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Dipeptidyl peptidase 4 (EC 3.4.14.5) (Dipeptidyl peptidase IV) (DPP IV) (T-cell activation antigen CD26) (CD antigen CD26) [Cleaved into: Dipeptidyl peptidase 4 membrane form (Dipeptidyl peptidase IV membrane form); Dipeptidyl peptidase 4 soluble form (Dipeptidyl peptidase IV soluble form)]

 DPP4_PIG                Reviewed;         766 AA.
P22411; Q866G2;
01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
13-SEP-2004, sequence version 3.
28-MAR-2018, entry version 148.
RecName: Full=Dipeptidyl peptidase 4;
EC=3.4.14.5 {ECO:0000250|UniProtKB:P27487};
AltName: Full=Dipeptidyl peptidase IV;
Short=DPP IV;
AltName: Full=T-cell activation antigen CD26;
AltName: CD_antigen=CD26;
Contains:
RecName: Full=Dipeptidyl peptidase 4 membrane form;
AltName: Full=Dipeptidyl peptidase IV membrane form;
Contains:
RecName: Full=Dipeptidyl peptidase 4 soluble form;
AltName: Full=Dipeptidyl peptidase IV soluble form;
Name=DPP4; Synonyms=CD26;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
TISSUE=Kidney;
PubMed=14719797; DOI=10.1515/BC.2003.172;
Baer J., Weber A., Hoffmann T., Stork J., Wermann M., Wagner L.,
Aust S., Gerhartz B., Demuth H.-U.;
"Characterisation of human dipeptidyl peptidase IV expressed in Pichia
pastoris. A structural and mechanistic comparison between the
recombinant human and the purified porcine enzyme.";
Biol. Chem. 384:1553-1563(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 2-67.
TISSUE=Kidney;
PubMed=7903569; DOI=10.1007/BF00361393;
Thomsen P.D., Qvist H., Marklund L., Andersson L., Sjostrom H.,
Noren O.;
"Assignment of the dipeptidylpeptidase IV (DPP4) gene to pig
chromosome 15q21.";
Mamm. Genome 4:604-607(1993).
[3]
PROTEIN SEQUENCE OF 38-71.
TISSUE=Kidney;
PubMed=1675855;
Seidl R., Mann K., Schaeffer W.;
"N-terminal amino-acid sequence of pig kidney dipeptidyl peptidase IV
solubilized by autolysis.";
Biol. Chem. Hoppe-Seyler 372:213-214(1991).
[4]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 39-766, GLYCOSYLATION AT
ASN-85; ASN-92; ASN-229; ASN-279; ASN-321 AND ASN-685, AND
HOMODIMERIZATION.
PubMed=12690074; DOI=10.1073/pnas.0230620100;
Engel M., Hoffmann T., Wagner L., Wermann M., Heiser U.,
Kiefersauer R., Huber R., Bode W., Demuth H.-U., Brandstetter H.;
"The crystal structure of dipeptidyl peptidase IV (CD26) reveals its
functional regulation and enzymatic mechanism.";
Proc. Natl. Acad. Sci. U.S.A. 100:5063-5068(2003).
-!- FUNCTION: Cell surface glycoprotein receptor involved in the
costimulatory signal essential for T-cell receptor (TCR)-mediated
T-cell activation. Acts as a positive regulator of T-cell
coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC. Its
binding to CAV1 and CARD11 induces T-cell proliferation and NF-
kappa-B activation in a T-cell receptor/CD3-dependent manner. Its
interaction with ADA also regulates lymphocyte-epithelial cell
adhesion. In association with FAP is involved in the pericellular
proteolysis of the extracellular matrix (ECM), the migration and
invasion of endothelial cells into the ECM. May be involved in the
promotion of lymphatic endothelial cells adhesion, migration and
tube formation. When overexpressed, enhanced cell proliferation, a
process inhibited by GPC3. Acts also as a serine exopeptidase with
a dipeptidyl peptidase activity that regulates various
physiological processes by cleaving peptides in the circulation,
including many chemokines, mitogenic growth factors, neuropeptides
and peptide hormones (By similarity). Removes N-terminal
dipeptides sequentially from polypeptides having unsubstituted N-
termini provided that the penultimate residue is proline.
