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N-acetylated-alpha-linked acidic dipeptidase 2 (EC 3.4.17.21) (Glutamate carboxypeptidase III) (GCPIII) (N-acetylated-alpha-linked acidic dipeptidase II) (NAALADase II)

 NALD2_HUMAN             Reviewed;         740 AA.
Q9Y3Q0; B3KQR4; Q4KKV4; Q4VAM9;
11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
25-OCT-2017, entry version 143.
RecName: Full=N-acetylated-alpha-linked acidic dipeptidase 2;
EC=3.4.17.21;
AltName: Full=Glutamate carboxypeptidase III;
Short=GCPIII;
AltName: Full=N-acetylated-alpha-linked acidic dipeptidase II;
Short=NAALADase II;
Name=NAALAD2;
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), AND FUNCTION.
TISSUE=Lung carcinoma;
PubMed=10085079; DOI=10.1074/jbc.274.13.8470;
Pangalos M.N., Neefs J.-M., Somers M., Verhasselt P., Bekkers M.,
van der Helm L., Fraiponts E., Ashton D., Gordon R.D.;
"Isolation and expression of novel human glutamate carboxypeptidases
with N-acetylated alpha-linked acidic dipeptidase and dipeptidyl
peptidase IV activity.";
J. Biol. Chem. 274:8470-8483(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=16303743; DOI=10.1093/dnares/12.2.117;
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
Isogai T.;
"Signal sequence and keyword trap in silico for selection of full-
length human cDNAs encoding secretion or membrane proteins from oligo-
capped cDNA libraries.";
DNA Res. 12:117-126(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
ILE-101.
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).
[6]
X-RAY CRYSTALLOGRAPHY (1.29 ANGSTROMS) OF 36-740 ALONE AND IN COMPLEX
WITH GLUTAMATE AND INHIBITORS, SUBUNIT, ZINC-BINDING SITES, COFACTOR,
AND GLYCOSYLATION AT ASN-111; ASN-185; ASN-449 AND ASN-628.
PubMed=19678840; DOI=10.1111/j.1742-4658.2009.07152.x;
Hlouchova K., Barinka C., Konvalinka J., Lubkowski J.;
"Structural insight into the evolutionary and pharmacologic homology
of glutamate carboxypeptidases II and III.";
FEBS J. 276:4448-4462(2009).
-!- FUNCTION: Has N-acetylated-alpha-linked-acidic dipeptidase
(NAALADase) activity. Also exhibits a dipeptidyl-peptidase IV type
activity. Inactivate the peptide neurotransmitter N-
acetylaspartylglutamate. {ECO:0000269|PubMed:10085079}.
-!- CATALYTIC ACTIVITY: Release of an unsubstituted, C-terminal
glutamyl residue, typically from Ac-Asp-Glu or folylpoly-gamma-
glutamates.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:19678840};
Note=Binds 2 Zn(2+) ions per subunit. Required for NAALADase
activity. {ECO:0000269|PubMed:19678840};
-!- ENZYME REGULATION: Inhibited by quisqualate.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19678840}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:Q04609}; Single-pass type II membrane
protein {ECO:0000250|UniProtKB:Q04609}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9Y3Q0-1; Sequence=Displayed;
Name=2;
IsoId=Q9Y3Q0-2; Sequence=VSP_054147, VSP_054148;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highest expression in the testis. Also found
in ovary and spleen. Weak expression in prostate, heart and
placenta. In brain, expressed in striatum, parietal cortex and
ventral striatum with lower levels in hippocampus, brain stem,
putamen and superior colliculus.
-!- DOMAIN: The NAALADase activity is found in the central region, the
dipeptidyl peptidase IV type activity in the C-terminal.
-!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
{ECO:0000305}.
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EMBL; AJ012370; CAB39967.1; -; mRNA.
EMBL; AK075390; BAG52126.1; -; mRNA.
EMBL; AP000648; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471065; EAW66865.1; -; Genomic_DNA.
EMBL; BC096316; AAH96316.1; -; mRNA.
EMBL; BC096317; AAH96317.1; -; mRNA.
EMBL; BC096318; AAH96318.1; -; mRNA.
EMBL; BC099646; AAH99646.1; -; mRNA.
