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Dipeptidyl peptidase 4 (EC 3.4.14.5) (Bile canaliculus domain-specific membrane glycoprotein) (Dipeptidyl peptidase IV) (DPP IV) (GP110 glycoprotein) (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); Dipeptidyl peptidase 4 60 kDa soluble form (Dipeptidyl peptidase IV 60 kDa soluble form)]

 DPP4_RAT                Reviewed;         767 AA.
P14740;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
07-DEC-2004, sequence version 2.
10-MAY-2017, entry version 150.
RecName: Full=Dipeptidyl peptidase 4;
EC=3.4.14.5 {ECO:0000250|UniProtKB:P27487};
AltName: Full=Bile canaliculus domain-specific membrane glycoprotein;
AltName: Full=Dipeptidyl peptidase IV;
Short=DPP IV;
AltName: Full=GP110 glycoprotein;
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;
Contains:
RecName: Full=Dipeptidyl peptidase 4 60 kDa soluble form;
AltName: Full=Dipeptidyl peptidase IV 60 kDa soluble form;
Name=Dpp4; Synonyms=Cd26;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=2563382;
Ogata S., Misumi Y., Ikehara Y.;
"Primary structure of rat liver dipeptidyl peptidase IV deduced from
its cDNA and identification of the NH2-terminal signal sequence as the
membrane-anchoring domain.";
J. Biol. Chem. 264:3596-3601(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3479775; DOI=10.1073/pnas.84.22.7962;
Hong W., Doyle D.;
"cDNA cloning for a bile canaliculus domain-specific membrane
glycoprotein of rat hepatocytes.";
Proc. Natl. Acad. Sci. U.S.A. 84:7962-7966(1987).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-40.
PubMed=3182821;
Hong W.J., Doyle D.;
"Membrane orientation of rat gp110 as studied by in vitro
translation.";
J. Biol. Chem. 263:16892-16898(1988).
[4]
PROTEIN SEQUENCE OF 28-58, AND TISSUE SPECIFICITY.
PubMed=1970322; DOI=10.1002/hep.1840110403;
McCaughan G.W., Wickson J.E., Creswick P.F., Gorrell M.D.;
"Identification of the bile canalicular cell surface molecule GP110 as
the ectopeptidase dipeptidyl peptidase IV: an analysis by tissue
distribution, purification and N-terminal amino acid sequence.";
Hepatology 11:534-544(1990).
[5]
PROTEIN SEQUENCE OF 281-302, AND MUTAGENESIS OF GLY-629; TRP-630;
SER-631; TYR-632 AND GLY-633.
TISSUE=Kidney;
PubMed=7905271;
Iwaki-Egawa S., Watanabe Y., Fujimoto Y.;
"N-terminal amino acid sequence of the 60-kDa protein of rat kidney
dipeptidyl peptidase IV.";
Biol. Chem. Hoppe-Seyler 374:973-975(1993).
[6]
PROTEIN SEQUENCE OF 624-648.
PubMed=1347701; DOI=10.1021/bi00124a019;
Ogata S., Misumi Y., Tsuji E., Takami N., Oda K., Ikehara Y.;
"Identification of the active site residues in dipeptidyl peptidase IV
by affinity labeling and site-directed mutagenesis.";
Biochemistry 31:2582-2587(1992).
[7]
SIGNAL-ANCHOR.
PubMed=1974258; DOI=10.1083/jcb.111.2.323;
Hong W., Doyle D.;
"Molecular dissection of the NH2-terminal signal/anchor sequence of
rat dipeptidyl peptidase IV.";
J. Cell Biol. 111:323-328(1990).
[8]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 38-767 IN COMPLEX WITH
INHIBITORS, GLYCOSYLATION AT ASN-83; ASN-90; ASN-227; ASN-319 AND
ASN-521, AND DISULFIDE BONDS.
