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Index > Protein center > DPEP1(Gene name) > Human
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  • DPEP1 (Gene name),
  • Dipeptidase 1 (Protein name ),  DPEP1_HUMAN 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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  • Vaild Sequence
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  • Gene name:
    DPEP1(MDP;RDP);
    Protein name:
    Dipeptidase 1;
    Alternative:
    Microsomal dipeptidase;Dehydropeptidase-I;Renal dipeptidase(hRDP);
    Organism:
    Human (Homo sapiens). 
    General Annotation
    Sub Unit:
    Homodimer; disulfide-linked.
    Function:
    Hydrolyzes a wide range of dipeptides. Implicated in the renal metabolism of glutathione and its conjugates. Converts leukotriene D4 to leukotriene E4; it may play an important role in the regulation of leukotriene activity.
    Subcellular Location:
    Apical cell membrane Lipid-anchor GPI-anchor Cell projection microvillus membrane Lipid-anchor GPI-anchor Brush border membrane.
    Protein Attributes:
    Sequence length:
    411
    Sequence:
    50:
    MWSGWWLWPL | VAVCTADFFR | DEAERIMRDS | PVIDGHNDLP | WQLLDMFNNR | 
    100:
    LQDERANLTT | LAGTHTNIPK | LRAGFVGGQF | WSVYTPCDTQ | NKDAVRRTLE | 
    150:
    QMDVVHRMCR | MYPETFLYVT | SSAGIRQAFR | EGKVASLIGV | EGGHSIDSSL | 
    200:
    GVLRALYQLG | MRYLTLTHSC | NTPWADNWLV | DTGDSEPQSQ | GLSPFGQRVV | 
    250:
    KELNRLGVLI | DLAHVSVATM | KATLQLSRAP | VIFSHSSAYS | VCASRRNVPD | 
    300:
    DVLRLVKQTD | SLVMVNFYNN | YISCTNKANL | SQVADHLDHI | KEVAGARAVG | 
    350:
    FGGDFDGVPR | VPEGLEDVSK | YPDLIAELLR | RNWTEAEVKG | ALADNLLRVF | 
    400:
    EAVEQASNLT | QAPEEEPIPL | DQLGGSCRTH | YGYSSGASSL | HRHWGLLLAS | 
    411:
    LAPLVLCLSL | L
    3D Structure:
    N/A
    Predicted Eptitope:
    Please Sign in.
    EIAab Sequence  Vaild Sequence:
    Please Sign in.
    Related Databases
    KEGG:
    SMR:
    MIM:
    UniGene:
    Pfam:
    String:
    Uniprot:
     
    FOR
    ELISA Kit for Human Dipeptidase 1
    Cat.:
    E9674h
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    MSDS:
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    Packing:
    96T
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    ELISA Kit for Human Dipeptidase 1
    Cat.:
    E9674m
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    MSDS:
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    Packing:
    96T
    ELISA Kit for Human Dipeptidase 1
    Cat.:
    E9674r
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    MSDS:
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    96T
    ELISA Kit for Human Dipeptidase 1
    Cat.:
    E9674b
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    MSDS:
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    Packing:
    96T
    ELISA Kit for Human Dipeptidase 1
    MSDS:
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    ELISA Kit for Human Dipeptidase 1
    Cat.:
    E9674p
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    Packing:
    96T
    CLIA Kit for Human Dipeptidase 1
    Cat.:
    U9674b
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    MSDS:
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    Packing:
    96T
    CLIA Kit for Human Dipeptidase 1
    Cat.:
    U9674m
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    MSDS:
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    Packing:
    96T
    CLIA Kit for Human Dipeptidase 1
    Cat.:
    U9674r
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    MSDS:
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    Packing:
    96T
    CLIA Kit for Human Dipeptidase 1
    Cat.:
    U9674p
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    MSDS:
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    Packing:
    96T
    CLIA Kit for Human Dipeptidase 1
    Cat.:
    U9674h
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    CLIA Kit for Human Dipeptidase 1
    MSDS:
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    Polyclonal Antibody for Human Dipeptidase 1
    Polyclonal Antibody for Human Dipeptidase 1
    Polyclonal Antibody for Human Dipeptidase 1
    Cat.:
    P9674Rb-h
    Price:
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    Packing:
    40ug/0.2ml
    Polyclonal Antibody for Human Dipeptidase 1
    Polyclonal Antibody for Human Dipeptidase 1
    Polyclonal Antibody for Human Dipeptidase 1
    Cat.:
    P9674Rb-m
    Price:
    Please sign in first.
    Packing:
    40ug/0.2ml
    Monoclonal Antibody for Human Dipeptidase 1
    Monoclonal Antibody for Human Dipeptidase 1
    Monoclonal Antibody for Human Dipeptidase 1
    Monoclonal Antibody for Human Dipeptidase 1
    Monoclonal Antibody for Human Dipeptidase 1
    Monoclonal Antibody for Human Dipeptidase 1
    Protein for Human Dipeptidase 1
    Protein for Human Dipeptidase 1
    Protein for Human Dipeptidase 1
    Protein for Human Dipeptidase 1
    Protein for Human Dipeptidase 1
    Protein for Human Dipeptidase 1

    R&D Technical Data

    s

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    s
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    Precision

    Intra-assay Precision (Precision within an assay):Three samples of known concentration were tested twenty times on one plate to assess intra-assay precision.

