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

Neprilysin (EC 3.4.24.11) (Atriopeptidase) (Common acute lymphocytic leukemia antigen) (CALLA) (Enkephalinase) (Neutral endopeptidase 24.11) (NEP) (Neutral endopeptidase) (Skin fibroblast elastase) (SFE) (CD antigen CD10)

 NEP_HUMAN               Reviewed;         750 AA.
P08473; A8K6U6; D3DNJ9; Q3MIX4;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
18-JUL-2018, entry version 215.
RecName: Full=Neprilysin;
EC=3.4.24.11 {ECO:0000269|PubMed:15283675, ECO:0000269|PubMed:27588448, ECO:0000269|PubMed:8168535};
AltName: Full=Atriopeptidase;
AltName: Full=Common acute lymphocytic leukemia antigen;
Short=CALLA;
AltName: Full=Enkephalinase;
AltName: Full=Neutral endopeptidase 24.11;
Short=NEP;
Short=Neutral endopeptidase;
AltName: Full=Skin fibroblast elastase;
Short=SFE;
AltName: CD_antigen=CD10;
Name=MME; Synonyms=EPN;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Kidney;
PubMed=2971756; DOI=10.1084/jem.168.4.1247;
Letarte M., Vera S., Tran R., Addis J.B.L., Onizuka R.J.,
Quackenbush E.J., Jongeneel C.V., McInnes R.R.;
"Common acute lymphocytic leukemia antigen is identical to neutral
endopeptidase.";
J. Exp. Med. 168:1247-1253(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2968607; DOI=10.1073/pnas.85.13.4819;
Shipp M.A., Richardson N.E., Sayre P.H., Brown N.R., Masteller E.L.,
Clayton L.K., Ritz J., Reinherz E.L.;
"Molecular cloning of the common acute lymphoblastic leukemia antigen
(CALLA) identifies a type II integral membrane protein.";
Proc. Natl. Acad. Sci. U.S.A. 85:4819-4823(1988).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2528730; DOI=10.1073/pnas.86.18.7103;
D'Adamio L., Shipp M.A., Masteller E.L., Reinherz E.L.;
"Organization of the gene encoding common acute lymphoblastic leukemia
antigen (neutral endopeptidase 24.11): multiple miniexons and separate
5' untranslated regions.";
Proc. Natl. Acad. Sci. U.S.A. 86:7103-7107(1989).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
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 [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
[6]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 3-750.
TISSUE=Placenta;
PubMed=3162217; DOI=10.1016/0014-5793(88)80828-7;
Malfroy B., Kuang W.-J., Seeburg P.H., Mason A.J., Schofield P.R.;
"Molecular cloning and amino acid sequence of human enkephalinase
(neutral endopeptidase).";
FEBS Lett. 229:206-210(1988).
[9]
FUNCTION.
PubMed=2972276; DOI=10.1042/bj2540531;
Vanneste Y., Michel A., Dimaline R., Najdovski T.,
Deschodt-Lanckman M.;
"Hydrolysis of alpha-human atrial natriuretic peptide in vitro by
human kidney membranes and purified endopeptidase-24.11. Evidence for
a novel cleavage site.";
Biochem. J. 254:531-537(1988).
[10]
FUNCTION IN THE DEGRADATION OF ANF.
PubMed=2531377; DOI=10.1016/0196-9781(89)90131-9;
Yandle T.G., Brennan S.O., Espiner E.A., Nicholls M.G., Richards A.M.;
"Endopeptidase-24.11 in human plasma degrades atrial natriuretic
factor (ANF) to ANF(99-105/106-126).";
Peptides 10:891-894(1989).
[11]
ACTIVE SITE ASP-651, AND CATALYTIC ACTIVITY.
PubMed=8168535; DOI=10.1111/j.1432-1033.1994.tb18760.x;
Le Moual H., Dion N., Roques B.P., Crine P., Boileau G.;
"Asp650 is crucial for catalytic activity of neutral endopeptidase 24-
11.";
Eur. J. Biochem. 221:475-480(1994).
[12]
GLYCOSYLATION AT ASN-145 AND ASN-285.
PubMed=12754519; DOI=10.1038/nbt827;
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
"Identification and quantification of N-linked glycoproteins using
hydrazide chemistry, stable isotope labeling and mass spectrometry.";
Nat. Biotechnol. 21:660-666(2003).
[13]
FUNCTION IN ANGIOTENSIN PEPTIDE METABOLISM, BIOPHYSICOCHEMICAL
PROPERTIES, AND CATALYTIC ACTIVITY.
PubMed=15283675; DOI=10.1042/BJ20040634;
Rice G.I., Thomas D.A., Grant P.J., Turner A.J., Hooper N.M.;
"Evaluation of angiotensin-converting enzyme (ACE), its homologue ACE2
and neprilysin in angiotensin peptide metabolism.";
Biochem. J. 383:45-51(2004).
[14]
FUNCTION, AND INHIBITION BY OPIORPHIN.
PubMed=17101991; DOI=10.1073/pnas.0605865103;
Wisner A., Dufour E., Messaoudi M., Nejdi A., Marcel A.,
Ungeheuer M.-N., Rougeot C.;
"Human opiorphin, a natural antinociceptive modulator of opioid-
dependent pathways.";
Proc. Natl. Acad. Sci. U.S.A. 103:17979-17984(2006).
