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Neuroendocrine convertase 1 (NEC 1) (EC 3.4.21.93) (Prohormone convertase 1) (Proprotein convertase 1) (PC1)

 NEC1_HUMAN              Reviewed;         753 AA.
P29120; B7Z8T7; E9PHA1; P78478; Q92532;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 2.
27-SEP-2017, entry version 173.
RecName: Full=Neuroendocrine convertase 1;
Short=NEC 1;
EC=3.4.21.93;
AltName: Full=Prohormone convertase 1;
AltName: Full=Proprotein convertase 1;
Short=PC1;
Flags: Precursor;
Name=PCSK1; Synonyms=NEC1;
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).
PubMed=1547893; DOI=10.1016/0014-5793(92)80169-H;
Creemers J.W.M., Roebroek A.J.M., van de Ven W.J.M.;
"Expression in human lung tumor cells of the proprotein processing
enzyme PC1/PC3. Cloning and primary sequence of a 5 kb cDNA.";
FEBS Lett. 300:82-88(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1605851; DOI=10.1089/dna.1992.11.283;
Seidah N.G., Hamelin J., Gaspar A.M., Day R., Chretien M.;
"The cDNA sequence of the human pro-hormone and pro-protein convertase
PC1.";
DNA Cell Biol. 11:283-289(1992).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLN-80 AND GLU-665.
PubMed=8666140; DOI=10.2337/diab.45.7.897;
Ohagi S., Sakaguchi H., Sanke T., Tatsuta H., Hanabusa T., Nanjo K.;
"Human prohormone convertase 3 gene: exon-intron organization and
molecular scanning for mutations in Japanese subjects with NIDDM.";
Diabetes 45:897-901(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Trachea;
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=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-60.
PubMed=7797529; DOI=10.1074/jbc.270.25.15391;
Jansen E.;
"Neuroendocrine-specific expression of the human prohormone convertase
1 gene. Hormonal regulation of transcription through distinct cAMP
response elements.";
J. Biol. Chem. 270:15391-15397(1995).
[7]
GLYCOSYLATION AT THR-632, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=23234360; DOI=10.1021/pr300963h;
Halim A., Ruetschi U., Larson G., Nilsson J.;
"LC-MS/MS characterization of O-glycosylation sites and glycan
structures of human cerebrospinal fluid glycoproteins.";
J. Proteome Res. 12:573-584(2013).
[8]
VARIANT PC1 DEFICIENCY ARG-483.
PubMed=9207799; DOI=10.1038/ng0797-303;
Jackson R.S., Creemers J.W., Ohagi S., Raffin-Sanson M.-L.,
Sanders L., Montague C.T., Hutton J.C., O'Rahilly S.;
"Obesity and impaired prohormone processing associated with mutations
in the human prohormone convertase 1 gene.";
Nat. Genet. 16:303-306(1997).
[9]
VARIANTS ASP-221; GLU-665 AND THR-690.
PubMed=10391209; DOI=10.1038/10290;
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
"Characterization of single-nucleotide polymorphisms in coding regions
of human genes.";
Nat. Genet. 22:231-238(1999).
[10]
ERRATUM.
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
Nat. Genet. 23:373-373(1999).
[11]
VARIANT PC1 DEFICIENCY ALA-213 DEL.
PubMed=14617756; DOI=10.1172/JCI200318784;
Jackson R.S., Creemers J.W., Farooqi I.S., Raffin-Sanson M.-L.,
Varro A., Dockray G.J., Holst J.J., Brubaker P.L., Corvol P.,
Polonsky K.S., Ostrega D., Becker K.L., Bertagna X., Hutton J.C.,
White A., Dattani M.T., Hussain K., Middleton S.J., Nicole T.M.,
Milla P.J., Lindley K.J., O'Rahilly S.;
"Small-intestinal dysfunction accompanies the complex endocrinopathy
of human proprotein convertase 1 deficiency.";
J. Clin. Invest. 112:1550-1560(2003).
[12]
VARIANT PC1 DEFICIENCY LEU-307, CHARACTERIZATION OF VARIANT PC1
DEFICIENCY LEU-307, AND VARIANTS GLU-665 AND THR-690.