PubMed=16768443; DOI=10.1021/bi060184f;
Longenecker K.L., Stewart K.D., Madar D.J., Jakob C.G., Fry E.H.,
Wilk S., Lin C.W., Ballaron S.J., Stashko M.A., Lubben T.H., Yong H.,
Pireh D., Pei Z., Basha F., Wiedeman P.E., von Geldern T.W.,
Trevillyan J.M., Stoll V.S.;
"Crystal structures of DPP-IV (CD26) from rat kidney exhibit flexible
accommodation of peptidase-selective inhibitors.";
Biochemistry 45:7474-7482(2006).
-!- 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. Removes N-terminal dipeptides sequentially
from polypeptides having unsubstituted N-termini provided that the
penultimate residue is proline. {ECO:0000250|UniProtKB:P27487}.
-!- 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:0000269|PubMed:16768443}.
-!- SUBUNIT: Monomer. Homodimer. Heterodimer with Seprase (FAP).
Requires homodimerization for optimal dipeptidyl peptidase
activity and T-cell costimulation. Found in a membrane raft
complex, at least composed of BCL10, CARD11, DPP4 and IKBKB.
Associates with collagen. Interacts with PTPRC; the interaction is
enhanced in a interleukin-12-dependent manner in activated
lymphocytes. Interacts (via extracellular domain) with ADA; does
not inhibit its dipeptidyl peptidase activity. Interacts with CAV1
(via the N-terminus); the interaction is direct. Interacts (via
cytoplasmic tail) with CARD11 (via PDZ domain); its
homodimerization is necessary for interaction with CARD11.
Interacts with IGF2R; the interaction is direct. Interacts with
GPC3. {ECO:0000250|UniProtKB:P27487}.
-!- 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}.
-!- TISSUE SPECIFICITY: Expressed in bile ducts and other epithelial
brush borders (small intestine, kidney, colon, pancreatic duct);
acinar structures in salivary glands; endothelial structures and T
cell areas in thymus, spleen and lymph node.
{ECO:0000269|PubMed:1970322}.
-!- 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.
{ECO:0000250}.
-!- 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; J04591; AAA41096.1; -; mRNA.
EMBL; J02997; AAA41272.1; -; mRNA.
PIR; A39914; A39914.
RefSeq; NP_036921.1; NM_012789.1.
UniGene; Rn.91364; -.
PDB; 2GBC; X-ray; 2.80 A; A/B=38-767.
PDB; 2GBF; X-ray; 3.10 A; A/B=38-767.
PDB; 2GBG; X-ray; 3.00 A; A/B=38-767.
PDB; 2GBI; X-ray; 3.30 A; A/B=38-767.
PDB; 2I3Z; X-ray; 2.90 A; A/B=38-767.
PDB; 2OAE; X-ray; 3.00 A; A/B=38-767.
PDB; 4FFV; X-ray; 2.40 A; A/B=38-767.
PDB; 4FFW; X-ray; 2.90 A; A/B=38-767.
PDBsum; 2GBC; -.
PDBsum; 2GBF; -.
PDBsum; 2GBG; -.
PDBsum; 2GBI; -.
PDBsum; 2I3Z; -.
PDBsum; 2OAE; -.
PDBsum; 4FFV; -.
PDBsum; 4FFW; -.
ProteinModelPortal; P14740; -.
SMR; P14740; -.
IntAct; P14740; 1.
MINT; MINT-4655516; -.
STRING; 10116.ENSRNOP00000045536; -.
BindingDB; P14740; -.
ChEMBL; CHEMBL4653; -.
ESTHER; ratno-dpp4; DPP4N_Peptidase_S9.
MEROPS; S09.003; -.
iPTMnet; P14740; -.
PhosphoSitePlus; P14740; -.
SwissPalm; P14740; -.
PaxDb; P14740; -.
PRIDE; P14740; -.
GeneID; 25253; -.
KEGG; rno:25253; -.
UCSC; RGD:2515; rat.
CTD; 1803; -.
RGD; 2515; Dpp4.
eggNOG; KOG2100; Eukaryota.
eggNOG; COG1506; LUCA.
HOGENOM; HOG000231875; -.
HOVERGEN; HBG005527; -.
InParanoid; P14740; -.
KO; K01278; -.
PhylomeDB; P14740; -.
BRENDA; 3.4.14.5; 5301.
EvolutionaryTrace; P14740; -.