[15]
IDENTIFICATION AS SKIN FIBROBLAST ELASTASE, AND FUNCTION.
PubMed=20876573; DOI=10.1074/jbc.M110.161547;
Morisaki N., Moriwaki S., Sugiyama-Nakagiri Y., Haketa K., Takema Y.,
Imokawa G.;
"Neprilysin is identical to skin fibroblast elastase: its role in skin
aging and UV responses.";
J. Biol. Chem. 285:39819-39827(2010).
[16]
MYRISTOYLATION AT GLY-2.
PubMed=19756956; DOI=10.1007/s11010-009-0253-8;
Zheng R., Horiguchi A., Iida K., Lee J., Shen R., Goodman O.B. Jr.,
Nanus D.M.;
"Neutral endopeptidase is a myristoylated protein.";
Mol. Cell. Biochem. 335:173-180(2010).
[17]
GLYCOSYLATION AT ASN-628.
PubMed=22766194; DOI=10.1016/j.bbagen.2012.06.017;
Sato B., Katagiri Y.U., Iijima K., Yamada H., Ito S., Kawasaki N.,
Okita H., Fujimoto J., Kiyokawa N.;
"The human CD10 lacking an N-glycan at Asn(628) is deficient in
surface expression and neutral endopeptidase activity.";
Biochim. Biophys. Acta 1820:1715-1723(2012).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 AND SER-6, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[19]
FUNCTION, CATALYTIC ACTIVITY, INVOLVEMENT IN CMT2T, VARIANTS CMT2T
ALA-12; CYS-347; PRO-348 AND ASP-422, AND CHARACTERIZATION OF VARIANTS
CMT2T CYS-347 AND ASP-422.
PubMed=27588448; DOI=10.1016/j.ajhg.2016.07.008;
Auer-Grumbach M., Toegel S., Schabhuettl M., Weinmann D., Chiari C.,
Bennett D.L., Beetz C., Klein D., Andersen P.M., Boehme I.,
Fink-Puches R., Gonzalez M., Harms M.B., Motley W., Reilly M.M.,
Renner W., Rudnik-Schoeneborn S., Schlotter-Weigel B.,
Themistocleous A.C., Weishaupt J.H., Ludolph A.C., Wieland T., Tao F.,
Abreu L., Windhager R., Zitzelsberger M., Strom T.M., Walther T.,
Scherer S.S., Zuechner S., Martini R., Senderek J.;
"Rare variants in MME, encoding metalloprotease neprilysin, are linked
to late-onset autosomal-dominant axonal polyneuropathies.";
Am. J. Hum. Genet. 99:607-623(2016).
[20]
INVOLVEMENT IN CMT2T, VARIANTS CMT2T CYS-411 DEL AND ARG-621, VARIANT
HIS-497, AND CHARACTERIZATION OF VARIANT CMT2T ARG-621.
PubMed=26991897; DOI=10.1002/ana.24612;
Higuchi Y., Hashiguchi A., Yuan J., Yoshimura A., Mitsui J.,
Ishiura H., Tanaka M., Ishihara S., Tanabe H., Nozuma S., Okamoto Y.,
Matsuura E., Ohkubo R., Inamizu S., Shiraishi W., Yamasaki R.,
Ohyagi Y., Kira J., Oya Y., Yabe H., Nishikawa N., Tobisawa S.,
Matsuda N., Masuda M., Kugimoto C., Fukushima K., Yano S.,
Yoshimura J., Doi K., Nakagawa M., Morishita S., Tsuji S.,
Takashima H.;
"Mutations in MME cause an autosomal-recessive Charcot-Marie-Tooth
disease type 2.";
Ann. Neurol. 79:659-672(2016).
[21]
INVOLVEMENT IN SCA43, AND VARIANT SCA43 TYR-143.
PubMed=27583304; DOI=10.1212/NXG.0000000000000094;
Depondt C., Donatello S., Rai M., Wang F.C., Manto M., Simonis N.,
Pandolfo M.;
"MME mutation in dominant spinocerebellar ataxia with neuropathy
(SCA43).";
Neurol. Genet. 2:E94-E94(2016).
[22]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND GLYCOSYLATION AT ASN-145;
ASN-325 AND ASN-628.
PubMed=10669592; DOI=10.1006/jmbi.1999.3492;
Oefner C., D'Arcy A., Hennig M., Winkler F.K., Dale G.E.;
"Structure of human neutral endopeptidase (Neprilysin) complexed with
phosphoramidon.";
J. Mol. Biol. 296:341-349(2000).
[23]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 55-750 IN COMPLEXES WITH
ZINC IONS AND SYNTHETIC INHIBITORS, DISULFIDE BONDS, COFACTOR, AND
GLYCOSYLATION AT ASN-145; ASN-325 AND ASN-628.
PubMed=14747736; DOI=10.1107/S0907444903027410;
Oefner C., Roques B.P., Fournie-Zaluski M.-C., Dale G.E.;
"Structural analysis of neprilysin with various specific and potent
inhibitors.";
Acta Crystallogr. D 60:392-396(2004).
[24]
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 55-750 IN COMPLEX WITH ZINC
IONS AND THE SYNTHETIC INHIBITOR MCB3937, DISULFIDE BONDS, COFACTOR,
AND GLYCOSYLATION AT ASN-145; ASN-325 AND ASN-628.