PubMed=17595246; DOI=10.1210/jc.2007-0687;
Farooqi I.S., Volders K., Stanhope R., Heuschkel R., White A.,
Lank E., Keogh J., O'Rahilly S., Creemers J.W.M.;
"Hyperphagia and early-onset obesity due to a novel homozygous
missense mutation in prohormone convertase 1/3.";
J. Clin. Endocrinol. Metab. 92:3369-3373(2007).
[13]
VARIANT ASP-221, CHARACTERIZATION OF VARIANT ASP-221, AND
POLYMORPHISM.
PubMed=18604207; DOI=10.1038/ng.177;
Benzinou M., Creemers J.W.M., Choquet H., Lobbens S., Dina C.,
Durand E., Guerardel A., Boutin P., Jouret B., Heude B., Balkau B.,
Tichet J., Marre M., Potoczna N., Horber F., Le Stunff C.,
Czernichow S., Sandbaek A., Lauritzen T., Borch-Johnsen K.,
Andersen G., Kiess W., Koerner A., Kovacs P., Jacobson P.,
Carlsson L.M.S., Walley A.J., Joergensen T., Hansen T., Pedersen O.,
Meyre D., Froguel P.;
"Common nonsynonymous variants in PCSK1 confer risk of obesity.";
Nat. Genet. 40:943-945(2008).
-!- FUNCTION: Involved in the processing of hormone and other protein
precursors at sites comprised of pairs of basic amino acid
residues. Substrates include POMC, renin, enkephalin, dynorphin,
somatostatin, insulin and AGRP. {ECO:0000250|UniProtKB:P63239}.
-!- CATALYTIC ACTIVITY: Release of protein hormones, neuropeptides and
renin from their precursors, generally by hydrolysis of -Lys-
Arg-|- bonds.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle.
Note=Localized in the secretion granules.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P29120-1; Sequence=Displayed;
Name=2;
IsoId=P29120-2; Sequence=VSP_046100;
Note=No experimental confirmation available.;
-!- PTM: O-glycosylated. {ECO:0000269|PubMed:23234360}.
-!- POLYMORPHISM: Genetic variations in PCSK1 define the body mass
index quantitative trait locus 12 (BMIQ12) [MIM:612362]. Variance
in body mass index is a susceptibility factor for obesity.
{ECO:0000269|PubMed:18604207}.
-!- DISEASE: Proprotein convertase 1 deficiency (PC1 deficiency)
[MIM:600955]: Characterized by obesity, hypogonadism,
hypoadrenalism, reactive hypoglycemia as well as marked small-
intestinal absorptive dysfunction It is due to impaired processing
of prohormones. {ECO:0000269|PubMed:14617756,
ECO:0000269|PubMed:17595246, ECO:0000269|PubMed:9207799}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
{ECO:0000305}.
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EMBL; X64810; CAA46031.1; -; mRNA.
EMBL; M90753; AAA59918.1; -; mRNA.
EMBL; D73407; BAA11133.1; -; Genomic_DNA.
EMBL; AK303888; BAH14073.1; -; mRNA.
EMBL; AC008951; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC108107; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; U24128; AAA73788.1; -; Genomic_DNA.
CCDS; CCDS4081.1; -. [P29120-1]
CCDS; CCDS54881.1; -. [P29120-2]
PIR; S21106; KXHUC1.
RefSeq; NP_000430.3; NM_000439.4. [P29120-1]
RefSeq; NP_001171346.1; NM_001177875.1. [P29120-2]
UniGene; Hs.78977; -.
ProteinModelPortal; P29120; -.
SMR; P29120; -.
BioGrid; 111151; 7.
IntAct; P29120; 1.
MINT; MINT-6630348; -.
STRING; 9606.ENSP00000308024; -.
BindingDB; P29120; -.
ChEMBL; CHEMBL3182; -.
DrugBank; DB00030; Insulin Human.
DrugBank; DB00071; Insulin Pork.
GuidetoPHARMACOLOGY; 2382; -.
MEROPS; S08.072; -.
iPTMnet; P29120; -.
PhosphoSitePlus; P29120; -.
UniCarbKB; P29120; -.
BioMuta; PCSK1; -.
DMDM; 116242674; -.
EPD; P29120; -.
PaxDb; P29120; -.
PeptideAtlas; P29120; -.
PRIDE; P29120; -.
Ensembl; ENST00000311106; ENSP00000308024; ENSG00000175426. [P29120-1]
Ensembl; ENST00000508626; ENSP00000421600; ENSG00000175426. [P29120-2]
GeneID; 5122; -.
KEGG; hsa:5122; -.