CCDS; CCDS8288.1; -. [Q9Y3Q0-1]
RefSeq; NP_001287859.1; NM_001300930.1.
RefSeq; NP_005458.1; NM_005467.3. [Q9Y3Q0-1]
UniGene; Hs.112482; -.
UniGene; Hs.503560; -.
PDB; 3FEC; X-ray; 1.49 A; A=36-740.
PDB; 3FED; X-ray; 1.29 A; A=36-740.
PDB; 3FEE; X-ray; 1.56 A; A=36-740.
PDB; 3FF3; X-ray; 1.37 A; A=36-740.
PDBsum; 3FEC; -.
PDBsum; 3FED; -.
PDBsum; 3FEE; -.
PDBsum; 3FF3; -.
ProteinModelPortal; Q9Y3Q0; -.
SMR; Q9Y3Q0; -.
BioGrid; 115321; 4.
IntAct; Q9Y3Q0; 2.
MINT; MINT-2823431; -.
STRING; 9606.ENSP00000432481; -.
BindingDB; Q9Y3Q0; -.
ChEMBL; CHEMBL2609; -.
MEROPS; M28.012; -.
iPTMnet; Q9Y3Q0; -.
PhosphoSitePlus; Q9Y3Q0; -.
BioMuta; NAALAD2; -.
DMDM; 20139300; -.
EPD; Q9Y3Q0; -.
PaxDb; Q9Y3Q0; -.
PeptideAtlas; Q9Y3Q0; -.
PRIDE; Q9Y3Q0; -.
Ensembl; ENST00000375944; ENSP00000365111; ENSG00000077616. [Q9Y3Q0-2]
Ensembl; ENST00000534061; ENSP00000432481; ENSG00000077616. [Q9Y3Q0-1]
GeneID; 10003; -.
KEGG; hsa:10003; -.
UCSC; uc001pdf.5; human. [Q9Y3Q0-1]
CTD; 10003; -.
DisGeNET; 10003; -.
EuPathDB; HostDB:ENSG00000077616.10; -.
GeneCards; NAALAD2; -.
HGNC; HGNC:14526; NAALAD2.
HPA; HPA060820; -.
HPA; HPA065419; -.
MIM; 611636; gene.
neXtProt; NX_Q9Y3Q0; -.
OpenTargets; ENSG00000077616; -.
PharmGKB; PA31430; -.
eggNOG; KOG2195; Eukaryota.
eggNOG; COG2234; LUCA.
GeneTree; ENSGT00550000074421; -.
HOGENOM; HOG000134689; -.
HOVERGEN; HBG051639; -.
InParanoid; Q9Y3Q0; -.
KO; K01301; -.
OMA; SFRKVRM; -.
OrthoDB; EOG091G02ZM; -.
PhylomeDB; Q9Y3Q0; -.
TreeFam; TF312981; -.
Reactome; R-HSA-70614; Amino acid synthesis and interconversion (transamination).
EvolutionaryTrace; Q9Y3Q0; -.
GenomeRNAi; 10003; -.
PRO; PR:Q9Y3Q0; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000077616; -.
CleanEx; HS_NAALAD2; -.
ExpressionAtlas; Q9Y3Q0; baseline and differential.
Genevisible; Q9Y3Q0; HS.
GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0004180; F:carboxypeptidase activity; NAS:UniProtKB.
GO; GO:0016805; F:dipeptidase activity; TAS:Reactome.
GO; GO:0008239; F:dipeptidyl-peptidase activity; NAS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0050129; F:N-formylglutamate deformylase activity; IEA:Ensembl.
GO; GO:0008236; F:serine-type peptidase activity; NAS:UniProtKB.
GO; GO:0008652; P:cellular amino acid biosynthetic process; TAS:Reactome.
GO; GO:0042135; P:neurotransmitter catabolic process; IEA:Ensembl.
GO; GO:0006508; P:proteolysis; NAS:UniProtKB.
Gene3D; 1.20.930.40; -; 1.
InterPro; IPR003137; PA_domain.
InterPro; IPR007484; Peptidase_M28.
InterPro; IPR007365; TFR-like_dimer_dom.
InterPro; IPR036757; TFR-like_dimer_dom_sf.
Pfam; PF02225; PA; 1.
Pfam; PF04389; Peptidase_M28; 1.