PubMed=17704566; DOI=10.1107/S0907444907036281;
Oefner C., Pierau S., Schulz H., Dale G.E.;
"Structural studies of a bifunctional inhibitor of neprilysin and DPP-
IV.";
Acta Crystallogr. D 63:975-981(2007).
-!- FUNCTION: Thermolysin-like specificity, but is almost confined on
acting on polypeptides of up to 30 amino acids (PubMed:15283675,
PubMed:8168535). Biologically important in the destruction of
opioid peptides such as Met- and Leu-enkephalins by cleavage of a
Gly-Phe bond (PubMed:17101991). Able to cleave angiotensin-1,
angiotensin-2 and angiotensin 1-9 (PubMed:15283675). Involved in
the degradation of atrial natriuretic factor (ANF)
(PubMed:2531377, PubMed:2972276). Displays UV-inducible elastase
activity toward skin preelastic and elastic fibers
(PubMed:20876573). {ECO:0000269|PubMed:15283675,
ECO:0000269|PubMed:17101991, ECO:0000269|PubMed:20876573,
ECO:0000269|PubMed:2531377, ECO:0000269|PubMed:27588448,
ECO:0000269|PubMed:2972276}.
-!- CATALYTIC ACTIVITY: Preferential cleavage of polypeptides between
hydrophobic residues, particularly with Phe or Tyr at P1'.
{ECO:0000269|PubMed:15283675, ECO:0000269|PubMed:27588448,
ECO:0000269|PubMed:8168535}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:14747736,
ECO:0000269|PubMed:17704566};
Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:14747736,
ECO:0000269|PubMed:17704566};
-!- ENZYME REGULATION: Inhibited in a dose dependent manner by
opiorphin. {ECO:0000269|PubMed:17101991}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=55.1 uM for angiotensin-1 {ECO:0000269|PubMed:15283675};
KM=179 uM for angiotensin-2 {ECO:0000269|PubMed:15283675};
KM=111.4 uM for angiotensin 1-9 {ECO:0000269|PubMed:15283675};
-!- INTERACTION:
P21926:CD9; NbExp=6; IntAct=EBI-353759, EBI-4280101;
P08107:HSPA1B; NbExp=3; IntAct=EBI-353759, EBI-629985;
P04792:HSPB1; NbExp=4; IntAct=EBI-353759, EBI-352682;
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane
protein.
-!- PTM: Myristoylation is a determinant of membrane targeting.
{ECO:0000269|PubMed:19756956}.
-!- PTM: Glycosylation at Asn-628 is necessary both for surface
expression and neutral endopeptidase activity.
{ECO:0000269|PubMed:10669592, ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:14747736, ECO:0000269|PubMed:17704566,
ECO:0000269|PubMed:22766194}.
-!- DISEASE: Charcot-Marie-Tooth disease 2T (CMT2T) [MIM:617017]: An
axonal form of Charcot-Marie-Tooth disease, a disorder of the
peripheral nervous system, characterized by progressive weakness
and atrophy, initially of the peroneal muscles and later of the
distal muscles of the arms. Charcot-Marie-Tooth disease is
classified in two main groups on the basis of electrophysiologic
properties and histopathology: primary peripheral demyelinating
neuropathies (designated CMT1 when they are dominantly inherited)
and primary peripheral axonal neuropathies (CMT2). Neuropathies of
the CMT2 group are characterized by signs of axonal degeneration
in the absence of obvious myelin alterations, normal or slightly
reduced nerve conduction velocities, and progressive distal muscle
weakness and atrophy. {ECO:0000269|PubMed:26991897,
ECO:0000269|PubMed:27588448}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Spinocerebellar ataxia 43 (SCA43) [MIM:617018]: A form of
spinocerebellar ataxia, a clinically and genetically heterogeneous
group of cerebellar disorders. Patients show progressive
incoordination of gait and often poor coordination of hands,
speech and eye movements, due to degeneration of the cerebellum
with variable involvement of the brainstem and spinal cord. SCA43
is a slowly progressive, autosomal dominant form.
{ECO:0000269|PubMed:27583304}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: Important cell surface marker in the diagnostic of
human acute lymphocytic leukemia.
-!- SIMILARITY: Belongs to the peptidase M13 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA30157.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/MMEID41386ch3q25.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; Y00811; CAA68752.1; -; mRNA.
EMBL; J03779; AAA51915.1; -; mRNA.
EMBL; M26628; AAA52294.1; -; Genomic_DNA.
EMBL; M26607; AAA52294.1; JOINED; Genomic_DNA.
EMBL; M26608; AAA52294.1; JOINED; Genomic_DNA.
EMBL; M26609; AAA52294.1; JOINED; Genomic_DNA.
EMBL; M26610; AAA52294.1; JOINED; Genomic_DNA.
EMBL; M26611; AAA52294.1; JOINED; Genomic_DNA.
EMBL; M26612; AAA52294.1; JOINED; Genomic_DNA.
EMBL; M26613; AAA52294.1; JOINED; Genomic_DNA.
EMBL; M26614; AAA52294.1; JOINED; Genomic_DNA.
EMBL; M26615; AAA52294.1; JOINED; Genomic_DNA.
EMBL; M26616; AAA52294.1; JOINED; Genomic_DNA.
EMBL; M26617; AAA52294.1; JOINED; Genomic_DNA.
EMBL; M26618; AAA52294.1; JOINED; Genomic_DNA.
