
InterPro; IPR000209; Peptidase_S8/S53_dom.
InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
InterPro; IPR023827; Peptidase_S8_Asp-AS.
InterPro; IPR022398; Peptidase_S8_His-AS.
InterPro; IPR023828; Peptidase_S8_Ser-AS.
InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
InterPro; IPR002884; PrprotnconvertsP.
InterPro; IPR032815; S8_pro-domain.
Pfam; PF01483; P_proprotein; 1.
Pfam; PF00082; Peptidase_S8; 1.
Pfam; PF16470; S8_pro-domain; 1.
PRINTS; PR00723; SUBTILISIN.
SMART; SM00261; FU; 2.
SUPFAM; SSF49785; SSF49785; 1.
SUPFAM; SSF52743; SSF52743; 1.
SUPFAM; SSF54897; SSF54897; 1.
SUPFAM; SSF57184; SSF57184; 1.
PROSITE; PS51829; P_HOMO_B; 1.
PROSITE; PS00136; SUBTILASE_ASP; 1.
PROSITE; PS00137; SUBTILASE_HIS; 1.
PROSITE; PS00138; SUBTILASE_SER; 1.
1: Evidence at protein level;
3D-structure; Autocatalytic cleavage; Calcium; Cell membrane;
Cleavage on pair of basic residues; Complete proteome; Disulfide bond;
Endosome; Glycoprotein; Golgi apparatus; Hydrolase; Membrane;
Metal-binding; Phosphoprotein; Protease; Reference proteome; Repeat;
Secreted; Serine protease; Signal; Transmembrane; Transmembrane helix;
Zymogen.
SIGNAL 1 24 {ECO:0000255}.
PROPEP 25 107 Inhibition peptide.
{ECO:0000250|UniProtKB:P09958}.
/FTId=PRO_0000027030.
CHAIN 108 793 Furin.
/FTId=PRO_0000027031.
TOPO_DOM 108 714 Lumenal. {ECO:0000305}.
TRANSMEM 715 735 Helical. {ECO:0000255}.
TOPO_DOM 736 793 Cytoplasmic. {ECO:0000305}.
DOMAIN 144 427 Peptidase S8. {ECO:0000255}.
DOMAIN 444 576 P/Homo B. {ECO:0000255|PROSITE-
ProRule:PRU01173}.
REPEAT 577 620 FU 1. {ECO:0000255}.
REPEAT 638 681 FU 2. {ECO:0000255}.
REGION 191 192 Substrate binding. {ECO:0000244|PDB:1P8J,
ECO:0000305|PubMed:12794637}.
REGION 253 258 Substrate binding. {ECO:0000244|PDB:1P8J,
ECO:0000305|PubMed:12794637}.
REGION 292 295 Substrate binding. {ECO:0000244|PDB:1P8J,
ECO:0000305|PubMed:12794637}.
REGION 758 761 Cell surface signal.
{ECO:0000250|UniProtKB:P09958}.
MOTIF 498 500 Cell attachment site.
{ECO:0000255|PROSITE-ProRule:PRU00293}.
MOTIF 772 778 Trans Golgi network signal.
{ECO:0000250|UniProtKB:P09958}.
ACT_SITE 153 153 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU10080}.
ACT_SITE 194 194 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU10081}.
ACT_SITE 368 368 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU10082}.
METAL 115 115 Calcium 1. {ECO:0000244|PDB:1P8J,
ECO:0000269|PubMed:12794637}.
METAL 162 162 Calcium 1. {ECO:0000244|PDB:1P8J,
ECO:0000269|PubMed:12794637}.
METAL 174 174 Calcium 2.
{ECO:0000250|UniProtKB:P09958}.
METAL 179 179 Calcium 2.
{ECO:0000250|UniProtKB:P09958}.
METAL 181 181 Calcium 2; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P09958}.
METAL 205 205 Calcium 1; via carbonyl oxygen.
{ECO:0000244|PDB:1P8J,
ECO:0000269|PubMed:12794637}.
METAL 208 208 Calcium 1. {ECO:0000244|PDB:1P8J,
ECO:0000269|PubMed:12794637}.
METAL 210 210 Calcium 1; via carbonyl oxygen.
{ECO:0000244|PDB:1P8J,
ECO:0000269|PubMed:12794637}.
METAL 212 212 Calcium 1; via carbonyl oxygen.
{ECO:0000244|PDB:1P8J,
ECO:0000269|PubMed:12794637}.
METAL 258 258 Calcium 3. {ECO:0000244|PDB:1P8J,
ECO:0000269|PubMed:12794637}.
METAL 301 301 Calcium 3. {ECO:0000244|PDB:1P8J,
ECO:0000269|PubMed:12794637}.
METAL 331 331 Calcium 3. {ECO:0000244|PDB:1P8J,
ECO:0000269|PubMed:12794637}.
BINDING 154 154 Substrate. {ECO:0000244|PDB:1P8J,
ECO:0000305|PubMed:12794637}.
BINDING 236 236 Substrate. {ECO:0000244|PDB:1P8J,
ECO:0000305|PubMed:12794637}.
