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Neuroendocrine convertase 2 (NEC 2) (EC 3.4.21.94) (Egg-laying defective protein 3) (Kex2-like prohormone convertase 2) (CELPC2) (Prohormone convertase 2) (PC2) (Proprotein convertase 2)

 NEC2_CAEEL              Reviewed;         652 AA.
G5ECN9; E9P883; Q18772;
15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
14-DEC-2011, sequence version 1.
27-SEP-2017, entry version 61.
RecName: Full=Neuroendocrine convertase 2 {ECO:0000250|UniProtKB:P16519};
Short=NEC 2 {ECO:0000250|UniProtKB:P16519};
EC=3.4.21.94 {ECO:0000305|PubMed:12657671, ECO:0000305|PubMed:15180830, ECO:0000305|PubMed:16945111, ECO:0000305|PubMed:23665919, ECO:0000305|PubMed:24671950};
AltName: Full=Egg-laying defective protein 3 {ECO:0000303|PubMed:11813735};
AltName: Full=Kex2-like prohormone convertase 2 {ECO:0000303|PubMed:7954663};
Short=CELPC2 {ECO:0000303|PubMed:7954663};
AltName: Full=Prohormone convertase 2 {ECO:0000250|UniProtKB:P16519};
Short=PC2 {ECO:0000303|PubMed:11717360};
AltName: Full=Proprotein convertase 2 {ECO:0000303|PubMed:11717360};
Flags: Precursor;
Name=egl-3 {ECO:0000312|WormBase:C51E3.7a};
Synonyms=kpc-2 {ECO:0000312|WormBase:C51E3.7a};
ORFNames=C51E3.7 {ECO:0000312|WormBase:C51E3.7a};
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239 {ECO:0000312|EMBL:AAA56868.1};
[1] {ECO:0000312|EMBL:AAA56868.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND TISSUE SPECIFICITY.
STRAIN=BA713 {ECO:0000312|EMBL:AAA56868.1};
PubMed=7954663; DOI=10.1007/BF02088586;
Gomez-Saladin E., Wilson D.L., Dickerson I.M.;
"Isolation and in situ localization of a cDNA encoding a Kex2-like
prohormone convertase in the nematode Caenorhabditis elegans.";
Cell. Mol. Neurobiol. 14:9-25(1994).
[2] {ECO:0000312|Proteomes:UP000001940}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[3] {ECO:0000305}
FUNCTION, AND MUTAGENESIS OF GLU-117; GLY-176; CYS-496 AND GLY-594.
PubMed=11813735;
Trent C., Tsuing N., Horvitz H.R.;
"Egg-laying defective mutants of the nematode Caenorhabditis
elegans.";
Genetics 104:619-647(1983).
[4] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
GLY-594 AND GLY-621.
PubMed=11717360;
Kass J., Jacob T.C., Kim P., Kaplan J.M.;
"The EGL-3 proprotein convertase regulates mechanosensory responses of
Caenorhabditis elegans.";
J. Neurosci. 21:9265-9272(2001).
[5] {ECO:0000305}
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND MUTAGENESIS OF GLY-621.
PubMed=12657671;
Jacob T.C., Kaplan J.M.;
"The EGL-21 carboxypeptidase E facilitates acetylcholine release at
Caenorhabditis elegans neuromuscular junctions.";
J. Neurosci. 23:2122-2130(2003).
[6] {ECO:0000305}
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=15180830; DOI=10.1111/j.1600-0854.2004.00195.x;
Zahn T.R., Angleson J.K., MacMorris M.A., Domke E., Hutton J.F.,
Schwartz C., Hutton J.C.;
"Dense core vesicle dynamics in Caenorhabditis elegans neurons and the
role of kinesin UNC-104.";
Traffic 5:544-559(2004).
[7] {ECO:0000305}
FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLU-117; GLY-176 AND
GLY-594.
PubMed=16945111; DOI=10.1111/j.1471-4159.2006.04014.x;
Husson S.J., Clynen E., Baggerman G., Janssen T., Schoofs L.;
"Defective processing of neuropeptide precursors in Caenorhabditis
elegans lacking proprotein convertase 2 (KPC-2/EGL-3): mutant analysis
by mass spectrometry.";
J. Neurochem. 98:1999-2012(2006).
[8] {ECO:0000305}
FUNCTION.
PubMed=17564681; DOI=10.1111/j.1471-4159.2007.04474.x;
Husson S.J., Janssen T., Baggerman G., Bogert B., Kahn-Kirby A.H.,
Ashrafi K., Schoofs L.;
"Impaired processing of FLP and NLP peptides in carboxypeptidase E
(EGL-21)-deficient Caenorhabditis elegans as analyzed by mass
spectrometry.";
J. Neurochem. 102:246-260(2007).
[9] {ECO:0000305}
FUNCTION.