UCSC; uc003kls.3; human. [P29120-1]
CTD; 5122; -.
DisGeNET; 5122; -.
EuPathDB; HostDB:ENSG00000175426.10; -.
GeneCards; PCSK1; -.
HGNC; HGNC:8743; PCSK1.
HPA; HPA048564; -.
MalaCards; PCSK1; -.
MIM; 162150; gene.
MIM; 600955; phenotype.
MIM; 612362; phenotype.
neXtProt; NX_P29120; -.
OpenTargets; ENSG00000175426; -.
Orphanet; 71528; Obesity due to prohormone convertase I deficiency.
PharmGKB; PA33089; -.
eggNOG; KOG3525; Eukaryota.
eggNOG; COG1404; LUCA.
eggNOG; COG4935; LUCA.
GeneTree; ENSGT00750000117358; -.
HOGENOM; HOG000192536; -.
HOVERGEN; HBG008705; -.
InParanoid; P29120; -.
KO; K01359; -.
OMA; FEPRALK; -.
OrthoDB; EOG091G05HI; -.
PhylomeDB; P29120; -.
TreeFam; TF314277; -.
Reactome; R-HSA-209952; Peptide hormone biosynthesis.
Reactome; R-HSA-264876; Insulin processing.
Reactome; R-HSA-381771; Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
Reactome; R-HSA-400511; Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP).
Reactome; R-HSA-422085; Synthesis, secretion, and deacylation of Ghrelin.
SignaLink; P29120; -.
ChiTaRS; PCSK1; human.
GeneWiki; Proprotein_convertase_1; -.
GenomeRNAi; 5122; -.
PMAP-CutDB; P29120; -.
PRO; PR:P29120; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000175426; -.
CleanEx; HS_PCSK1; -.
ExpressionAtlas; P29120; baseline and differential.
Genevisible; P29120; HS.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
GO; GO:0004252; F:serine-type endopeptidase activity; ISS:BHF-UCL.
GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
GO; GO:0008152; P:metabolic process; TAS:ProtInc.
GO; GO:0043043; P:peptide biosynthetic process; ISS:BHF-UCL.
GO; GO:0016486; P:peptide hormone processing; TAS:Reactome.
GO; GO:0006508; P:proteolysis; TAS:ProtInc.
CDD; cd04059; Peptidases_S8_Protein_converta; 1.
Gene3D; 2.60.120.260; -; 1.
Gene3D; 3.40.50.200; -; 1.
InterPro; IPR008979; Galactose-bd-like.
InterPro; IPR034182; Kexin/furin.
InterPro; IPR009020; Peptidase/Inhibitor_I9.
InterPro; IPR000209; Peptidase_S8/S53_dom.
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; IPR022005; Proho_convert.
InterPro; IPR002884; PrprotnconvertsP.
InterPro; IPR032815; S8_pro-domain.
Pfam; PF01483; P_proprotein; 1.
Pfam; PF00082; Peptidase_S8; 1.
Pfam; PF12177; Proho_convert; 1.
Pfam; PF16470; S8_pro-domain; 1.
PRINTS; PR00723; SUBTILISIN.
SUPFAM; SSF49785; SSF49785; 1.
SUPFAM; SSF52743; SSF52743; 1.
SUPFAM; SSF54897; SSF54897; 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;
Alternative splicing; Calcium; Cleavage on pair of basic residues;
Complete proteome; Cytoplasmic vesicle; Disease mutation;
Disulfide bond; Glycoprotein; Hydrolase; Obesity; Polymorphism;
Protease; Reference proteome; Serine protease; Signal; Zymogen.
SIGNAL 1 27 {ECO:0000255}.
PROPEP 28 110 {ECO:0000255}.
/FTId=PRO_0000027057.
CHAIN 111 753 Neuroendocrine convertase 1.
/FTId=PRO_0000027058.
DOMAIN 162 451 Peptidase S8.
DOMAIN 460 597 P/Homo B. {ECO:0000255|PROSITE-
ProRule:PRU01173}.
ACT_SITE 167 167 Charge relay system. {ECO:0000250}.
ACT_SITE 208 208 Charge relay system. {ECO:0000250}.
ACT_SITE 382 382 Charge relay system. {ECO:0000250}.
CARBOHYD 173 173 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 401 401 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 632 632 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:23234360}.
DISULFID 225 374 {ECO:0000250}.