Pfam; PF04253; TFR_dimer; 1.
SUPFAM; SSF47672; SSF47672; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Carboxypeptidase;
Cell membrane; Complete proteome; Dipeptidase; Glycoprotein;
Hydrolase; Membrane; Metal-binding; Metalloprotease;
Multifunctional enzyme; Polymorphism; Protease; Reference proteome;
Signal-anchor; Transmembrane; Transmembrane helix; Zinc.
CHAIN 1 740 N-acetylated-alpha-linked acidic
dipeptidase 2.
/FTId=PRO_0000174121.
TOPO_DOM 1 7 Cytoplasmic. {ECO:0000255}.
TRANSMEM 8 31 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 32 740 Extracellular. {ECO:0000255}.
REGION 264 577 NAALADase.
REGION 507 508 Substrate binding. {ECO:0000244|PDB:3FEC,
ECO:0000244|PDB:3FEE,
ECO:0000244|PDB:3FF3,
ECO:0000269|PubMed:19678840}.
REGION 524 526 Substrate binding.
{ECO:0000250|UniProtKB:Q04609}.
REGION 542 543 Substrate binding. {ECO:0000244|PDB:3FEC,
ECO:0000244|PDB:3FED,
ECO:0000244|PDB:3FEE,
ECO:0000244|PDB:3FF3,
ECO:0000269|PubMed:19678840}.
REGION 689 690 Substrate binding. {ECO:0000244|PDB:3FEC,
ECO:0000244|PDB:3FED,
ECO:0000244|PDB:3FEE,
ECO:0000244|PDB:3FF3,
ECO:0000269|PubMed:19678840}.
ACT_SITE 414 414 Nucleophile; for NAALADase activity.
{ECO:0000250|UniProtKB:Q04609}.
ACT_SITE 618 618 Charge relay system. {ECO:0000255}.
ACT_SITE 656 656 Charge relay system. {ECO:0000255}.
ACT_SITE 679 679 Charge relay system. {ECO:0000255}.
METAL 259 259 Calcium. {ECO:0000244|PDB:3FEC,
ECO:0000244|PDB:3FED,
ECO:0000244|PDB:3FEE,
ECO:0000244|PDB:3FF3,
ECO:0000269|PubMed:19678840}.
METAL 262 262 Calcium; via carbonyl oxygen.
{ECO:0000244|PDB:3FEC,
ECO:0000244|PDB:3FED,
ECO:0000244|PDB:3FEE,
ECO:0000244|PDB:3FF3,
ECO:0000269|PubMed:19678840}.
METAL 367 367 Zinc 1; via tele nitrogen; catalytic.
{ECO:0000244|PDB:3FEC,
ECO:0000244|PDB:3FED,
ECO:0000244|PDB:3FEE,
ECO:0000244|PDB:3FF3,
ECO:0000269|PubMed:19678840}.
METAL 377 377 Zinc 1; catalytic. {ECO:0000244|PDB:3FEC,
ECO:0000244|PDB:3FED,
ECO:0000244|PDB:3FEE,
ECO:0000244|PDB:3FF3,
ECO:0000269|PubMed:19678840}.
METAL 377 377 Zinc 2. {ECO:0000244|PDB:3FEC,
ECO:0000244|PDB:3FED,
ECO:0000244|PDB:3FEE,
ECO:0000244|PDB:3FF3,
ECO:0000269|PubMed:19678840}.
METAL 415 415 Zinc 2. {ECO:0000244|PDB:3FEC,
ECO:0000244|PDB:3FED,
ECO:0000244|PDB:3FEE,
ECO:0000244|PDB:3FF3,
ECO:0000269|PubMed:19678840}.
METAL 423 423 Calcium. {ECO:0000244|PDB:3FEC,
ECO:0000244|PDB:3FED,
ECO:0000244|PDB:3FEE,
ECO:0000244|PDB:3FF3,
ECO:0000269|PubMed:19678840}.
METAL 426 426 Calcium. {ECO:0000244|PDB:3FEC,
ECO:0000244|PDB:3FED,
ECO:0000244|PDB:3FEE,
ECO:0000244|PDB:3FF3,
ECO:0000269|PubMed:19678840}.