PubMed=17611271; DOI=10.1523/JNEUROSCI.1405-07.2007;
Liu T., Kim K., Li C., Barr M.M.;
"FMRFamide-like neuropeptides and mechanosensory touch receptor
neurons regulate male sexual turning behavior in Caenorhabditis
elegans.";
J. Neurosci. 27:7174-7182(2007).
[10] {ECO:0000305}
FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH FSN-1, UBIQUITINATION,
AND REGION.
PubMed=23665919; DOI=10.1038/emboj.2013.91;
Hung W.L., Hwang C., Gao S., Liao E.H., Chitturi J., Wang Y., Li H.,
Stigloher C., Bessereau J.L., Zhen M.;
"Attenuation of insulin signalling contributes to FSN-1-mediated
regulation of synapse development.";
EMBO J. 32:1745-1760(2013).
[11] {ECO:0000305}
FUNCTION, AND MUTAGENESIS OF CYS-496.
PubMed=23658528; DOI=10.1371/journal.pgen.1003472;
Stawicki T.M., Takayanagi-Kiya S., Zhou K., Jin Y.;
"Neuropeptides function in a homeostatic manner to modulate
excitation-inhibition imbalance in C. elegans.";
PLoS Genet. 9:E1003472-E1003472(2013).
[12] {ECO:0000305}
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=24671950; DOI=10.1242/dev.103846;
Hung W.L., Wang Y., Chitturi J., Zhen M.;
"A Caenorhabditis elegans developmental decision requires insulin
signaling-mediated neuron-intestine communication.";
Development 141:1767-1779(2014).
-!- FUNCTION: Serine endoprotease which cleaves preproteins at paired
basic amino acids (PubMed:12657671, PubMed:15180830,
PubMed:16945111, PubMed:23665919, PubMed:24671950). Processes
FMRFamide-like (flp) and neuropeptide-like protein (nlp)
neuropeptides (PubMed:12657671, PubMed:16945111). Probably by
processing flp-1 and flp-18, modulates the neuronal excitation-
inhibition balance and thus the level of activity of the locomotor
circuit (PubMed:23658528). Regulates sensitivity to mechanosensory
stimuli (PubMed:11717360). By processing neuropeptides, modulates
basal acetylcholine release at the ventral cord neuromuscular
junctions (PubMed:12657671). Probably by processing flp
neuropeptides, regulates the turning step of male mating behavior
(PubMed:17611271). Cleaves pro-insulin-like proteins ins-3, ins-4
and ins-6 into their mature active forms (PubMed:23665919,
PubMed:24671950). Together with convertase kpc-1, cleaves pro-
insulin-like protein ins-18 (PubMed:24671950). By controlling ins-
4 and ins-6 processing and thus the activation of the daf-2/InsR
pathway, negatively modulates synapse development and synaptic
transmission at neuromuscular junctions (PubMed:23665919).
Similarly, by controlling ins-4 and ins-6 processing, negatively
regulates dauer formation under optimal environmental conditions
(PubMed:24671950). Under adverse environmental conditions, may
promote dauer formation by processing ins-18, a daf-2/InsR
antagonist (PubMed:24671950). May cleave dense-core vesicle
membrane protein ida-1 (PubMed:15180830). Involved in egg-laying,
fat storage and locomotion (PubMed:11813735, PubMed:11717360,
PubMed:17564681). {ECO:0000269|PubMed:11717360,
ECO:0000269|PubMed:11813735, ECO:0000269|PubMed:12657671,
ECO:0000269|PubMed:15180830, ECO:0000269|PubMed:16945111,
ECO:0000269|PubMed:17564681, ECO:0000269|PubMed:17611271,
ECO:0000269|PubMed:23658528, ECO:0000269|PubMed:23665919,
ECO:0000269|PubMed:24671950}.
-!- CATALYTIC ACTIVITY: Release of protein hormones and neuropeptides
from their precursors, generally by hydrolysis of -Lys-
Arg-|- bonds. {ECO:0000303|PubMed:12657671,
ECO:0000305|PubMed:15180830, ECO:0000305|PubMed:16945111,
ECO:0000305|PubMed:23665919, ECO:0000305|PubMed:24671950}.
-!- SUBUNIT: Interacts (via C-terminus) with F-box protein fsn-1 (via
SPRY domain); the interaction results in egl-3 proteasomal
degradation. {ECO:0000269|PubMed:23665919}.