EMBL; M26619; AAA52294.1; JOINED; Genomic_DNA.
EMBL; M26620; AAA52294.1; JOINED; Genomic_DNA.
EMBL; M26621; AAA52294.1; JOINED; Genomic_DNA.
EMBL; M26622; AAA52294.1; JOINED; Genomic_DNA.
EMBL; M26623; AAA52294.1; JOINED; Genomic_DNA.
EMBL; M26624; AAA52294.1; JOINED; Genomic_DNA.
EMBL; M26625; AAA52294.1; JOINED; Genomic_DNA.
EMBL; M26626; AAA52294.1; JOINED; Genomic_DNA.
EMBL; M26627; AAA52294.1; JOINED; Genomic_DNA.
EMBL; AK291761; BAF84450.1; -; mRNA.
EMBL; EU326307; ACA05913.1; -; Genomic_DNA.
EMBL; CH471052; EAW78754.1; -; Genomic_DNA.
EMBL; CH471052; EAW78755.1; -; Genomic_DNA.
EMBL; CH471052; EAW78756.1; -; Genomic_DNA.
EMBL; CH471052; EAW78757.1; -; Genomic_DNA.
EMBL; CH471052; EAW78758.1; -; Genomic_DNA.
EMBL; BC101632; AAI01633.1; -; mRNA.
EMBL; BC101658; AAI01659.1; -; mRNA.
EMBL; X07166; CAA30157.1; ALT_INIT; mRNA.
CCDS; CCDS3172.1; -.
PIR; A41387; HYHUN.
RefSeq; NP_000893.2; NM_000902.3.
RefSeq; NP_009218.2; NM_007287.2.
RefSeq; NP_009219.2; NM_007288.2.
RefSeq; NP_009220.2; NM_007289.2.
RefSeq; XP_006713709.1; XM_006713646.3.
RefSeq; XP_006713710.1; XM_006713647.3.
RefSeq; XP_011511157.1; XM_011512855.2.
RefSeq; XP_011511158.1; XM_011512856.2.
RefSeq; XP_011511159.1; XM_011512857.2.
UniGene; Hs.307734; -.
PDB; 1DL9; Model; -; A=508-750.
PDB; 1DMT; X-ray; 2.10 A; A=55-750.
PDB; 1QVD; Model; -; A=55-750.
PDB; 1R1H; X-ray; 1.95 A; A=55-750.
PDB; 1R1I; X-ray; 2.60 A; A=55-750.
PDB; 1R1J; X-ray; 2.35 A; A=55-750.
PDB; 1Y8J; X-ray; 2.25 A; A=55-750.
PDB; 2QPJ; X-ray; 2.05 A; A=55-750.
PDB; 2YB9; X-ray; 2.40 A; A=55-750.
PDB; 4CTH; X-ray; 2.15 A; A=52-750.
PDB; 5JMY; X-ray; 2.00 A; A/B=53-750.
PDBsum; 1DL9; -.
PDBsum; 1DMT; -.
PDBsum; 1QVD; -.
PDBsum; 1R1H; -.
PDBsum; 1R1I; -.
PDBsum; 1R1J; -.
PDBsum; 1Y8J; -.
PDBsum; 2QPJ; -.
PDBsum; 2YB9; -.
PDBsum; 4CTH; -.
PDBsum; 5JMY; -.
ProteinModelPortal; P08473; -.
SMR; P08473; -.
BioGrid; 110455; 102.
IntAct; P08473; 80.
MINT; P08473; -.
STRING; 9606.ENSP00000353679; -.
BindingDB; P08473; -.
ChEMBL; CHEMBL1944; -.
DrugBank; DB00616; Candoxatril.
DrugBank; DB11623; Candoxatrilat.
DrugBank; DB06655; Liraglutide.
DrugBank; DB02558; N-(3-Phenyl-2-Sulfanylpropanoyl)Phenylalanylalanine.
DrugBank; DB00886; Omapatrilat.
DrugBank; DB02557; Phosphoramidon.
DrugBank; DB09292; Sacubitril.
DrugBank; DB05796; SLV 306.
DrugBank; DB08626; Thiorphan.
GuidetoPHARMACOLOGY; 1611; -.
MEROPS; M13.001; -.
CarbonylDB; P08473; -.
iPTMnet; P08473; -.
PhosphoSitePlus; P08473; -.
BioMuta; MME; -.
DMDM; 128062; -.
EPD; P08473; -.
MaxQB; P08473; -.
PaxDb; P08473; -.
PeptideAtlas; P08473; -.
PRIDE; P08473; -.
ProteomicsDB; 52110; -.
Ensembl; ENST00000360490; ENSP00000353679; ENSG00000196549.
Ensembl; ENST00000460393; ENSP00000418525; ENSG00000196549.
Ensembl; ENST00000462745; ENSP00000419653; ENSG00000196549.
Ensembl; ENST00000492661; ENSP00000420389; ENSG00000196549.
Ensembl; ENST00000493237; ENSP00000417079; ENSG00000196549.
Ensembl; ENST00000615825; ENSP00000478173; ENSG00000196549.
GeneID; 4311; -.
KEGG; hsa:4311; -.
UCSC; uc003fab.2; human.
CTD; 4311; -.
DisGeNET; 4311; -.
EuPathDB; HostDB:ENSG00000196549.10; -.
GeneCards; MME; -.