PRO; PR:P14740; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-SubCell.
GO; GO:0009986; C:cell surface; IDA:RGD.
GO; GO:0030139; C:endocytic vesicle; ISS:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0005518; F:collagen binding; IDA:RGD.
GO; GO:0008239; F:dipeptidyl-peptidase activity; IDA:RGD.
GO; GO:0042277; F:peptide binding; IDA:RGD.
GO; GO:0002020; F:protease binding; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:RGD.
GO; GO:0005102; F:receptor binding; ISS:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0043542; P:endothelial cell migration; ISS:UniProtKB.
GO; GO:0051234; P:establishment of localization; IMP:RGD.
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:0006508; P:proteolysis; IDA:RGD.
GO; GO:0002709; P:regulation of T cell mediated immunity; IMP:RGD.
GO; GO:0031295; P:T cell costimulation; ISS:UniProtKB.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR002471; Pept_S9_AS.
InterPro; IPR001375; Peptidase_S9.
InterPro; IPR002469; Peptidase_S9B_N.
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 1 767 Dipeptidyl peptidase 4 membrane form.
/FTId=PRO_0000027219.
CHAIN 37 767 Dipeptidyl peptidase 4 soluble form.
/FTId=PRO_0000027220.
CHAIN 281 767 Dipeptidyl peptidase 4 60 kDa soluble
form.
/FTId=PRO_0000027221.
TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.
TRANSMEM 7 28 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 29 767 Extracellular. {ECO:0000255}.
ACT_SITE 631 631 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU10084}.
ACT_SITE 709 709 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU10084}.
ACT_SITE 741 741 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU10084}.
CARBOHYD 83 83 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16768443}.
CARBOHYD 90 90 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16768443}.
CARBOHYD 148 148 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
CARBOHYD 217 217 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
CARBOHYD 227 227 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16768443}.
CARBOHYD 319 319 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16768443}.
CARBOHYD 521 521 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16768443}.
CARBOHYD 686 686 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
DISULFID 326 337 {ECO:0000269|PubMed:16768443}.
DISULFID 383 395 {ECO:0000269|PubMed:16768443}.
DISULFID 445 448 {ECO:0000269|PubMed:16768443}.
DISULFID 455 473 {ECO:0000269|PubMed:16768443}.
DISULFID 650 763 {ECO:0000269|PubMed:16768443}.
MUTAGEN 629 629 G->A: Reduced activity.
{ECO:0000269|PubMed:7905271}.
MUTAGEN 629 629 G->R: Reduced activity.
{ECO:0000269|PubMed:7905271}.
MUTAGEN 630 630 W->E: No effect on activity.
{ECO:0000269|PubMed:7905271}.
MUTAGEN 631 631 S->A: Reduced activity.
{ECO:0000269|PubMed:7905271}.
MUTAGEN 632 632 Y->F: No effect on activity.
{ECO:0000269|PubMed:7905271}.
MUTAGEN 632 632 Y->G: Reduced activity.
{ECO:0000269|PubMed:7905271}.
MUTAGEN 632 632 Y->L: Reduced activity.
{ECO:0000269|PubMed:7905271}.
MUTAGEN 633 633 G->A: Reduced activity.
{ECO:0000269|PubMed:7905271}.
MUTAGEN 633 633 G->S: Reduced activity.
{ECO:0000269|PubMed:7905271}.
CONFLICT 38 38 R -> A (in Ref. 1; AAA41096).
{ECO:0000305}.
CONFLICT 54 54 Missing (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 183 183 I -> T (in Ref. 2; AAA41272).
{ECO:0000305}.
CONFLICT 332 332 T -> N (in Ref. 2; AAA41272).
{ECO:0000305}.
CONFLICT 352 352 C -> V (in Ref. 2; AAA41272).
{ECO:0000305}.
CONFLICT 394 394 V -> D (in Ref. 2; AAA41272).
{ECO:0000305}.
CONFLICT 562 562 L -> F (in Ref. 2; AAA41272).
{ECO:0000305}.
CONFLICT 624 624 R -> Q (in Ref. 2; AAA41272).