-!- SUBCELLULAR LOCATION: Cell projection, axon
{ECO:0000269|PubMed:11717360, ECO:0000269|PubMed:12657671}.
Cytoplasmic vesicle, secretory vesicle lumen
{ECO:0000303|PubMed:11717360}. Secreted
{ECO:0000303|PubMed:24671950}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=a {ECO:0000312|WormBase:C51E3.7a};
IsoId=G5ECN9-1; Sequence=Displayed;
Name=b {ECO:0000312|WormBase:C51E3.7b};
IsoId=G5ECN9-2; Sequence=VSP_058830;
Note=No experimental confirmation available. {ECO:0000305};
Name=c {ECO:0000312|WormBase:C51E3.7c};
IsoId=G5ECN9-3; Sequence=VSP_058829;
Note=No experimental confirmation available. {ECO:0000305};
-!- TISSUE SPECIFICITY: Expressed in head and tail ganglia
(PubMed:7954663, PubMed:11717360, PubMed:12657671,
PubMed:24671950). Expressed in neurons including mechanosensory
and motor neurons, and interneurons (at protein level)
(PubMed:11717360, PubMed:12657671). Expressed in the nerve ring,
ventral nerve cord and intestine (PubMed:24671950).
{ECO:0000269|PubMed:11717360, ECO:0000269|PubMed:12657671,
ECO:0000269|PubMed:24671950, ECO:0000269|PubMed:7954663}.
-!- PTM: Ubiquitinated. {ECO:0000269|PubMed:23665919}.
-!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
{ECO:0000305}.
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EMBL; U04995; AAA56868.1; -; mRNA.
EMBL; BX284605; CAB01635.1; -; Genomic_DNA.
EMBL; BX284605; CAB01642.1; -; Genomic_DNA.
EMBL; BX284605; CBZ01786.1; -; Genomic_DNA.
PIR; C89181; C89181.
PIR; T20131; T20131.
RefSeq; NP_001023732.1; NM_001028561.3. [G5ECN9-1]
RefSeq; NP_001256192.1; NM_001269263.1. [G5ECN9-3]
RefSeq; NP_505614.3; NM_073213.6. [G5ECN9-2]
UniGene; Cel.18027; -.
ProteinModelPortal; G5ECN9; -.
SMR; G5ECN9; -.
STRING; 6239.C51E3.7a; -.
MEROPS; S08.109; -.
EPD; G5ECN9; -.
PaxDb; G5ECN9; -.
PeptideAtlas; G5ECN9; -.
EnsemblMetazoa; C51E3.7a; C51E3.7a; WBGene00001172. [G5ECN9-1]
EnsemblMetazoa; C51E3.7b; C51E3.7b; WBGene00001172. [G5ECN9-2]
EnsemblMetazoa; C51E3.7c.1; C51E3.7c.1; WBGene00001172. [G5ECN9-3]
EnsemblMetazoa; C51E3.7c.2; C51E3.7c.2; WBGene00001172. [G5ECN9-3]
GeneID; 179412; -.
KEGG; cel:CELE_C51E3.7; -.
CTD; 179412; -.
WormBase; C51E3.7a; CE08940; WBGene00001172; egl-3.
WormBase; C51E3.7b; CE08941; WBGene00001172; egl-3.
WormBase; C51E3.7c; CE45708; WBGene00001172; egl-3.
eggNOG; KOG3525; Eukaryota.
eggNOG; KOG3526; Eukaryota.
eggNOG; COG1404; LUCA.
eggNOG; COG4935; LUCA.
GeneTree; ENSGT00750000117358; -.
HOGENOM; HOG000192536; -.
KO; K01360; -.
OMA; PQRGVLK; -.
OrthoDB; EOG091G05HI; -.
SignaLink; Q18772; -.
PRO; PR:G5ECN9; -.
Proteomes; UP000001940; Chromosome V.
Bgee; WBGene00001172; -.
ExpressionAtlas; G5ECN9; baseline and differential.
GO; GO:0030424; C:axon; IDA:WormBase.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0098770; F:FBXO family protein binding; IPI:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; IMP:UniProtKB.
GO; GO:0090474; P:arg-arg specific dibasic protein processing; IMP:UniProtKB.
GO; GO:0008340; P:determination of adult lifespan; IGI:UniProtKB.
GO; GO:0090472; P:dibasic protein processing; IMP:UniProtKB.
GO; GO:0030070; P:insulin processing; IMP:UniProtKB.
GO; GO:0030536; P:larval feeding behavior; IMP:UniProtKB.