{ECO:0000250|UniProtKB:P27487, ECO:0000269|PubMed:14719797}.
-!- CATALYTIC ACTIVITY: Release of an N-terminal dipeptide, Xaa-Yaa-|-
Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided
Zaa is neither Pro nor hydroxyproline.
{ECO:0000250|UniProtKB:P27487, ECO:0000255|PROSITE-
ProRule:PRU10084}.
-!- ENZYME REGULATION: Inhibited by GPC3 and diprotin A.
{ECO:0000250}.
-!- SUBUNIT: Monomer. Homodimer (PubMed:12690074). Heterodimer with
Seprase (FAP) (By similarity). Requires homodimerization for
optimal dipeptidyl peptidase activity and T-cell costimulation (By
similarity). Found in a membrane raft complex, at least composed
of BCL10, CARD11, DPP4 and IKBKB (By similarity). Associates with
collagen (By similarity). Interacts with PTPRC; the interaction is
enhanced in a interleukin-12-dependent manner in activated
lymphocytes (By similarity). Interacts (via extracellular domain)
with ADA; does not inhibit its dipeptidyl peptidase activity (By
similarity). Interacts with CAV1 (via the N-terminus); the
interaction is direct (By similarity). Interacts (via cytoplasmic
tail) with CARD11 (via PDZ domain); its homodimerization is
necessary for interaction with CARD11 (By similarity). Interacts
with IGF2R; the interaction is direct (By similarity). Interacts
with GPC3 (By similarity). {ECO:0000250|UniProtKB:P27487,
ECO:0000269|PubMed:12690074}.
-!- SUBCELLULAR LOCATION: Dipeptidyl peptidase 4 soluble form:
Secreted. Note=Detected in the serum and the seminal fluid.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane
protein. Apical cell membrane {ECO:0000250}; Single-pass type II
membrane protein {ECO:0000250}. Cell projection, invadopodium
membrane {ECO:0000250}; Single-pass type II membrane protein
{ECO:0000250}. Cell projection, lamellipodium membrane
{ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Cell junction {ECO:0000250}. Membrane raft {ECO:0000250}.
Note=Translocated to the apical membrane through the concerted
action of N- and O-Glycans and its association with lipid
microdomains containing cholesterol and sphingolipids.
Redistributed to membrane rafts in T-cell in a interleukin-12-
dependent activation. Its interaction with CAV1 is necessary for
its translocation to membrane rafts. Colocalized with PTPRC in
membrane rafts. Colocalized with FAP in invadopodia and
lamellipodia of migratory activated endothelial cells in
collagenous matrix. Colocalized with FAP on endothelial cells of
capillary-like microvessels but not large vessels within invasive
breast ductal carcinoma. Colocalized with ADA at the cell junction
in lymphocyte-epithelial cell adhesion. Colocalized with IGF2R in
internalized cytoplasmic vesicles adjacent to the cell surface (By
similarity). {ECO:0000250}.
-!- PTM: The soluble form (Dipeptidyl peptidase 4 soluble form also
named SDPP) derives from the membrane form (Dipeptidyl peptidase 4
membrane form also named MDPP) by proteolytic processing.
-!- PTM: N- and O-Glycosylated. {ECO:0000250}.
-!- PTM: Phosphorylated. Mannose 6-phosphate residues in the
carbohydrate moiety are necessary for interaction with IGF2R in
activated T-cells. Mannose 6-phosphorylation is induced during T-
cell activation (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase S9B family. DPPIV subfamily.
{ECO:0000305}.
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EMBL; AY198323; AAO43404.1; -; mRNA.
EMBL; X73276; CAA51717.1; -; mRNA.
PIR; I47134; I47134.
PIR; S14746; S14746.
RefSeq; NP_999422.1; NM_214257.1.
UniGene; Ssc.16236; -.
PDB; 1ORV; X-ray; 1.80 A; A/B/C/D=39-766.
PDB; 1ORW; X-ray; 2.84 A; A/B/C/D=39-766.