BINDING 264 264 Substrate. {ECO:0000244|PDB:1P8J,
ECO:0000305|PubMed:12794637}.
BINDING 306 306 Substrate. {ECO:0000244|PDB:1P8J,
ECO:0000305|PubMed:12794637}.
BINDING 308 308 Substrate. {ECO:0000244|PDB:1P8J,
ECO:0000305|PubMed:12794637}.
BINDING 368 368 Substrate. {ECO:0000244|PDB:1P8J,
ECO:0000305|PubMed:12794637}.
SITE 75 76 Cleavage, second; by autolysis.
{ECO:0000250|UniProtKB:P09958}.
SITE 107 108 Cleavage, first; by autolysis.
{ECO:0000250|UniProtKB:P09958}.
MOD_RES 772 772 Phosphoserine.
{ECO:0000250|UniProtKB:P09958}.
MOD_RES 774 774 Phosphoserine.
{ECO:0000250|UniProtKB:P09958}.
CARBOHYD 387 387 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:1P8J,
ECO:0000269|PubMed:12794637}.
CARBOHYD 440 440 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:1P8J,
ECO:0000269|PubMed:12794637}.
DISULFID 211 360 {ECO:0000269|PubMed:12794637}.
DISULFID 303 333 {ECO:0000269|PubMed:12794637}.
DISULFID 450 474 {ECO:0000269|PubMed:12794637}.
CONFLICT 746 746 V -> M (in Ref. 1; CAA37988).
{ECO:0000305}.
HELIX 118 120 {ECO:0000244|PDB:1P8J}.
TURN 122 124 {ECO:0000244|PDB:1P8J}.
HELIX 135 139 {ECO:0000244|PDB:1P8J}.
STRAND 148 154 {ECO:0000244|PDB:1P8J}.
TURN 161 163 {ECO:0000244|PDB:1P8J}.
HELIX 164 166 {ECO:0000244|PDB:1P8J}.
HELIX 169 171 {ECO:0000244|PDB:1P8J}.
TURN 175 178 {ECO:0000244|PDB:1P8J}.
HELIX 194 203 {ECO:0000244|PDB:1P8J}.
STRAND 206 211 {ECO:0000244|PDB:1P8J}.
TURN 215 218 {ECO:0000244|PDB:1P8J}.
STRAND 219 225 {ECO:0000244|PDB:1P8J}.
STRAND 227 229 {ECO:0000244|PDB:1P8J}.
HELIX 233 240 {ECO:0000244|PDB:1P8J}.
TURN 244 246 {ECO:0000244|PDB:1P8J}.
STRAND 249 252 {ECO:0000244|PDB:1P8J}.
STRAND 259 261 {ECO:0000244|PDB:1P8J}.
HELIX 268 280 {ECO:0000244|PDB:1P8J}.
HELIX 282 284 {ECO:0000244|PDB:1P8J}.
STRAND 288 292 {ECO:0000244|PDB:1P8J}.
HELIX 297 299 {ECO:0000244|PDB:1P8J}.
HELIX 303 305 {ECO:0000244|PDB:1P8J}.
TURN 307 310 {ECO:0000244|PDB:1P8J}.
STRAND 314 320 {ECO:0000244|PDB:1P8J}.
STRAND 338 341 {ECO:0000244|PDB:1P8J}.
STRAND 351 355 {ECO:0000244|PDB:1P8J}.
TURN 356 358 {ECO:0000244|PDB:1P8J}.
STRAND 359 364 {ECO:0000244|PDB:1P8J}.
HELIX 367 384 {ECO:0000244|PDB:1P8J}.
HELIX 390 400 {ECO:0000244|PDB:1P8J}.
STRAND 419 421 {ECO:0000244|PDB:1P8J}.
TURN 422 424 {ECO:0000244|PDB:1P8J}.
HELIX 431 438 {ECO:0000244|PDB:1P8J}.
STRAND 448 455 {ECO:0000244|PDB:1P8J}.
STRAND 464 471 {ECO:0000244|PDB:1P8J}.
STRAND 482 496 {ECO:0000244|PDB:1P8J}.
HELIX 498 500 {ECO:0000244|PDB:1P8J}.
STRAND 501 506 {ECO:0000244|PDB:1P8J}.
STRAND 512 516 {ECO:0000244|PDB:1P8J}.
STRAND 528 535 {ECO:0000244|PDB:1P8J}.
TURN 537 540 {ECO:0000244|PDB:1P8J}.
STRAND 545 553 {ECO:0000244|PDB:1P8J}.
STRAND 555 557 {ECO:0000244|PDB:1P8J}.
STRAND 561 573 {ECO:0000244|PDB:1P8J}.