DISULFID 317 347 {ECO:0000250}.
DISULFID 467 494 {ECO:0000250}.
VAR_SEQ 1 59 MERRAWSLQCTAFVLFCAWCALNSAKAKRQFVNEWAAEIPG
GPEAASAIAEELGYDLLG -> MGKGSISFLFFS (in
isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046100.
VARIANT 80 80 R -> Q (in dbSNP:rs1799904).
{ECO:0000269|PubMed:8666140}.
/FTId=VAR_013906.
VARIANT 213 213 Missing (in PC1 deficiency).
{ECO:0000269|PubMed:14617756}.
/FTId=VAR_022777.
VARIANT 221 221 N -> D (associated with susceptibility to
obesity; induces a 10.4% reduction of
activity (P = 0.03) when compared to the
wild-type enzyme; dbSNP:rs6232).
{ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:18604207}.
/FTId=VAR_013907.
VARIANT 307 307 S -> L (in PC1 deficiency; in vitro the
mutation markedly impairs the catalytic
activity of the enzyme; however
intracellular trafficking of this mutant
enzyme appears normal; retains some
autocatalytic activity even though it is
completely inactive on other substrates;
dbSNP:rs137852824).
{ECO:0000269|PubMed:17595246}.
/FTId=VAR_055002.
VARIANT 483 483 G -> R (in PC1 deficiency; prevents
processing of pro-PCSK1 and leads to its
retention in the endoplasmic reticulum;
dbSNP:rs137852821).
{ECO:0000269|PubMed:9207799}.
/FTId=VAR_022778.
VARIANT 665 665 Q -> E (in dbSNP:rs6234).
{ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:17595246,
ECO:0000269|PubMed:8666140}.
/FTId=VAR_013908.
VARIANT 690 690 S -> T (in dbSNP:rs6235).
{ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:17595246}.
/FTId=VAR_013909.
CONFLICT 357 357 S -> G (in Ref. 1; CAA46031).
{ECO:0000305}.
CONFLICT 370 371 LH -> VD (in Ref. 3; BAA11133).
{ECO:0000305}.
CONFLICT 617 617 R -> G (in Ref. 4; BAH14073).
{ECO:0000305}.
SEQUENCE 753 AA; 84152 MW; D3CBD1B92093A208 CRC64;
MERRAWSLQC TAFVLFCAWC ALNSAKAKRQ FVNEWAAEIP GGPEAASAIA EELGYDLLGQ
IGSLENHYLF KHKNHPRRSR RSAFHITKRL SDDDRVIWAE QQYEKERSKR SALRDSALNL
FNDPMWNQQW YLQDTRMTAA LPKLDLHVIP VWQKGITGKG VVITVLDDGL EWNHTDIYAN
YDPEASYDFN DNDHDPFPRY DPTNENKHGT RCAGEIAMQA NNHKCGVGVA YNSKVGGIRM
LDGIVTDAIE ASSIGFNPGH VDIYSASWGP NDDGKTVEGP GRLAQKAFEY GVKQGRQGKG
SIFVWASGNG GRQGDNCDCD GYTDSIYTIS ISSASQQGLS PWYAEKCSST LATSYSSGDY
TDQRITSADL HNDCTETHTG TSASAPLAAG IFALALEANP NLTWRDMQHL VVWTSEYDPL
ANNPGWKKNG AGLMVNSRFG FGLLNAKALV DLADPRTWRS VPEKKECVVK DNDFEPRALK
ANGEVIIEIP TRACEGQENA IKSLEHVQFE ATIEYSRRGD LHVTLTSAAG TSTVLLAERE
RDTSPNGFKN WDFMSVHTWG ENPIGTWTLR ITDMSGRIQN EGRIVNWKLI LHGTSSQPEH
MKQPRVYTSY NTVQNDRRGV EKMVDPGEEQ PTQENPKENT LVSKSPSSSS VGGRRDELEE
GAPSQAMLRL LQSAFSKNSP PKQSPKKSPS AKLNIPYENF YEALEKLNKP SQLKDSEDSL
YNDYVDVFYN TKPYKHRDDR LLQALVDILN EEN


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EIAAB26836 KEX2-like endoprotease 2,NEC 2,Nec2,Nec-2,Neuroendocrine convertase 2,PC2,Pcsk2,Prohormone convertase 2,Proprotein convertase 2,Rat,Rattus norvegicus,Rpc2
EIAAB26837 Homo sapiens,Human,KEX2-like endoprotease 2,NEC 2,NEC2,Neuroendocrine convertase 2,PC2,PCSK2,Prohormone convertase 2,Proprotein convertase 2