HGNC; HGNC:7154; MME.
HPA; CAB000013; -.
HPA; HPA052583; -.
HPA; HPA056072; -.
MalaCards; MME; -.
MIM; 120520; gene.
MIM; 617017; phenotype.
MIM; 617018; phenotype.
neXtProt; NX_P08473; -.
OpenTargets; ENSG00000196549; -.
PharmGKB; PA30864; -.
eggNOG; KOG3624; Eukaryota.
eggNOG; COG3590; LUCA.
GeneTree; ENSGT00760000119162; -.
HOGENOM; HOG000245574; -.
HOVERGEN; HBG005554; -.
InParanoid; P08473; -.
KO; K01389; -.
OMA; TATWRRC; -.
OrthoDB; EOG091G025Y; -.
PhylomeDB; P08473; -.
TreeFam; TF315192; -.
BRENDA; 3.4.24.11; 2681.
Reactome; R-HSA-2022377; Metabolism of Angiotensinogen to Angiotensins.
Reactome; R-HSA-6798695; Neutrophil degranulation.
SIGNOR; P08473; -.
ChiTaRS; MME; human.
EvolutionaryTrace; P08473; -.
GeneWiki; Neprilysin; -.
GenomeRNAi; 4311; -.
PRO; PR:P08473; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000196549; -.
CleanEx; HS_MME; -.
ExpressionAtlas; P08473; baseline and differential.
Genevisible; P08473; HS.
GO; GO:0030424; C:axon; ISS:UniProtKB.
GO; GO:0005903; C:brush border; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
GO; GO:0044306; C:neuron projection terminus; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
GO; GO:0045202; C:synapse; ISS:UniProtKB.
GO; GO:0008021; C:synaptic vesicle; ISS:UniProtKB.
GO; GO:0004175; F:endopeptidase activity; IDA:UniProtKB.
GO; GO:0008238; F:exopeptidase activity; IDA:BHF-UCL.
GO; GO:0004222; F:metalloendopeptidase activity; IDA:UniProtKB.
GO; GO:0008237; F:metallopeptidase activity; EXP:Reactome.
GO; GO:0042277; F:peptide binding; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0097242; P:amyloid-beta clearance; ISS:ARUK-UCL.
GO; GO:0050435; P:amyloid-beta metabolic process; ISS:UniProtKB.
GO; GO:0002003; P:angiotensin maturation; TAS:Reactome.
GO; GO:0071345; P:cellular response to cytokine stimulus; IDA:UniProtKB.
GO; GO:0071492; P:cellular response to UV-A; IDA:UniProtKB.
GO; GO:0071493; P:cellular response to UV-B; IDA:UniProtKB.
GO; GO:0046449; P:creatinine metabolic process; IMP:UniProtKB.
GO; GO:0001822; P:kidney development; IEP:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0006518; P:peptide metabolic process; ISS:UniProtKB.
GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
GO; GO:0090399; P:replicative senescence; IEP:UniProtKB.
GO; GO:0019233; P:sensory perception of pain; ISS:UniProtKB.
CDD; cd08662; M13; 1.
Gene3D; 3.40.390.10; -; 3.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
InterPro; IPR029727; MME/CD10/NEP.
InterPro; IPR000718; Peptidase_M13.
InterPro; IPR018497; Peptidase_M13_C.
InterPro; IPR008753; Peptidase_M13_N.
PANTHER; PTHR11733; PTHR11733; 1.
PANTHER; PTHR11733:SF114; PTHR11733:SF114; 1.
Pfam; PF01431; Peptidase_M13; 1.
Pfam; PF05649; Peptidase_M13_N; 1.
PRINTS; PR00786; NEPRILYSIN.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Charcot-Marie-Tooth disease;
Complete proteome; Disease mutation; Disulfide bond; Glycoprotein;
Hydrolase; Lipoprotein; Membrane; Metal-binding; Metalloprotease;
Myristate; Neurodegeneration; Neuropathy; Phosphoprotein; Protease;
Reference proteome; Signal-anchor; Spinocerebellar ataxia;
Transmembrane; Transmembrane helix; Zinc.
INIT_MET 1 1 Removed.
CHAIN 2 750 Neprilysin.
/FTId=PRO_0000078213.
TOPO_DOM 2 28 Cytoplasmic. {ECO:0000255}.
TRANSMEM 29 51 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 52 750 Extracellular. {ECO:0000255}.
MOTIF 16 23 Stop-transfer sequence. {ECO:0000255}.
ACT_SITE 585 585
ACT_SITE 651 651 Proton donor. {ECO:0000255|PROSITE-
ProRule:PRU10095,
ECO:0000269|PubMed:8168535}.
METAL 584 584 Zinc; catalytic.
METAL 588 588 Zinc; catalytic.
METAL 647 647 Zinc; catalytic.
BINDING 103 103 Substrate carboxyl. {ECO:0000250}.
MOD_RES 4 4 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 6 6 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000269|PubMed:19756956}.
CARBOHYD 145 145 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:10669592,
ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:14747736,
ECO:0000269|PubMed:17704566}.
CARBOHYD 285 285 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754519}.
CARBOHYD 325 325 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:10669592,
ECO:0000269|PubMed:14747736,
ECO:0000269|PubMed:17704566}.
CARBOHYD 628 628 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:10669592,
ECO:0000269|PubMed:14747736,
ECO:0000269|PubMed:17704566,
ECO:0000269|PubMed:22766194}.