PDB; 2AJ8; X-ray; 2.11 A; A/B/C/D=39-766.
PDB; 2AJB; X-ray; 2.75 A; A/B/C/D=39-766.
PDB; 2AJC; X-ray; 1.95 A; A/B/C/D=39-766.
PDB; 2AJD; X-ray; 2.56 A; A/B/C/D=39-766.
PDB; 2BUA; X-ray; 2.56 A; A/B/C/D=39-766.
PDB; 2BUC; X-ray; 2.50 A; A/B/C/D=39-766.
PDB; 5LLS; X-ray; 2.41 A; A/B/C/D=1-766.
PDBsum; 1ORV; -.
PDBsum; 1ORW; -.
PDBsum; 2AJ8; -.
PDBsum; 2AJB; -.
PDBsum; 2AJC; -.
PDBsum; 2AJD; -.
PDBsum; 2BUA; -.
PDBsum; 2BUC; -.
PDBsum; 5LLS; -.
ProteinModelPortal; P22411; -.
SMR; P22411; -.
STRING; 9823.ENSSSCP00000028692; -.
BindingDB; P22411; -.
ChEMBL; CHEMBL3813; -.
ESTHER; sussc-dpp4; DPP4N_Peptidase_S9.
MEROPS; S09.003; -.
iPTMnet; P22411; -.
PaxDb; P22411; -.
PeptideAtlas; P22411; -.
PRIDE; P22411; -.
Ensembl; ENSSSCT00000017306; ENSSSCP00000016843; ENSSSCG00000015894.
GeneID; 397492; -.
KEGG; ssc:397492; -.
CTD; 1803; -.
eggNOG; KOG2100; Eukaryota.
eggNOG; COG1506; LUCA.
GeneTree; ENSGT00760000119233; -.
HOGENOM; HOG000231875; -.
HOVERGEN; HBG005527; -.
InParanoid; P22411; -.
KO; K01278; -.
OMA; QFILLEY; -.
OrthoDB; EOG091G0BU5; -.
TreeFam; TF313309; -.
BRENDA; 3.4.14.5; 6170.
Reactome; R-SSC-381771; Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
Reactome; R-SSC-400511; Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP).
EvolutionaryTrace; P22411; -.
PRO; PR:P22411; -.
Proteomes; UP000008227; Chromosome 15.
Bgee; ENSSSCG00000015894; -.
ExpressionAtlas; P22411; differential.
Genevisible; P22411; SS.
GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0009986; C:cell surface; ISS:UniProtKB.
GO; GO:0030139; C:endocytic vesicle; ISS:UniProtKB.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0046581; C:intercellular canaliculus; IEA:Ensembl.
GO; GO:0071438; C:invadopodium membrane; ISS:UniProtKB.
GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
GO; GO:0008239; F:dipeptidyl-peptidase activity; ISS:UniProtKB.
GO; GO:0002020; F:protease binding; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0005102; F:receptor binding; ISS:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0001618; F:virus receptor activity; IEA:Ensembl.
GO; GO:0001662; P:behavioral fear response; IEA:Ensembl.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0043542; P:endothelial cell migration; ISS:UniProtKB.
GO; GO:0035641; P:locomotory exploration behavior; IEA:Ensembl.
GO; GO:0010716; P:negative regulation of extracellular matrix disassembly; ISS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0036343; P:psychomotor behavior; IEA:Ensembl.
GO; GO:0033632; P:regulation of cell-cell adhesion mediated by integrin; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0042110; P:T cell activation; IEA:Ensembl.
GO; GO:0031295; P:T cell costimulation; ISS:UniProtKB.
Gene3D; 2.140.10.30; -; 1.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR002471; Pept_S9_AS.
InterPro; IPR001375; Peptidase_S9.
InterPro; IPR002469; Peptidase_S9B_N.
InterPro; IPR038554; Peptidase_S9B_N_sf.
Pfam; PF00930; DPPIV_N; 1.
Pfam; PF00326; Peptidase_S9; 1.
SUPFAM; SSF53474; SSF53474; 1.
PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
1: Evidence at protein level;
3D-structure; Aminopeptidase; Cell adhesion; Cell junction;
Cell membrane; Cell projection; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
Membrane; Protease; Reference proteome; Secreted; Serine protease;
Signal-anchor; Transmembrane; Transmembrane helix.
CHAIN 1 766 Dipeptidyl peptidase 4 membrane form.
/FTId=PRO_0000027217.
CHAIN 38 766 Dipeptidyl peptidase 4 soluble form.
/FTId=PRO_0000027218.
TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.
TRANSMEM 7 27 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 28 766 Extracellular. {ECO:0000255}.
ACT_SITE 630 630 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU10084}.
ACT_SITE 708 708 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU10084}.
ACT_SITE 740 740 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU10084}.
CARBOHYD 85 85 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12690074}.
CARBOHYD 92 92 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12690074}.
CARBOHYD 229 229 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12690074}.
CARBOHYD 279 279 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12690074}.
CARBOHYD 321 321 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12690074}.
CARBOHYD 685 685 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12690074}.
DISULFID 385 394
DISULFID 444 447
DISULFID 454 472
DISULFID 649 762
CONFLICT 32 32 Missing (in Ref. 2). {ECO:0000305}.
HELIX 45 50 {ECO:0000244|PDB:1ORV}.
STRAND 60 62 {ECO:0000244|PDB:1ORV}.
STRAND 64 72 {ECO:0000244|PDB:1ORV}.
STRAND 75 80 {ECO:0000244|PDB:1ORV}.
TURN 81 83 {ECO:0000244|PDB:1ORV}.
STRAND 87 90 {ECO:0000244|PDB:1ORV}.
HELIX 92 96 {ECO:0000244|PDB:2AJ8}.
STRAND 98 100 {ECO:0000244|PDB:2AJ8}.
STRAND 104 107 {ECO:0000244|PDB:1ORV}.
STRAND 111 122 {ECO:0000244|PDB:1ORV}.
STRAND 124 126 {ECO:0000244|PDB:1ORV}.
STRAND 128 136 {ECO:0000244|PDB:1ORV}.
TURN 137 140 {ECO:0000244|PDB:1ORV}.
STRAND 152 157 {ECO:0000244|PDB:1ORV}.
STRAND 159 162 {ECO:0000244|PDB:2AJC}.
STRAND 164 168 {ECO:0000244|PDB:1ORV}.
STRAND 171 177 {ECO:0000244|PDB:1ORV}.
TURN 191 193 {ECO:0000244|PDB:1ORV}.
STRAND 194 198 {ECO:0000244|PDB:1ORV}.
HELIX 201 206 {ECO:0000244|PDB:1ORV}.
STRAND 209 212 {ECO:0000244|PDB:1ORV}.
STRAND 214 216 {ECO:0000244|PDB:1ORV}.
STRAND 220 229 {ECO:0000244|PDB:1ORV}.
STRAND 235 240 {ECO:0000244|PDB:1ORV}.
STRAND 250 255 {ECO:0000244|PDB:1ORV}.
STRAND 265 272 {ECO:0000244|PDB:1ORV}.
HELIX 273 275 {ECO:0000244|PDB:1ORV}.
STRAND 283 287 {ECO:0000244|PDB:1ORV}.
HELIX 291 294 {ECO:0000244|PDB:1ORV}.
STRAND 298 307 {ECO:0000244|PDB:1ORV}.
STRAND 310 317 {ECO:0000244|PDB:1ORV}.
STRAND 320 330 {ECO:0000244|PDB:1ORV}.
TURN 332 334 {ECO:0000244|PDB:1ORV}.
HELIX 341 343 {ECO:0000244|PDB:1ORV}.
STRAND 344 348 {ECO:0000244|PDB:1ORV}.
STRAND 350 352 {ECO:0000244|PDB:1ORV}.
STRAND 354 358 {ECO:0000244|PDB:1ORV}.
STRAND 368 376 {ECO:0000244|PDB:1ORV}.
STRAND 378 380 {ECO:0000244|PDB:2AJ8}.
STRAND 382 388 {ECO:0000244|PDB:1ORV}.