GO; GO:1905910; P:negative regulation of dauer entry; IGI:UniProtKB.
GO; GO:1904810; P:negative regulation of dense core granule transport; IMP:UniProtKB.
GO; GO:0061096; P:negative regulation of turning behavior involved in mating; IMP:WormBase.
GO; GO:0007274; P:neuromuscular synaptic transmission; IGI:UniProtKB.
GO; GO:0061837; P:neuropeptide processing; IMP:UniProtKB.
GO; GO:0014057; P:positive regulation of acetylcholine secretion, neurotransmission; IMP:UniProtKB.
GO; GO:1905852; P:positive regulation of backward locomotion; IGI:UniProtKB.
GO; GO:0060456; P:positive regulation of digestive system process; IMP:UniProtKB.
GO; GO:1905850; P:positive regulation of forward locomotion; IMP:UniProtKB.
GO; GO:1905954; P:positive regulation of lipid localization; IMP:UniProtKB.
GO; GO:0090326; P:positive regulation of locomotion involved in locomotory behavior; IMP:UniProtKB.
GO; GO:1901046; P:positive regulation of oviposition; IMP:UniProtKB.
GO; GO:0045887; P:positive regulation of synaptic growth at neuromuscular junction; IGI:UniProtKB.
GO; GO:0043058; P:regulation of backward locomotion; IGI:UniProtKB.
GO; GO:1903998; P:regulation of eating behavior; IMP:UniProtKB.
GO; GO:0090325; P:regulation of locomotion involved in locomotory behavior; IMP:WormBase.
GO; GO:0006937; P:regulation of muscle contraction; IMP:UniProtKB.
GO; GO:1900073; P:regulation of neuromuscular synaptic transmission; IGI:UniProtKB.
GO; GO:0008582; P:regulation of synaptic growth at neuromuscular junction; IGI:UniProtKB.
GO; GO:0009612; P:response to mechanical stimulus; IMP:UniProtKB.
GO; GO:1904014; P:response to serotonin; IMP:UniProtKB.
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; 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.
SUPFAM; SSF49785; SSF49785; 1.
SUPFAM; SSF52743; SSF52743; 1.
SUPFAM; SSF54897; SSF54897; 1.
PROSITE; PS00136; SUBTILASE_ASP; 1.
PROSITE; PS00137; SUBTILASE_HIS; 1.
PROSITE; PS00138; SUBTILASE_SER; 1.
1: Evidence at protein level;
Alternative splicing; Cell projection;
Cleavage on pair of basic residues; Complete proteome;
Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Hydrolase;
Protease; Reference proteome; Secreted; Serine protease; Signal;
Ubl conjugation; Zymogen.
SIGNAL 1 22 {ECO:0000255}.
PROPEP 23 107 {ECO:0000255}.
/FTId=PRO_0000439343.
CHAIN 108 652 Neuroendocrine convertase 2.
{ECO:0000255}.
/FTId=PRO_5008958380.
DOMAIN 165 423 Peptidase S8. {ECO:0000255}.
REGION 501 652 Required for ubiquitination-mediated
degradation.
{ECO:0000269|PubMed:23665919}.
ACT_SITE 174 174 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU10080}.
ACT_SITE 215 215 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU10081}.
ACT_SITE 390 390 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU10082}.
CARBOHYD 167 167 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 290 290 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 451 451 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 542 542 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
DISULFID 232 382 {ECO:0000250|UniProtKB:P23188}.
DISULFID 324 354 {ECO:0000250|UniProtKB:P23188}.
DISULFID 496 522 {ECO:0000250|UniProtKB:P23188}.
VAR_SEQ 1 125 Missing (in isoform c). {ECO:0000305}.
/FTId=VSP_058829.
VAR_SEQ 93 188 Missing (in isoform b). {ECO:0000305}.
/FTId=VSP_058830.
MUTAGEN 117 117 E->Q: In n588; loss of nlp and flp
neuropeptide production. Egg-laying
defects characterized by egg retention
and resistance to serotonin and
imipramine-induced egg-laying. Coiling
behavior. {ECO:0000269|PubMed:11813735,
ECO:0000269|PubMed:16945111}.
MUTAGEN 176 176 G->E: In n729; loss of nlp and flp
neuropeptide production. Egg-laying
defects characterized by egg retention
and resistance to serotonin and
imipramine-induced egg-laying. Coiling
behavior. {ECO:0000269|PubMed:11813735,
ECO:0000269|PubMed:16945111}.