EIAAB30201 KEX2-like endoprotease 3,Mouse,Mus musculus,NEC 3,Nec3,Nec-3,Neuroendocrine convertase 3,Pcsk4,Prohormone convertase 3,Proprotein convertase subtilisin_kexin type 4
EIAAB30202 KEX2-like endoprotease 3,NEC 3,Nec3,Nec-3,Neuroendocrine convertase 3,PC4,Pcsk4,Prohormone convertase 3,Proprotein convertase subtilisin_kexin type 4,Rat,Rattus norvegicus
EIAAB26834 Att-1,Furin homolog,Mouse,Mus musculus,NEC 1,Nec1,Nec-1,Neuroendocrine convertase 1,PC1,PC3,Pcsk1,Prohormone convertase 1,Propeptide-processing protease,Proprotein convertase 1
EIAAB30209 Mouse,Mus musculus,PC7,Pc7,Pcsk7,Prohormone convertase 7,Proprotein convertase 7,Proprotein convertase subtilisin_kexin type 7,SPC7,Subtilisin_kexin-like protease PC7,Subtilisin-like proprotein conver
EIAAB30211 PC7,Pc7,Pcsk7,Prohormone convertase 7,Proprotein convertase 7,Proprotein convertase subtilisin_kexin type 7,Rat,Rattus norvegicus,rPC7,Subtilisin_kexin-like protease PC7
EIAAB30205 Mouse,Mus musculus,PC5,PC6,Pcsk5,Proprotein convertase 5,Proprotein convertase 6,Proprotein convertase subtilisin_kexin type 5,SPC6,Subtilisin_kexin-like protease PC5,Subtilisin-like proprotein conver
EIAAB30204 Homo sapiens,hPC6,Human,PC5,PC5,PC6,PC6,PCSK5,Proprotein convertase 5,Proprotein convertase 6,Proprotein convertase subtilisin_kexin type 5,Subtilisin_kexin-like protease PC5
EIAAB30206 PC5,PC6,Pcsk5,Proprotein convertase 5,Proprotein convertase 6,Proprotein convertase subtilisin_kexin type 5,Rat,Rattus norvegicus,rPC5,Subtilisin_kexin-like protease PC5
EIAAB30213 Mouse,Mus musculus,Narc1,NARC-1,Neural apoptosis-regulated convertase 1,PC9,Pcsk9,Proprotein convertase 9,Proprotein convertase subtilisin_kexin type 9,Subtilisin_kexin-like protease PC9
EIAAB30212 Narc1,NARC-1,Neural apoptosis-regulated convertase 1,PC9,Pcsk9,Proprotein convertase 9,Proprotein convertase subtilisin_kexin type 9,Rat,Rattus norvegicus,Subtilisin_kexin-like protease PC9
EIAAB30214 Homo sapiens,Human,NARC1,NARC-1,Neural apoptosis-regulated convertase 1,PC9,PCSK9,Proprotein convertase 9,Proprotein convertase subtilisin_kexin type 9,PSEC0052,Subtilisin_kexin-like protease PC9
EIAAB30203 Homo sapiens,Human,PC4,PC4,PCSK4,Proprotein convertase 4,Proprotein convertase subtilisin_kexin type 4,UNQ2757_PRO6496
18-272-195521 NEC2 - Rabbit polyclonal to NEC2; EC 3.4.21.94; NEC 2; PC2; Prohormone convertase 2; Proprotein convertase 2; KEX2-like endoprotease 2 Polyclonal 0.05 ml
EIAAB30199 Homo sapiens,Human,PCSK1N,Proprotein convertase 1 inhibitor,Proprotein convertase subtilisin_kexin type 1 inhibitor,ProSAAS,pro-SAAS
EIAAB30200 Pcsk1n,Proprotein convertase 1 inhibitor,Proprotein convertase subtilisin_kexin type 1 inhibitor,ProSAAS,pro-SAAS,Rat,Rattus norvegicus
EIAAB30198 IA-4,Mouse,Mus musculus,Pcsk1n,Proprotein convertase 1 inhibitor,Proprotein convertase subtilisin_kexin type 1 inhibitor,ProSAAS,pro-SAAS


 

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