METAL 443 443 Zinc 1; catalytic. {ECO:0000244|PDB:3FEC,
ECO:0000244|PDB:3FED,
ECO:0000244|PDB:3FEE,
ECO:0000244|PDB:3FF3,
ECO:0000269|PubMed:19678840}.
METAL 543 543 Zinc 2; via tele nitrogen.
{ECO:0000244|PDB:3FEC,
ECO:0000244|PDB:3FED,
ECO:0000244|PDB:3FEE,
ECO:0000244|PDB:3FF3,
ECO:0000269|PubMed:19678840}.
BINDING 200 200 Substrate. {ECO:0000244|PDB:3FEC,
ECO:0000244|PDB:3FED,
ECO:0000244|PDB:3FEE,
ECO:0000244|PDB:3FF3,
ECO:0000269|PubMed:19678840}.
BINDING 247 247 Substrate. {ECO:0000244|PDB:3FEC,
ECO:0000244|PDB:3FED,
ECO:0000244|PDB:3FEE,
ECO:0000244|PDB:3FF3,
ECO:0000269|PubMed:19678840}.
BINDING 414 414 Substrate. {ECO:0000244|PDB:3FEC,
ECO:0000244|PDB:3FED,
ECO:0000244|PDB:3FEE,
ECO:0000244|PDB:3FF3,
ECO:0000269|PubMed:19678840}.
BINDING 542 542 Substrate.
{ECO:0000250|UniProtKB:Q04609}.
CARBOHYD 111 111 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3FEC,
ECO:0000244|PDB:3FED,
ECO:0000244|PDB:3FEE,
ECO:0000244|PDB:3FF3,
ECO:0000269|PubMed:19678840}.
CARBOHYD 143 143 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:Q04609}.
CARBOHYD 185 185 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3FEC,
ECO:0000244|PDB:3FED,
ECO:0000244|PDB:3FEE,
ECO:0000244|PDB:3FF3,
ECO:0000269|PubMed:19678840}.
CARBOHYD 314 314 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 449 449 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3FEC,
ECO:0000244|PDB:3FED,
ECO:0000244|PDB:3FEE,
ECO:0000244|PDB:3FF3,
ECO:0000269|PubMed:19678840}.
CARBOHYD 603 603 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 628 628 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3FEC,
ECO:0000244|PDB:3FED,
ECO:0000244|PDB:3FEE,
ECO:0000244|PDB:3FF3,
ECO:0000269|PubMed:19678840}.
VAR_SEQ 266 305 EYTFRLDVEEGVGIPRIPVHPIGYNDAEILLRYLGGIAPP
-> GTSYLLQVATTNMLENHFLESMMLSLILKIKPTLVWPG
KK (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_054147.
VAR_SEQ 306 740 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_054148.
VARIANT 101 101 V -> I (in dbSNP:rs11018879).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_034120.
VARIANT 446 446 I -> V (in dbSNP:rs10830430).
/FTId=VAR_034121.
HELIX 47 54 {ECO:0000244|PDB:3FED}.
HELIX 57 67 {ECO:0000244|PDB:3FED}.
STRAND 68 70 {ECO:0000244|PDB:3FED}.
HELIX 77 93 {ECO:0000244|PDB:3FED}.
STRAND 96 109 {ECO:0000244|PDB:3FED}.
STRAND 117 121 {ECO:0000244|PDB:3FED}.
STRAND 127 130 {ECO:0000244|PDB:3FED}.
STRAND 164 166 {ECO:0000244|PDB:3FED}.
HELIX 172 180 {ECO:0000244|PDB:3FED}.
STRAND 190 194 {ECO:0000244|PDB:3FED}.
HELIX 200 209 {ECO:0000244|PDB:3FED}.
STRAND 213 218 {ECO:0000244|PDB:3FED}.
HELIX 221 224 {ECO:0000244|PDB:3FED}.
TURN 232 234 {ECO:0000244|PDB:3FED}.
STRAND 235 237 {ECO:0000244|PDB:3FED}.
HELIX 273 275 {ECO:0000244|PDB:3FED}.
STRAND 284 287 {ECO:0000244|PDB:3FED}.
HELIX 289 297 {ECO:0000244|PDB:3FED}.
HELIX 307 309 {ECO:0000244|PDB:3FED}.