{ECO:0000305}.
HELIX 43 48 {ECO:0000244|PDB:4FFV}.
STRAND 58 60 {ECO:0000244|PDB:2GBF}.
STRAND 62 72 {ECO:0000244|PDB:4FFV}.
STRAND 74 82 {ECO:0000244|PDB:4FFV}.
STRAND 84 88 {ECO:0000244|PDB:4FFV}.
HELIX 90 93 {ECO:0000244|PDB:4FFV}.
HELIX 97 99 {ECO:0000244|PDB:4FFW}.
STRAND 100 105 {ECO:0000244|PDB:4FFV}.
STRAND 109 120 {ECO:0000244|PDB:4FFV}.
STRAND 122 124 {ECO:0000244|PDB:4FFV}.
STRAND 126 134 {ECO:0000244|PDB:4FFV}.
TURN 135 138 {ECO:0000244|PDB:4FFV}.
STRAND 139 141 {ECO:0000244|PDB:2I3Z}.
STRAND 148 150 {ECO:0000244|PDB:4FFV}.
STRAND 152 155 {ECO:0000244|PDB:4FFV}.
STRAND 157 160 {ECO:0000244|PDB:4FFV}.
STRAND 162 166 {ECO:0000244|PDB:4FFV}.
STRAND 169 175 {ECO:0000244|PDB:4FFV}.
TURN 189 191 {ECO:0000244|PDB:4FFV}.
STRAND 192 196 {ECO:0000244|PDB:4FFV}.
HELIX 199 204 {ECO:0000244|PDB:4FFV}.
STRAND 207 210 {ECO:0000244|PDB:4FFV}.
STRAND 212 214 {ECO:0000244|PDB:4FFV}.
STRAND 216 227 {ECO:0000244|PDB:4FFV}.
STRAND 233 238 {ECO:0000244|PDB:4FFV}.
STRAND 248 253 {ECO:0000244|PDB:4FFV}.
STRAND 263 271 {ECO:0000244|PDB:4FFV}.
HELIX 273 276 {ECO:0000244|PDB:2I3Z}.
STRAND 283 285 {ECO:0000244|PDB:2GBC}.
TURN 289 293 {ECO:0000244|PDB:4FFV}.
STRAND 296 305 {ECO:0000244|PDB:4FFV}.
STRAND 308 329 {ECO:0000244|PDB:4FFV}.
TURN 330 333 {ECO:0000244|PDB:4FFV}.
STRAND 334 336 {ECO:0000244|PDB:4FFV}.
HELIX 339 341 {ECO:0000244|PDB:4FFV}.
STRAND 342 346 {ECO:0000244|PDB:4FFV}.
STRAND 348 350 {ECO:0000244|PDB:4FFV}.
STRAND 352 356 {ECO:0000244|PDB:4FFV}.
STRAND 366 374 {ECO:0000244|PDB:4FFV}.
STRAND 376 378 {ECO:0000244|PDB:4FFW}.
STRAND 380 388 {ECO:0000244|PDB:4FFV}.
TURN 391 393 {ECO:0000244|PDB:2I3Z}.
STRAND 396 398 {ECO:0000244|PDB:4FFV}.
STRAND 401 403 {ECO:0000244|PDB:4FFV}.
STRAND 405 411 {ECO:0000244|PDB:4FFV}.
STRAND 413 421 {ECO:0000244|PDB:4FFV}.
HELIX 423 425 {ECO:0000244|PDB:4FFV}.
STRAND 430 438 {ECO:0000244|PDB:4FFV}.
STRAND 443 450 {ECO:0000244|PDB:4FFV}.
TURN 452 454 {ECO:0000244|PDB:4FFV}.
STRAND 455 462 {ECO:0000244|PDB:4FFV}.
STRAND 466 473 {ECO:0000244|PDB:4FFV}.
STRAND 475 478 {ECO:0000244|PDB:4FFV}.
STRAND 480 488 {ECO:0000244|PDB:4FFV}.
STRAND 491 496 {ECO:0000244|PDB:4FFV}.
HELIX 499 504 {ECO:0000244|PDB:4FFV}.