MUTAGEN 496 496 C->Y: In n589; temperature-sensitive
mutant. Egg-laying defects characterized
by egg retention and resistance to
serotonin and imipramine-induced egg-
laying. Coiling behavior. Increases
spontaneous convulsions in an acr-2 n2420
mutant background.
{ECO:0000269|PubMed:11813735,
ECO:0000269|PubMed:23658528}.
MUTAGEN 594 594 G->E: In n150; temperature-sensitive
mutant. Loss of nlp and flp neuropeptide
production. Egg-laying defects
characterized by egg retention and
resistance to serotonin and imipramine-
induced egg-laying. Restores sensitivity
to nose touch in a glr-1 n2461 mutant
background. {ECO:0000269|PubMed:11717360,
ECO:0000269|PubMed:11813735,
ECO:0000269|PubMed:16945111}.
MUTAGEN 621 621 G->R: In nu349; egg-laying defects
characterized by egg retention and
resistance to serotonin and imipramine-
induced egg-laying. Loss of localization
to secretory vesicles in axons. Loss of
FMRFamide-like peptide (FaRP) production
in neurons. Resistance to acetylcholine
esterase inhibitor aldicarb-induced
paralysis. Insensitive to body touch but
not to nose touch. Restores sensitivity
to nose touch, high osmolarity and
volatile repellents in a glr-1 n2461 or
lin-10 n1508 mutant background.
{ECO:0000269|PubMed:11717360,
ECO:0000269|PubMed:12657671}.
SEQUENCE 652 AA; 72046 MW; 39E378E75C081A2B CRC64;
MKNTHVDLIC VFLSIFIGIG EAVDVYTNHF HVHLKEGGGL EDAHRIAKRH GFINRGQVAA
SDNEYHFVQP ALVHARTRRS AGHHAKLHND DEVLHVEQLK GYTRTKRGYR PLEQRLESQF
DFSAVMSPSD PLYGYQWYLK NTGQAGGKAR LDLNVERAWA MGFTGKNITT AIMDDGVDYM
HPDIKNNFNA EASYDFSSND PFPYPRYTDD WFNSHGTRCA GEIVAARDNG VCGVGVAYDG
KVAGIRMLDQ PYMTDLIEAN SMGHEPSKIH IYSASWGPTD DGKTVDGPRN ATMRAIVRGV
NEGRNGLGSI FVWASGDGGE DDDCNCDGYA ASMWTISINS AINNGENAHY DESCSSTLAS
TFSNGGRNPE TGVATTDLYG RCTRSHSGTS AAAPEAAGVF ALALEANPSL TWRDLQHLTV
LTSSRNSLFD GRCRDFPSLG INDNHRDSHG NCSHFEWQMN GVGLEYNHLF GFGVLDAAEM
VMLAMAWKTS PPRYHCTAGL IDTPHEIPAD GNLILEINTD GCAGSQFEVR YLEHVQAVVS
FNSTRRGDTT LYLISPMGTR TMILSRRPKD DDSKDGFTNW PFMTTHTWGE NPTGKWRLVA
RFQGPGAHAG TLKKFELMLH GTREAPYNLI EPIVGQTNKK LDTVQKAHKR SH


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EIAAB26833 Bos taurus,Bovine,NEC 1,Neuroendocrine convertase 1,PC1,PCSK1,Prohormone convertase 1,Proprotein convertase 1
EIAAB26835 Bos taurus,Bovine,NEC 2,Neuroendocrine convertase 2,PC2,PCSK2,Prohormone convertase 2,Proprotein convertase 2
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
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
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
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
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
EIAAB30203 Homo sapiens,Human,PC4,PC4,PCSK4,Proprotein convertase 4,Proprotein convertase subtilisin_kexin type 4,UNQ2757_PRO6496
18-783-76520 RABBIT ANTI HUMAN CARBOXYPEPTIDASE H (MATURE N-TERMINAL) - ENKEPHALIN CONVERTASE; EC 3.4.17.10; CPE; Carboxypeptidase H; CPH; Enkephalin convertase; Prohormone-processing carboxypeptidase Polyclonal 0.1 ml
18-783-76521 RABBIT ANTI HUMAN CARBOXYPEPTIDASE H (C-TERMINAL) - ENKEPHALIN CONVERTASE; EC 3.4.17.10; CPE; Carboxypeptidase H; CPH; Enkephalin convertase; Prohormone-processing carboxypeptidase Polyclonal 0.1 ml
EIAAB30199 Homo sapiens,Human,PCSK1N,Proprotein convertase 1 inhibitor,Proprotein convertase subtilisin_kexin type 1 inhibitor,ProSAAS,pro-SAAS


 

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