DISULFID 57 62
DISULFID 80 735
DISULFID 88 695
DISULFID 143 411
DISULFID 234 242
DISULFID 621 747
VARIANT 12 12 D -> A (in CMT2T; unknown pathological
significance).
{ECO:0000269|PubMed:27588448}.
/FTId=VAR_077684.
VARIANT 143 143 C -> Y (in SCA43; dbSNP:rs879255651).
{ECO:0000269|PubMed:27583304}.
/FTId=VAR_077685.
VARIANT 347 347 Y -> C (in CMT2T; results in reduction of
neprilysin activity; dbSNP:rs138218277).
{ECO:0000269|PubMed:27588448}.
/FTId=VAR_077686.
VARIANT 348 348 A -> P (in CMT2T; unknown pathological
significance; dbSNP:rs199567914).
{ECO:0000269|PubMed:27588448}.
/FTId=VAR_077687.
VARIANT 411 411 Missing (in CMT2T; unknown pathological
significance).
{ECO:0000269|PubMed:26991897}.
/FTId=VAR_077688.
VARIANT 422 422 A -> D (in CMT2T; late-onset form;
results in reduction of neprilysin
activity; dbSNP:rs777476150).
{ECO:0000269|PubMed:27588448}.
/FTId=VAR_077689.
VARIANT 497 497 Y -> H (in dbSNP:rs200308207).
{ECO:0000269|PubMed:26991897}.
/FTId=VAR_077690.
VARIANT 621 621 C -> R (in CMT2T; decrease of protein
expression; dbSNP:rs879253752).
{ECO:0000269|PubMed:26991897}.
/FTId=VAR_077691.
CONFLICT 26 26 P -> R (in Ref. 4; AAA51915).
{ECO:0000305}.
CONFLICT 44 44 T -> R (in Ref. 4; AAA51915).
{ECO:0000305}.
CONFLICT 81 81 T -> R (in Ref. 4; AAA51915).
{ECO:0000305}.
CONFLICT 304 304 T -> R (in Ref. 4; AAA51915).
{ECO:0000305}.
HELIX 60 72 {ECO:0000244|PDB:1R1H}.
TURN 79 81 {ECO:0000244|PDB:1R1H}.
HELIX 83 94 {ECO:0000244|PDB:1R1H}.
STRAND 102 105 {ECO:0000244|PDB:1R1H}.
HELIX 106 122 {ECO:0000244|PDB:1R1H}.
HELIX 131 144 {ECO:0000244|PDB:1R1H}.
HELIX 146 151 {ECO:0000244|PDB:1R1H}.
TURN 152 154 {ECO:0000244|PDB:1R1H}.
HELIX 155 158 {ECO:0000244|PDB:1R1H}.
HELIX 161 164 {ECO:0000244|PDB:1R1H}.
HELIX 168 170 {ECO:0000244|PDB:1R1H}.
STRAND 171 173 {ECO:0000244|PDB:1R1H}.
HELIX 174 177 {ECO:0000244|PDB:1R1H}.
TURN 178 181 {ECO:0000244|PDB:1R1H}.
HELIX 184 195 {ECO:0000244|PDB:1R1H}.
STRAND 200 208 {ECO:0000244|PDB:1R1H}.
STRAND 211 220 {ECO:0000244|PDB:1R1H}.
STRAND 225 228 {ECO:0000244|PDB:1R1H}.
HELIX 229 233 {ECO:0000244|PDB:1R1H}.
HELIX 236 238 {ECO:0000244|PDB:1R1H}.
HELIX 239 259 {ECO:0000244|PDB:1R1H}.
HELIX 266 286 {ECO:0000244|PDB:1R1H}.
HELIX 290 292 {ECO:0000244|PDB:1R1H}.
HELIX 296 299 {ECO:0000244|PDB:1R1H}.
STRAND 302 304 {ECO:0000244|PDB:1R1H}.
HELIX 305 311 {ECO:0000244|PDB:1R1H}.
STRAND 316 319 {ECO:0000244|PDB:1R1H}.
HELIX 323 331 {ECO:0000244|PDB:1R1H}.
HELIX 332 334 {ECO:0000244|PDB:1R1H}.
STRAND 343 347 {ECO:0000244|PDB:1R1H}.
HELIX 349 359 {ECO:0000244|PDB:1R1H}.
HELIX 364 379 {ECO:0000244|PDB:1R1H}.
HELIX 380 382 {ECO:0000244|PDB:1R1H}.
HELIX 385 389 {ECO:0000244|PDB:1R1H}.
HELIX 392 399 {ECO:0000244|PDB:1R1H}.
HELIX 407 418 {ECO:0000244|PDB:1R1H}.
HELIX 420 431 {ECO:0000244|PDB:1R1H}.
HELIX 436 454 {ECO:0000244|PDB:1R1H}.
HELIX 455 457 {ECO:0000244|PDB:1R1H}.
STRAND 459 461 {ECO:0000244|PDB:1R1I}.
HELIX 463 474 {ECO:0000244|PDB:1R1H}.
STRAND 477 481 {ECO:0000244|PDB:1R1H}.
HELIX 485 488 {ECO:0000244|PDB:1R1H}.
HELIX 490 496 {ECO:0000244|PDB:1R1H}.
