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Index > Protein center > Dpp4(Gene name) > Rat
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  • Dpp4 (Gene name),
  • Dipeptidyl peptidase 4 (Protein name ),  DPP4_RAT from NCBI database.
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  • General Annotation
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  • Antigen Annotation
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  • Predicted Eptitope
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  • Gene name:
    Dpp4(Cd26);
    Protein name:
    Dipeptidyl peptidase 4;
    Alternative:
    Dipeptidyl peptidase IV(DPP IV);Bile canaliculus domain-specific membrane glycoprotein;T-cell activation antigen CD26;GP110 glycoprotein;
    CD:
    CD26;
    Organism:
    Rat (Rattus norvegicus). 
    General Annotation
    Sub Unit:
    Monomer. 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 (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 (By similarity). Homodimer.
    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.
    Subcellular Location:
    Cell membrane Single-pass type II membrane protein Apical cell membrane Single-pass type II membrane protein Cell projection invadopodium membrane Single-pass type II membrane protein Cell projection lamellipodium membrane Single-pass type II membrane protein Cell junction Membrane raft 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.
    Protein Attributes:
    Sequence length:
    767
    Sequence:
    50:
    MKTPWKVLLG | LLGVAALVTI | ITVPVVLLNK | DEAAADSRRT | YTLADYLKNT | 
    100:
    FRVKSYSLRW | VSDSEYLYKQ | ENNILLFNAE | HGNSSIFLEN | STFEIFGDSI | 
    150:
    SDYSVSPDRL | FVLLEYNYVK | QWRHSYTASY | SIYDLNKRQL | ITEEKIPNNT | 
    200:
    QWITWSQEGH | KLAYVWKNDI | YVKIEPHLPS | HRITSTGKEN | VIFNGINDWV | 
    250:
    YEEEIFGAYS | ALWWSPNGTF | LAYAQFNDTG | VPLIEYSFYS | DESLQYPKTV | 
    300:
    WIPYPKAGAV | NPTVKFFIVN | TDSLSSTTTT | IPMQITAPAS | VTTGDHYLCD | 
    350:
    VAWVSEDRIS | LQWLRRIQNY | SVMAICDYDK | TTLVWNCPTT | QEHIETSATG | 
    400:
    WCGRFRPAEP | HFTSDGSSFY | KIVSDKDGYK | HICQFQKDRK | PEQVCTFITK | 
    450:
    GAWEVISIEA | LTSDYLYYIS | NEYKEMPGGR | NLYKIQLTDH | TNKKCLSCDL | 
    500:
    NPERCQYYSV | SLSKEAKYYQ | LGCRGPGLPL | YTLHRSTDQK | ELRVLEDNSA | 
    550:
    LDKMLQDVQM | PSKKLDFIVL | NETRFWYQMI | LPPHFDKSKK | YPLLIDVYAG | 
    600:
    PCSQKADAAF | RLNWATYLAS | TENIIVASFD | GRGSGYQGDK | IMHAINKRLG | 
    650:
    TLEVEDQIEA | ARQFLKMGFV | DSKRVAIWGW | SYGGYVTSMV | LGSGSGVFKC | 
    700:
    GIAVAPVSRW | EYYDSVYTER | YMGLPTPEDN | LDHYRNSTVM | SRAENFKQVE | 
    750:
    YLLIHGTADD | NVHFQQSAQI | SKALVDAGVD | FQAMWYTDED | HGIASSTAHQ | 
    767:
    HIYSHMSHFL | QQCFSLR
    3D Structure:
    N/A
    Predicted Eptitope:
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    EIAab Sequence  Vaild Sequence:
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    Related Databases
    String:
    Pfam:
    SMR:
    KEGG:
    UniGene:
    Uniprot:
     
    FOR
    ELISA Kit for Rat Dipeptidyl peptidase 4
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    E0884h
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    ELISA Kit for Rat Dipeptidyl peptidase 4
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    E0884m
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    ELISA Kit for Rat Dipeptidyl peptidase 4
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    E0884r
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    ELISA Kit for Rat Dipeptidyl peptidase 4
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    E0884p
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    ELISA Kit for Rat Dipeptidyl peptidase 4
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    E0884b
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    96T
    CLIA Kit for Rat Dipeptidyl peptidase 4
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    U0884m
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    Packing:
    96T
    Range:
    Please sign in first.