STRAND 394 397 {ECO:0000244|PDB:1ORV}.
STRAND 400 402 {ECO:0000244|PDB:1ORV}.
STRAND 404 410 {ECO:0000244|PDB:1ORV}.
STRAND 412 420 {ECO:0000244|PDB:1ORV}.
HELIX 422 424 {ECO:0000244|PDB:1ORV}.
STRAND 429 435 {ECO:0000244|PDB:1ORV}.
STRAND 438 446 {ECO:0000244|PDB:1ORV}.
TURN 447 449 {ECO:0000244|PDB:1ORV}.
TURN 451 453 {ECO:0000244|PDB:1ORV}.
STRAND 456 461 {ECO:0000244|PDB:1ORV}.
STRAND 465 472 {ECO:0000244|PDB:1ORV}.
STRAND 474 477 {ECO:0000244|PDB:1ORV}.
STRAND 479 484 {ECO:0000244|PDB:1ORV}.
TURN 485 488 {ECO:0000244|PDB:1ORV}.
STRAND 489 495 {ECO:0000244|PDB:1ORV}.
HELIX 498 504 {ECO:0000244|PDB:1ORV}.
STRAND 506 508 {ECO:0000244|PDB:2BUC}.
STRAND 511 519 {ECO:0000244|PDB:1ORV}.
STRAND 522 530 {ECO:0000244|PDB:1ORV}.
STRAND 536 538 {ECO:0000244|PDB:2BUC}.
STRAND 540 546 {ECO:0000244|PDB:1ORV}.
HELIX 563 569 {ECO:0000244|PDB:1ORV}.
STRAND 574 578 {ECO:0000244|PDB:1ORV}.
STRAND 584 586 {ECO:0000244|PDB:1ORV}.
HELIX 588 591 {ECO:0000244|PDB:1ORV}.
HELIX 592 594 {ECO:0000244|PDB:1ORV}.
TURN 598 600 {ECO:0000244|PDB:2BUC}.
HELIX 601 614 {ECO:0000244|PDB:1ORV}.
STRAND 619 629 {ECO:0000244|PDB:1ORV}.
HELIX 631 640 {ECO:0000244|PDB:1ORV}.
TURN 641 643 {ECO:0000244|PDB:1ORV}.
STRAND 648 654 {ECO:0000244|PDB:1ORV}.
HELIX 659 661 {ECO:0000244|PDB:1ORV}.
HELIX 664 671 {ECO:0000244|PDB:1ORV}.
TURN 676 679 {ECO:0000244|PDB:1ORV}.
HELIX 680 684 {ECO:0000244|PDB:1ORV}.
HELIX 689 697 {ECO:0000244|PDB:1ORV}.
STRAND 698 705 {ECO:0000244|PDB:1ORV}.
STRAND 709 711 {ECO:0000244|PDB:1ORV}.
HELIX 713 725 {ECO:0000244|PDB:1ORV}.
STRAND 731 735 {ECO:0000244|PDB:1ORV}.
HELIX 745 762 {ECO:0000244|PDB:1ORV}.