SEQUENCE 793 AA; 86772 MW; 0F120C2DE2E1A431 CRC64;
MELRSWLLWV VAAAGAVVLL AADAQGQKIF TNTWAVHIPG GPAVADRVAQ KHGFHNLGQI
FGDYYHFWHR AVTKRSLSPH RPRHSRLQRE PQVKWLEQQV AKRRAKRDVY QEPTDPKFPQ
QWYLSGVTQR DLNVKEAWAQ GFTGHGIVVS ILDDGIEKNH PDLAGNYDPG ASFDVNDQDP
DPQPRYTQMN DNRHGTRCAG EVAAVANNGV CGVGVAYNAR IGGVRMLDGE VTDAVEARSL
GLNPNHIHIY SASWGPEDDG KTVDGPARLA EEAFFRGVSQ GRGGLGSIFV WASGNGGREH
DSCNCDGYTN SIYTLSISSA TQFGNVPWYS EACSSTLATT YSSGNQNEKQ IVTTDLRQKC
TESHTGTSAS APLAAGIIAL TLEANKNLTW RDMQHLVVQT SKPAHLNADD WATNGVGRKV
SHSYGYGLLD AGAMVALAQN WTTVAPQRKC IVEILVEPKD IGKRLEVRKA VTACLGEPNH
ITRLEHVQAR LTLSYNRRGD LAIHLISPMG TRSTLLAARP HDYSADGFND WAFMTTHSWD
EDPAGEWVLE IENTSEANNY GTLTKFTLVL YGTAPEGLST PPESSGCKTL TSSQACVVCE
EGYSLHQKSC VQHCPPGFIP QVLDTHYSTE NDVEIIRASV CTPCHASCAT CQGPAPTDCL
SCPSHASLDP VEQTCSRQSQ SSRESRPQQQ PPALRPEVEM EPRLQAGLAS HLPEVLAGLS
CLIIVLIFGI VFLFLHRCSG FSFRGVKVYT MDRGLISYKG LPPEAWQEEC PSDSEEDEGR
GERTAFIKDQ SAL


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FUR-354E Protein: Recombinant Human Furin (Paired Basic Amino Acid Cleaving Enzyme) 20ug
FUR-354E Protein Recombinant Human Furin (Paired Basic Amino Acid Cleaving Enzyme) 20ug
CSB-EL009068HU Human furin (paired basic amino acid cleaving enzyme) (FURIN) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL009068BO Bovine furin (paired basic amino acid cleaving enzyme) (FURIN) ELISA kit, Species Bovine, Sample Type serum, plasma 96T
CSB-EL009068MO Mouse furin (paired basic amino acid cleaving enzyme) (FURIN) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
Y051641 Anti-PC9 (paired basic amino acid cleaving enzyme-9, PCSK9, proprotein convertase subtilisin_kexin type 9a, NARC-1, neural apoptosis regulated convertase 1); CT domain Antibody 100μg
Y051640 Anti-PC9 (paired basic amino acid cleaving enzyme-9, PCSK9, proprotein convertase subtilisin_kexin type 9a, NARC-1, neural apoptosis regulated convertase 1); Propeptide domain Antibody 100μg
Y051641 Anti-PC9 paired basic amino acid cleaving enzyme-9 PCSK9 proprotein convertase subtilisin per kexin type 9a NARC-1 neural apoptosis regulated convertase 1; CT domain antibody 250ug
Y051635 to PC4 (paired basic amino acid cleaving enzyme-4, PC4, PCSK4, Neuroendocrine Convertase-3); Homo-B domain Antibody 100μg
Y051635 to PC4 paired basic amino acid cleaving enzyme-4 PC4 PCSK4 Neuroendocrine Convertase-3; Homo-B domain antibody 250ug
Y051640 Anti-PC9 paired basic amino acid cleaving enzyme-9 PCSK9 proprotein convertase subtilisin per kexin type 9a NARC-1 neural apoptosis regulated convertase 1; Propeptide domain antibody 250ug
Y051632 Anti-PC2 (paired basic amino acid cleaving enzyme-2, SPC2); Amino end mature enzyme Antibody 100μg
Y051632 Anti-PC2 paired basic amino acid cleaving enzyme-2 SPC2; Amino end mature enzyme antibody 250ug
Y051636 Anti-PC5 (paired basic amino acid cleaving enzyme-5, PC5, PC6, PC5_6); Amino end mature enzyme Antibody 100μg
Y051639 Anti-PC7 (paired basic amino acid cleaving enzyme-7, PC7, PCKS7, SPC7, C8, PC8, LPC); Amino end mature enzyme Antibody 100μg
Y051642 Anti-PACE4 (paired basic amino acid cleaving enzyme-4, SPC4); Amino end mature enzyme Antibody 100μg
Y051642 Anti-PACE4 paired basic amino acid cleaving enzyme-4 SPC4; Amino end mature enzyme antibody 250ug
Y051639 Anti-PC7 paired basic amino acid cleaving enzyme-7 PC7 PCKS7 SPC7 C8 PC8 LPC; Amino end mature enzyme antibody 250ug
Y051638 Anti-PC7 paired basic amino acid cleaving enzyme-7 PC7 PCKS7 SPC7 C8 PC8 LPC; Amino end mature enzyme antibody 250ug
Y051638 Anti-PC7 (paired basic amino acid cleaving enzyme-7, PC7, PCKS7, SPC7, C8, PC8, LPC); Amino end mature enzyme Antibody 100μg
Y051636 Anti-PC5 paired basic amino acid cleaving enzyme-5 PC5 PC6 PC5 per 6; Amino end mature enzyme antibody 250ug


 

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