HELIX 505 507 {ECO:0000244|PDB:4FFV}.
STRAND 512 520 {ECO:0000244|PDB:4FFV}.
STRAND 523 531 {ECO:0000244|PDB:4FFV}.
STRAND 541 547 {ECO:0000244|PDB:4FFV}.
HELIX 564 570 {ECO:0000244|PDB:4FFV}.
STRAND 575 579 {ECO:0000244|PDB:4FFV}.
STRAND 585 587 {ECO:0000244|PDB:4FFV}.
HELIX 589 592 {ECO:0000244|PDB:4FFV}.
HELIX 593 595 {ECO:0000244|PDB:4FFV}.
TURN 599 601 {ECO:0000244|PDB:4FFV}.
HELIX 602 616 {ECO:0000244|PDB:4FFV}.
STRAND 620 630 {ECO:0000244|PDB:4FFV}.
HELIX 632 641 {ECO:0000244|PDB:4FFV}.
TURN 642 644 {ECO:0000244|PDB:4FFV}.
STRAND 649 655 {ECO:0000244|PDB:4FFV}.
HELIX 660 662 {ECO:0000244|PDB:4FFV}.
HELIX 665 672 {ECO:0000244|PDB:4FFV}.
TURN 677 680 {ECO:0000244|PDB:4FFV}.
HELIX 681 686 {ECO:0000244|PDB:4FFV}.
HELIX 690 698 {ECO:0000244|PDB:4FFV}.
STRAND 699 706 {ECO:0000244|PDB:4FFV}.
STRAND 710 712 {ECO:0000244|PDB:4FFV}.
HELIX 714 726 {ECO:0000244|PDB:4FFV}.
STRAND 732 736 {ECO:0000244|PDB:4FFV}.
HELIX 746 764 {ECO:0000244|PDB:4FFV}.
SEQUENCE 767 AA; 88089 MW; ED947174F1F3E440 CRC64;
MKTPWKVLLG LLGVAALVTI ITVPVVLLNK DEAAADSRRT YTLADYLKNT FRVKSYSLRW
VSDSEYLYKQ ENNILLFNAE HGNSSIFLEN STFEIFGDSI SDYSVSPDRL FVLLEYNYVK
QWRHSYTASY SIYDLNKRQL ITEEKIPNNT QWITWSQEGH KLAYVWKNDI YVKIEPHLPS
HRITSTGKEN VIFNGINDWV YEEEIFGAYS ALWWSPNGTF LAYAQFNDTG VPLIEYSFYS
DESLQYPKTV WIPYPKAGAV NPTVKFFIVN TDSLSSTTTT IPMQITAPAS VTTGDHYLCD
VAWVSEDRIS LQWLRRIQNY SVMAICDYDK TTLVWNCPTT QEHIETSATG WCGRFRPAEP
HFTSDGSSFY KIVSDKDGYK HICQFQKDRK PEQVCTFITK GAWEVISIEA LTSDYLYYIS
NEYKEMPGGR NLYKIQLTDH TNKKCLSCDL NPERCQYYSV SLSKEAKYYQ LGCRGPGLPL
YTLHRSTDQK ELRVLEDNSA LDKMLQDVQM PSKKLDFIVL NETRFWYQMI LPPHFDKSKK
YPLLIDVYAG PCSQKADAAF RLNWATYLAS TENIIVASFD GRGSGYQGDK IMHAINKRLG
TLEVEDQIEA ARQFLKMGFV DSKRVAIWGW SYGGYVTSMV LGSGSGVFKC GIAVAPVSRW
EYYDSVYTER YMGLPTPEDN LDHYRNSTVM SRAENFKQVE YLLIHGTADD NVHFQQSAQI
SKALVDAGVD FQAMWYTDED HGIASSTAHQ HIYSHMSHFL QQCFSLR


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Catalog number Product name Quantity
E0884r ELISA Bile canaliculus domain-specific membrane glycoprotein,Cd26,Dipeptidyl peptidase 4,Dipeptidyl peptidase IV,DPP IV,Dpp4,GP110 glycoprotein,Rat,Rattus norvegicus,T-cell activation antigen CD26 96T
U0884r CLIA Bile canaliculus domain-specific membrane glycoprotein,Cd26,Dipeptidyl peptidase 4,Dipeptidyl peptidase IV,DPP IV,Dpp4,GP110 glycoprotein,Rat,Rattus norvegicus,T-cell activation antigen CD26 96T
E0884r ELISA kit Bile canaliculus domain-specific membrane glycoprotein,Cd26,Dipeptidyl peptidase 4,Dipeptidyl peptidase IV,DPP IV,Dpp4,GP110 glycoprotein,Rat,Rattus norvegicus,T-cell activation antigen CD2 96T