    CLIA Kit for Rat Dipeptidyl peptidase 4
    Cat.:
    U0884b
    Price:
    Please sign in first.
    MSDS:
    Please sign in first.
    Packing:
    96T
    CLIA Kit for Rat Dipeptidyl peptidase 4
    Cat.:
    U0884h
    Price:
    Please sign in first.
    MSDS:
    Please sign in first.
    Packing:
    96T
    CLIA Kit for Rat Dipeptidyl peptidase 4
    Cat.:
    U0884p
    Price:
    Please sign in first.
    MSDS:
    Please sign in first.
    Packing:
    96T
    CLIA Kit for Rat Dipeptidyl peptidase 4
    Cat.:
    U0884r
    Price:
    Please sign in first.
    MSDS:
    Please sign in first.
    Packing:
    96T
    Polyclonal Antibody for Rat Dipeptidyl peptidase 4
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    P0884Rb-m
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    Packing:
    40ug/0.2ml
    Polyclonal Antibody for Rat Dipeptidyl peptidase 4
    Cat.:
    P0884Rb-h
    Price:
    Please sign in first.
    Packing:
    40ug/0.2ml
    Polyclonal Antibody for Rat Dipeptidyl peptidase 4
    Polyclonal Antibody for Rat Dipeptidyl peptidase 4
    Cat.:
    P0884Rb-r
    Price:
    Please sign in first.
    Packing:
    40ug/0.2ml
    Polyclonal Antibody for Rat Dipeptidyl peptidase 4
    Monoclonal Antibody for Rat Dipeptidyl peptidase 4
    Monoclonal Antibody for Rat Dipeptidyl peptidase 4
    Monoclonal Antibody for Rat Dipeptidyl peptidase 4
    Monoclonal Antibody for Rat Dipeptidyl peptidase 4
    Monoclonal Antibody for Rat Dipeptidyl peptidase 4
    Protein for Rat Dipeptidyl peptidase 4
    Protein for Rat Dipeptidyl peptidase 4
    Protein for Rat Dipeptidyl peptidase 4
    Protein for Rat Dipeptidyl peptidase 4
    Protein for Rat Dipeptidyl peptidase 4

    R&D Technical Data
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    Precision
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    Linearity
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    References
    1. 1.
      "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."
      Ogata S. , Misumi Y. , Ikehara Y.
      J. Biol. Chem.264:3596-3601(1989) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA];PARTIAL PROTEIN SEQUENCE
    2. 2.
      "cDNA cloning for a bile canaliculus domain-specific membrane glycoprotein of rat hepatocytes."
      Hong W. , Doyle D.
      Proc. Natl. Acad. Sci. U.S.A.84:7962-7966(1987) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA]
    3. 3.
      "Membrane orientation of rat gp110 as studied by in vitro translation."
      Hong W.J. , Doyle D.
      J. Biol. Chem.263:16892-16898(1988) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-40
    4. 4.
      "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."
      McCaughan G.W. , Wickson J.E. , Creswick P.F. , Gorrell M.D.
      Hepatology11:534-544(1990) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: PROTEIN SEQUENCE OF 28-58;TISSUE SPECIFICITY
    5. 5.
      "N-terminal amino acid sequence of the 60-kDa protein of rat kidney dipeptidyl peptidase IV."
      Iwaki-Egawa S. , Watanabe Y. , Fujimoto Y.
      Biol. Chem. Hoppe-Seyler374:973-975(1993) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: PROTEIN SEQUENCE OF 281-302;MUTAGENESIS OF GLY-629; TRP-630; SER-631; TRY-632 AND GLY-633
      tissue: Kidney.
    6. 6.
      "Identification of the active site residues in dipeptidyl peptidase IV by affinity labeling and site-directed mutagenesis."
      Ogata S. , Misumi Y. , Tsuji E. , Takami N. , Oda K. , Ikehara Y.
      Biochemistry31:2582-2587(1992) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: PROTEIN SEQUENCE OF 624-648
    7. 7.
      "Molecular dissection of the NH2-terminal signal/anchor sequence of rat dipeptidyl peptidase IV."
      Hong W. , Doyle D.
      J. Cell Biol.111:323-328(1990) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: SIGNAL-ANCHOR
    8. 8.
      "Crystal structures of DPP-IV (CD26) from rat kidney exhibit flexible accommodation of peptidase-selective inhibitors."
      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.
      Biochemistry45:7474-7482(2006) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: 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;DISULFIDE BONDS
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