SEQUENCE 766 AA; 88242 MW; 8800D520BAEA856D CRC64;
MKTPWKVLLG LLGIAALVTV ITVPVVLLNK GTDDAAADSR RTYTLTDYLK STFRVKFYTL
QWISDHEYLY KQENNILLFN AEYGNSSIFL ENSTFDELGY STNDYSVSPD RQFILFEYNY
VKQWRHSYTA SYDIYDLNKR QLITEERIPN NTQWITWSPV GHKLAYVWNN DIYVKNEPNL
SSQRITWTGK ENVIYNGVTD WVYEEEVFSA YSALWWSPNG TFLAYAQFND TEVPLIEYSF
YSDESLQYPK TVRIPYPKAG AENPTVKFFV VDTRTLSPNA SVTSYQIVPP ASVLIGDHYL
CGVTWVTEER ISLQWIRRAQ NYSIIDICDY DESTGRWISS VARQHIEIST TGWVGRFRPA
EPHFTSDGNS FYKIISNEEG YKHICHFQTD KSNCTFITKG AWEVIGIEAL TSDYLYYISN
EHKGMPGGRN LYRIQLNDYT KVTCLSCELN PERCQYYSAS FSNKAKYYQL RCFGPGLPLY
TLHSSSSDKE LRVLEDNSAL DKMLQDVQMP SKKLDVINLH GTKFWYQMIL PPHFDKSKKY
PLLIEVYAGP CSQKVDTVFR LSWATYLAST ENIIVASFDG RGSGYQGDKI MHAINRRLGT
FEVEDQIEAT RQFSKMGFVD DKRIAIWGWS YGGYVTSMVL GAGSGVFKCG IAVAPVSKWE
YYDSVYTERY MGLPTPEDNL DYYRNSTVMS RAENFKQVEY LLIHGTADDN VHFQQSAQLS
KALVDAGVDF QTMWYTDEDH GIASNMAHQH IYTHMSHFLK QCFSLP


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15-288-21442 Dipeptidyl peptidase 4 - EC 3.4.14.5; Dipeptidyl peptidase IV; DPP IV; T-cell activation antigen CD26; TP103; Adenosine deaminase complexing protein 2; ADABP Polyclonal 0.1 mg
15-288-21442 Dipeptidyl peptidase 4 - EC 3.4.14.5; Dipeptidyl peptidase IV; DPP IV; T-cell activation antigen CD26; TP103; Adenosine deaminase complexing protein 2; ADABP Polyclonal 0.05 mg
EIAAB11854 Dipeptidyl peptidase 9,Dipeptidyl peptidase IV-related protein 2,Dipeptidyl peptidase IX,Dipeptidyl peptidase-like protein 9,DP9,DPLP9,DPP IX,DPP9,DPRP2,DPRP-2,Homo sapiens,Human
U0884h CLIA ADABP,ADCP2,ADCP-2,Adenosine deaminase complexing protein 2,CD26,Dipeptidyl peptidase 4,Dipeptidyl peptidase IV,DPP IV,DPP4,Homo sapiens,Human,T-cell activation antigen CD26,TP103 96T
E0884h ELISA ADABP,ADCP2,ADCP-2,Adenosine deaminase complexing protein 2,CD26,Dipeptidyl peptidase 4,Dipeptidyl peptidase IV,DPP IV,DPP4,Homo sapiens,Human,T-cell activation antigen CD26,TP103 96T
E0884h ELISA kit ADABP,ADCP2,ADCP-2,Adenosine deaminase complexing protein 2,CD26,Dipeptidyl peptidase 4,Dipeptidyl peptidase IV,DPP IV,DPP4,Homo sapiens,Human,T-cell activation antigen CD26,TP103 96T
E0884b ELISA kit ACT3,Activation molecule 3,ADCP-I,Adenosine deaminase complexing protein,Bos taurus,Bovine,CD26,Dipeptidyl peptidase 4,Dipeptidyl peptidase IV,DPP IV,DPP4,T-cell activation antigen CD26,WC1 96T
E0884b ELISA ACT3,Activation molecule 3,ADCP-I,Adenosine deaminase complexing protein,Bos taurus,Bovine,CD26,Dipeptidyl peptidase 4,Dipeptidyl peptidase IV,DPP IV,DPP4,T-cell activation antigen CD26,WC10 96T
U0884b CLIA ACT3,Activation molecule 3,ADCP-I,Adenosine deaminase complexing protein,Bos taurus,Bovine,CD26,Dipeptidyl peptidase 4,Dipeptidyl peptidase IV,DPP IV,DPP4,T-cell activation antigen CD26,WC10 96T
EIAAB11845 Dipeptidyl aminopeptidase III,Dipeptidyl arylamidase III,Dipeptidyl peptidase 3,Dipeptidyl peptidase III,DPP III,DPP3,Homo sapiens,Human
EIAAB11855 Dipeptidyl peptidase 9,Dipeptidyl peptidase IX,Dipeptidyl peptidase-like protein 9,DP9,DPLP9,DPP IX,Dpp9,Mouse,Mus musculus


 

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