20-321-175240 DIPEPTIDYL PEPTIDASE IV (DPP IV). CD26 - MONOCLONAL ANTIBODY TO RAT DIPEPTIDYL PEPTIDASE IV (DPP IV). CD26; EC 3.4.14.5; Dipeptidyl peptidase IV; DPP IV; T-cell activation antigen CD26; TP103; Adenosi 0.1 mg
EIAAB11842 Dipeptidyl aminopeptidase II,Dipeptidyl peptidase 2,Dipeptidyl peptidase 7,Dipeptidyl peptidase II,DPP II,DPP2,DPP7,Homo sapiens,Human,QPP,Quiescent cell proline dipeptidase
EIAAB11844 Dipeptidyl aminopeptidase II,Dipeptidyl peptidase 2,Dipeptidyl peptidase 7,Dipeptidyl peptidase II,DPP II,Dpp2,Dpp7,Mouse,Mus musculus,Qpp,Quiescent cell proline dipeptidase
EIAAB11843 Dipeptidyl aminopeptidase II,Dipeptidyl peptidase 2,Dipeptidyl peptidase 7,Dipeptidyl peptidase II,DPP II,Dpp2,Dpp7,Quiescent cell proline dipeptidase,Rat,Rattus norvegicus
EIAAB11839 Dipeptidyl peptidase IV-related protein 3,Dipeptidyl peptidase X,Dipeptidyl peptidase-like protein 2,DPL2,DPP X,DPP10,DPRP3,DPRP-3,Homo sapiens,Human,Inactive dipeptidyl peptidase 10,KIAA1492
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
E0884m ELISA kit Cd26,Dipeptidyl peptidase 4,Dipeptidyl peptidase IV,DPP IV,Dpp4,Mouse,Mus musculus,T-cell activation antigen CD26,THAM,Thymocyte-activating molecule 96T
E0884m ELISA Cd26,Dipeptidyl peptidase 4,Dipeptidyl peptidase IV,DPP IV,Dpp4,Mouse,Mus musculus,T-cell activation antigen CD26,THAM,Thymocyte-activating molecule 96T
U0884m CLIA Cd26,Dipeptidyl peptidase 4,Dipeptidyl peptidase IV,DPP IV,Dpp4,Mouse,Mus musculus,T-cell activation antigen CD26,THAM,Thymocyte-activating molecule 96T
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
E0884p ELISA kit CD26,Dipeptidyl peptidase 4,Dipeptidyl peptidase IV,DPP IV,DPP4,Pig,Sus scrofa,T-cell activation antigen CD26 96T
U0884p CLIA CD26,Dipeptidyl peptidase 4,Dipeptidyl peptidase IV,DPP IV,DPP4,Pig,Sus scrofa,T-cell activation antigen CD26 96T
E0884p ELISA CD26,Dipeptidyl peptidase 4,Dipeptidyl peptidase IV,DPP IV,DPP4,Pig,Sus scrofa,T-cell activation antigen CD26 96T
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 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
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
EIAAB11845 Dipeptidyl aminopeptidase III,Dipeptidyl arylamidase III,Dipeptidyl peptidase 3,Dipeptidyl peptidase III,DPP III,DPP3,Homo sapiens,Human
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
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
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
EIAAB11855 Dipeptidyl peptidase 9,Dipeptidyl peptidase IX,Dipeptidyl peptidase-like protein 9,DP9,DPLP9,DPP IX,Dpp9,Mouse,Mus musculus


 

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