TURN 497 499 {ECO:0000244|PDB:1R1H}.
HELIX 507 523 {ECO:0000244|PDB:1R1H}.
TURN 524 527 {ECO:0000244|PDB:1R1H}.
STRAND 545 547 {ECO:0000244|PDB:1R1H}.
TURN 548 551 {ECO:0000244|PDB:1R1H}.
STRAND 552 556 {ECO:0000244|PDB:1R1H}.
HELIX 557 559 {ECO:0000244|PDB:1R1H}.
TURN 562 564 {ECO:0000244|PDB:1R1H}.
STRAND 567 569 {ECO:0000244|PDB:2YB9}.
HELIX 571 576 {ECO:0000244|PDB:1R1H}.
HELIX 578 587 {ECO:0000244|PDB:1R1H}.
HELIX 588 590 {ECO:0000244|PDB:1R1H}.
TURN 592 595 {ECO:0000244|PDB:1R1H}.
HELIX 609 627 {ECO:0000244|PDB:1R1H}.
HELIX 632 634 {ECO:0000244|PDB:1R1H}.
STRAND 636 638 {ECO:0000244|PDB:2YB9}.
TURN 641 644 {ECO:0000244|PDB:1R1H}.
HELIX 645 669 {ECO:0000244|PDB:1R1H}.
HELIX 682 692 {ECO:0000244|PDB:1R1H}.
STRAND 696 698 {ECO:0000244|PDB:1R1H}.
HELIX 700 709 {ECO:0000244|PDB:1R1H}.
HELIX 715 724 {ECO:0000244|PDB:1R1H}.
HELIX 727 732 {ECO:0000244|PDB:1R1H}.
SEQUENCE 750 AA; 85514 MW; BCF3827C39898630 CRC64;
MGKSESQMDI TDINTPKPKK KQRWTPLEIS LSVLVLLLTI IAVTMIALYA TYDDGICKSS
DCIKSAARLI QNMDATTEPC TDFFKYACGG WLKRNVIPET SSRYGNFDIL RDELEVVLKD
VLQEPKTEDI VAVQKAKALY RSCINESAID SRGGEPLLKL LPDIYGWPVA TENWEQKYGA
SWTAEKAIAQ LNSKYGKKVL INLFVGTDDK NSVNHVIHID QPRLGLPSRD YYECTGIYKE
ACTAYVDFMI SVARLIRQEE RLPIDENQLA LEMNKVMELE KEIANATAKP EDRNDPMLLY
NKMTLAQIQN NFSLEINGKP FSWLNFTNEI MSTVNISITN EEDVVVYAPE YLTKLKPILT
KYSARDLQNL MSWRFIMDLV SSLSRTYKES RNAFRKALYG TTSETATWRR CANYVNGNME
NAVGRLYVEA AFAGESKHVV EDLIAQIREV FIQTLDDLTW MDAETKKRAE EKALAIKERI
GYPDDIVSND NKLNNEYLEL NYKEDEYFEN IIQNLKFSQS KQLKKLREKV DKDEWISGAA
VVNAFYSSGR NQIVFPAGIL QPPFFSAQQS NSLNYGGIGM VIGHEITHGF DDNGRNFNKD
GDLVDWWTQQ SASNFKEQSQ CMVYQYGNFS WDLAGGQHLN GINTLGENIA DNGGLGQAYR
AYQNYIKKNG EEKLLPGLDL NHKQLFFLNF AQVWCGTYRP EYAVNSIKTD VHSPGNFRII
GTLQNSAEFS EAFHCRKNSY MNPEKKCRVW


Related products :

Catalog number Product name Quantity
E1785h ELISA kit Atriopeptidase,CALLA,Common acute lymphocytic leukemia antigen,Enkephalinase,EPN,Homo sapiens,Human,MME,NEP,Neprilysin,Neutral endopeptidase,Neutral endopeptidase 24.11,SFE,Skin fibroblast 96T
U1785h CLIA Atriopeptidase,CALLA,Common acute lymphocytic leukemia antigen,Enkephalinase,EPN,Homo sapiens,Human,MME,NEP,Neprilysin,Neutral endopeptidase,Neutral endopeptidase 24.11,SFE,Skin fibroblast elasta 96T
E1785h ELISA Atriopeptidase,CALLA,Common acute lymphocytic leukemia antigen,Enkephalinase,EPN,Homo sapiens,Human,MME,NEP,Neprilysin,Neutral endopeptidase,Neutral endopeptidase 24.11,SFE,Skin fibroblast elast 96T
20-783-70663 MOUSE ANTI HUMAN CD10 FITC - CALLA; EC 3.4.24.11; Neutral endopeptidase; NEP; Enkephalinase; Neutral endopeptidase 24.11; Atriopeptidase; Common acute lymphocytic leukemia antigen; CALLA; CD10 antigen 0.1 mg
20-783-70664 MOUSE ANTI HUMAN CD10 - CALLA; EC 3.4.24.11; Neutral endopeptidase; NEP; Enkephalinase; Neutral endopeptidase 24.11; Atriopeptidase; Common acute lymphocytic leukemia antigen; CALLA; CD10 antigen Mono 0.1 mg
20-783-70660 MOUSE ANTI HUMAN CD10 - CALLA; EC 3.4.24.11; Neutral endopeptidase; NEP; Enkephalinase; Neutral endopeptidase 24.11; Atriopeptidase; Common acute lymphocytic leukemia antigen; CALLA; CD10 antigen Mono 0.2 mg
20-783-70666 MOUSE ANTI HUMAN CD10 Azide Free - CALLA; EC 3.4.24.11; Neutral endopeptidase; NEP; Enkephalinase; Neutral endopeptidase 24.11; Atriopeptidase; Common acute lymphocytic leukemia antigen; CALLA; CD10 a 1 mg