STRAND 312 315 {ECO:0000244|PDB:3FED}.
STRAND 320 323 {ECO:0000244|PDB:3FED}.
STRAND 331 336 {ECO:0000244|PDB:3FED}.
STRAND 339 352 {ECO:0000244|PDB:3FED}.
STRAND 355 367 {ECO:0000244|PDB:3FED}.
STRAND 371 373 {ECO:0000244|PDB:3FED}.
TURN 375 378 {ECO:0000244|PDB:3FED}.
HELIX 379 397 {ECO:0000244|PDB:3FED}.
STRAND 403 412 {ECO:0000244|PDB:3FED}.
HELIX 414 416 {ECO:0000244|PDB:3FED}.
HELIX 419 435 {ECO:0000244|PDB:3FED}.
STRAND 436 441 {ECO:0000244|PDB:3FED}.
STRAND 445 447 {ECO:0000244|PDB:3FED}.
STRAND 449 456 {ECO:0000244|PDB:3FED}.
HELIX 458 460 {ECO:0000244|PDB:3FED}.
HELIX 461 468 {ECO:0000244|PDB:3FED}.
HELIX 483 490 {ECO:0000244|PDB:3FED}.
STRAND 491 493 {ECO:0000244|PDB:3FED}.
STRAND 496 500 {ECO:0000244|PDB:3FED}.
STRAND 507 509 {ECO:0000244|PDB:3FED}.
HELIX 512 516 {ECO:0000244|PDB:3FED}.
STRAND 522 528 {ECO:0000244|PDB:3FED}.
TURN 531 533 {ECO:0000244|PDB:3FED}.
STRAND 536 538 {ECO:0000244|PDB:3FED}.
TURN 540 543 {ECO:0000244|PDB:3FED}.
HELIX 549 555 {ECO:0000244|PDB:3FED}.
HELIX 561 579 {ECO:0000244|PDB:3FED}.
HELIX 587 605 {ECO:0000244|PDB:3FED}.
HELIX 606 608 {ECO:0000244|PDB:3FED}.
HELIX 609 615 {ECO:0000244|PDB:3FED}.
HELIX 620 640 {ECO:0000244|PDB:3FED}.
HELIX 648 664 {ECO:0000244|PDB:3FED}.
STRAND 679 685 {ECO:0000244|PDB:3FED}.
STRAND 688 695 {ECO:0000244|PDB:3FED}.
HELIX 696 702 {ECO:0000244|PDB:3FED}.
HELIX 705 707 {ECO:0000244|PDB:3FED}.
HELIX 711 736 {ECO:0000244|PDB:3FED}.
SEQUENCE 740 AA; 83592 MW; 040624D691ECF879 CRC64;
MAESRGRLYL WMCLAAALAS FLMGFMVGWF IKPLKETTTS VRYHQSIRWK LVSEMKAENI
KSFLRSFTKL PHLAGTEQNF LLAKKIQTQW KKFGLDSAKL VHYDVLLSYP NETNANYISI
VDEHETEIFK TSYLEPPPDG YENVTNIVPP YNAFSAQGMP EGDLVYVNYA RTEDFFKLER
EMGINCTGKI VIARYGKIFR GNKVKNAMLA GAIGIILYSD PADYFAPEVQ PYPKGWNLPG
TAAQRGNVLN LNGAGDPLTP GYPAKEYTFR LDVEEGVGIP RIPVHPIGYN DAEILLRYLG
GIAPPDKSWK GALNVSYSIG PGFTGSDSFR KVRMHVYNIN KITRIYNVVG TIRGSVEPDR
YVILGGHRDS WVFGAIDPTS GVAVLQEIAR SFGKLMSKGW RPRRTIIFAS WDAEEFGLLG
STEWAEENVK ILQERSIAYI NSDSSIEGNY TLRVDCTPLL YQLVYKLTKE IPSPDDGFES
KSLYESWLEK DPSPENKNLP RINKLGSGSD FEAYFQRLGI ASGRARYTKN KKTDKYSSYP
VYHTIYETFE LVEKFYDPTF KKQLSVAQLR GALVYELVDS KIIPFNIQDY AEALKNYAAS
IYNLSKKHDQ QLTDHGVSFD SLFSAVKNFS EAASDFHKRL IQVDLNNPIA VRMMNDQLML
LERAFIDPLG LPGKLFYRHI IFAPSSHNKY AGESFPGIYD AIFDIENKAN SRLAWKEVKK
HISIAAFTIQ AAAGTLKEVL


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EIAAB26325 GCPIII,Glutamate carboxypeptidase III,Mouse,Mus musculus,NAAG-peptidase II,Naalad2,NAALADase II,N-acetylaspartylglutamate peptidase II,N-acetylated-alpha-linked acidic dipeptidase 2,N-acetylated-alpha