20-783-70662 MOUSE ANTI HUMAN CD10 Biotin - CALLA; EC 3.4.24.11; Neutral endopeptidase; NEP; Enkephalinase; Neutral endopeptidase 24.11; Atriopeptidase; Common acute lymphocytic leukemia antigen; CALLA; CD10 antig 0.1 mg
20-783-70665 MOUSE ANTI HUMAN CD10 RPE - CALLA; EC 3.4.24.11; Neutral endopeptidase; NEP; Enkephalinase; Neutral endopeptidase 24.11; Atriopeptidase; Common acute lymphocytic leukemia antigen; CALLA; CD10 antigen 100 TESTS
20-783-70661 MOUSE ANTI HUMAN CD10 APC - CALLA; EC 3.4.24.11; Neutral endopeptidase; NEP; Enkephalinase; Neutral endopeptidase 24.11; Atriopeptidase; Common acute lymphocytic leukemia antigen; CALLA; CD10 antigen 100 TESTS
20-272-192044 CD10 - Mouse monoclonal [MEM - 78] to CD10; EC 3.4.24.11; Neutral endopeptidase; NEP; Enkephalinase; Neutral endopeptidase 24.11; Atriopeptidase; Common acute lymphocytic leukemia antigen; CALLA; CD10 0.1 mg
20-272-191863 CD10 (FITC) - Mouse monoclonal [SJ5-1B4] to CD10 (FITC); EC 3.4.24.11; Neutral endopeptidase; NEP; Enkephalinase; Neutral endopeptidase 24.11; Atriopeptidase; Common acute lymphocytic leukemia antigen 0.1 mg
20-272-191410 CD10. prediluted - Mouse monoclonal [56C6] to CD10. prediluted; EC 3.4.24.11; Neutral endopeptidase; NEP; Enkephalinase; Neutral endopeptidase 24.11; Atriopeptidase; Common acute lymphocytic leukemia 6 ml
E1785p ELISA kit Atriopeptidase,Enkephalinase,MME,NEP,Neprilysin,Neutral endopeptidase,Neutral endopeptidase 24.11,Pig,SFE,Skin fibroblast elastase,Sus scrofa 96T
E1785p ELISA Atriopeptidase,Enkephalinase,MME,NEP,Neprilysin,Neutral endopeptidase,Neutral endopeptidase 24.11,Pig,SFE,Skin fibroblast elastase,Sus scrofa 96T
U1785p CLIA Atriopeptidase,Enkephalinase,MME,NEP,Neprilysin,Neutral endopeptidase,Neutral endopeptidase 24.11,Pig,SFE,Skin fibroblast elastase,Sus scrofa 96T
E1785r ELISA kit Atriopeptidase,Enkephalinase,Mme,NEP,Neprilysin,Neutral endopeptidase,Neutral endopeptidase 24.11,Rat,Rattus norvegicus,SFE,Skin fibroblast elastase 96T
E1785r ELISA Atriopeptidase,Enkephalinase,Mme,NEP,Neprilysin,Neutral endopeptidase,Neutral endopeptidase 24.11,Rat,Rattus norvegicus,SFE,Skin fibroblast elastase 96T
U1785r CLIA Atriopeptidase,Enkephalinase,Mme,NEP,Neprilysin,Neutral endopeptidase,Neutral endopeptidase 24.11,Rat,Rattus norvegicus,SFE,Skin fibroblast elastase 96T
E1785m ELISA Atriopeptidase,Enkephalinase,Mme,Mouse,Mus musculus,NEP,Neprilysin,Neutral endopeptidase,Neutral endopeptidase 24.11,SFE,Skin fibroblast elastase 96T
E1785m ELISA kit Atriopeptidase,Enkephalinase,Mme,Mouse,Mus musculus,NEP,Neprilysin,Neutral endopeptidase,Neutral endopeptidase 24.11,SFE,Skin fibroblast elastase 96T
U1785m CLIA Atriopeptidase,Enkephalinase,Mme,Mouse,Mus musculus,NEP,Neprilysin,Neutral endopeptidase,Neutral endopeptidase 24.11,SFE,Skin fibroblast elastase 96T
E1785Rb ELISA kit Atriopeptidase,Enkephalinase,MME,NEP,Neprilysin,Neutral endopeptidase,Neutral endopeptidase 24.11,Oryctolagus cuniculus,Rabbit,SFE,Skin fibroblast elastase 96T
U1785Rb CLIA Atriopeptidase,Enkephalinase,MME,NEP,Neprilysin,Neutral endopeptidase,Neutral endopeptidase 24.11,Oryctolagus cuniculus,Rabbit,SFE,Skin fibroblast elastase 96T
E1785Rb ELISA Atriopeptidase,Enkephalinase,MME,NEP,Neprilysin,Neutral endopeptidase,Neutral endopeptidase 24.11,Oryctolagus cuniculus,Rabbit,SFE,Skin fibroblast elastase 96T


 

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