20-272-191781 PSMA - Mouse monoclonal [YPSMA-1] to PSMA; EC 3.4.17.21; Glutamate carboxypeptidase II; Membrane glutamate carboxypeptidase; mGCP; N-acetylated-alpha-linked acidic dipeptidase I; NAALADase I; Pteroylp 0.25 mg
EIAAB26273 Homo sapiens,Human,Inactive N-acetylated-alpha-linked acidic dipeptidase-like protein 2,NAALADase L2,NAALADL2
EIAAB26329 Gm964,Mouse,Mus musculus,NAALADase L,Naaladasel,Naaladl1,N-acetylated-alpha-linked acidic dipeptidase-like protein
EIAAB26328 100 kDa ileum brush border membrane protein,I100,Ileal dipeptidylpeptidase,NAALADase L,Naaladl,Naaladl1,N-acetylated-alpha-linked acidic dipeptidase-like protein,Rat,Rattus norvegicus
EIAAB26327 100 kDa ileum brush border membrane protein,Homo sapiens,Human,I100,Ileal dipeptidylpeptidase,NAALADase L,NAALADASEL,NAALADL,NAALADL1,N-acetylated-alpha-linked acidic dipeptidase-like protein
NAB2 NAALADL2 Gene N-acetylated alpha-linked acidic dipeptidase-like 2
NAB1 NAALADL1 Gene N-acetylated alpha-linked acidic dipeptidase-like 1
NALD2_HUMAN Human ELISA Kit FOR N-acetylated-alpha-linked acidic dipeptidase 2 96T
NAALADL2 NAALAD2 Gene N-acetylated alpha-linked acidic dipeptidase 2
G45IP_RAT Human ELISA Kit FOR N-acetylated-alpha-linked acidic dipeptidase-like protein 96T
TM207_MOUSE Human ELISA Kit FOR N-acetylated-alpha-linked acidic dipeptidase-like protein 96T
CSB-EL015399RA Rat N-acetylated-alpha-linked acidic dipeptidase-like protein(NAALADL1) ELISA kit 96T
CSB-EL015398HU Human N-acetylated-alpha-linked acidic dipeptidase 2(NAALAD2) ELISA kit 96T
CSB-EL015398MO Mouse N-acetylated-alpha-linked acidic dipeptidase 2(NAALAD2) ELISA kit 96T
E0153r Human ELISA Kit FOR N-acetylated-alpha-linked acidic dipeptidase-like protein 96T
CSB-EL015399RA Rat N-acetylated-alpha-linked acidic dipeptidase-like protein(NAALADL1) ELISA kit SpeciesRat 96T
CSB-EL015399MO Mouse N-acetylated-alpha-linked acidic dipeptidase-like protein(NAALADL1) ELISA kit 96T
CSB-EL015399HU Human N-acetylated-alpha-linked acidic dipeptidase-like protein(NAALADL1) ELISA kit 96T
CSB-EL015398MO Mouse N-acetylated-alpha-linked acidic dipeptidase 2(NAALAD2) ELISA kit SpeciesMouse 96T
CSB-EL015398HU Human N-acetylated-alpha-linked acidic dipeptidase 2(NAALAD2) ELISA kit SpeciesHuman 96T
NALDL_RAT ELISA Kit FOR N-acetylated-alpha-linked acidic dipeptidase-like protein; organism: Rat; gene name: Naaladl1 96T
CSB-EL015399HU Human N-acetylated-alpha-linked acidic dipeptidase-like protein(NAALADL1) ELISA kit SpeciesHuman 96T
CSB-EL015399MO Mouse N-acetylated-alpha-linked acidic dipeptidase-like protein(NAALADL1) ELISA kit SpeciesMouse 96T


 

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