    Intra-Assay CV: ≤6.4%

    Inter-assay Precision (Precision between assays):Three samples of known concentration were tested in five separate assays to assess inter-assay precision.

    Inter-Assay CV: ≤9.7%

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    Intra-assay Precision (Precision within an assay):Three samples of known concentration were tested twenty times on one plate to assess intra-assay precision.

    Intra-Assay CV: ≤3.9%

    Inter-assay Precision (Precision between assays):Three samples of known concentration were tested in five separate assays to assess inter-assay precision.

    Inter-Assay CV: ≤7.7%

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    Recovery

    Recovery was determined by spiking various levels of DPEP1 into serum and plasma .

    Sample Type

    Average(%)

    Recovery Range(%)

    Serum

    100

    96-107

    Plasma

    99

    93-105

     

     

     

     

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    Recovery was determined by spiking various levels of ACE into serum and plasma .

    Sample Type

    Average(%)

    Recovery Range(%)

    Serum

    99

    91-103

    Plasma

    98

    93-106

     

     

     

     

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    Linearity

     

    The linearity of the kit was assayed by testing samples spiked with appropriate concentration of DPEP1 and their serial dilutions. The results were demonstrated by the percentage of calculated concentration to the expected.  

     

    Sample

    1:2

    1:4

    1:8

    1:16

    serum(n=5)

    94-105%

    93-107%

    95-107%

    92-109%

    EDTA plasma(n=5)

    91-107%

    93-105%

    92-106%

    95-105%

    heparin plasma(n=5)

    93-104%

     

    94-103%

    96-103%

    91-109%

     

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    The linearity of the kit was assayed by testing samples spiked with appropriate concentration of ACE and their serial dilutions. The results were demonstrated by the percentage of calculated concentration to the expected.  

     

    Sample

    1:2

    1:4

    1:8

    1:16

    serum(n=5)

    92-105%

    90-101%

    95-105%

    92-109%

    EDTA plasma(n=5)

    89-95%

    93105%

    89-94%

    90-106%

    heparin plasma(n=5)

    93-104%

     

    94-110%

    101-111%

    91-110%

     

    For more information, please refer to the manual,Or contact our technical support: tech@eiaab.com.
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    References
    1. 1.
      "Cloning and structural analysis of genomic DNA for human renal dipeptidase."
      Satoh S. , Kusunoki C. , Konta Y. , Niwa M. , Kohsaka M.
      Biochim. Biophys. Acta1172:181-183(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: NUCLEOTIDE SEQUENCE [GENOMIC DNA]
      tissue: Liver.
    2. 2.
      "Primary structure of human microsomal dipeptidase deduced from molecular cloning."
      Adachi H. , Tawaragi Y. , Inuzuka C. , Kubota I. , Tsujimoto M. , Nishihara T. , Nakazato H.
      J. Biol. Chem.265:3992-3995(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: NUCLEOTIDE SEQUENCE [MRNA]
    3. 3.
      "Gene structural analysis and expression of human renal dipeptidase."
      Satoh S. , Ohtsuka K. , Keida Y. , Kusunoki C. , Konta Y. , Niwa M. , Kohsaka M.
      Biotechnol. Prog.10:134-140(1994) [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]
      tissue: Kidney.
    4. 4.
      "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N. , Chen X. , Rolfs A. , Halleck A. , Hines L. , Eisenstein S. , Koundinya M. , Raphael J. , Moreira D. , Kelley T. , LaBaer J. , Lin Y. , Phelan M. , Farmer A.
      Submitted (2003-05) to the EMBL/GenBank/DDBJ databases
      [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 [LARGE SCALE MRNA]
    5. 5.
      [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 [LARGE SCALE GENOMIC DNA]
    6. 6.
      "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res.14:2121-2127(2004) [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 [LARGE SCALE MRNA]
      tissue: Colon.
    7. 7.
      "Characterization of the glycosyl-phosphatidylinositol-anchored human renal dipeptidase reveals that it is more extensively glycosylated than the pig enzyme."
      Hooper N.M. , Keen J.N. , Turner A.J.
      Biochem. J.265:429-433(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 17-56; 111-121 AND 298-310
    8. 8.
      "Purification and characterization of human microsomal dipeptidase."
      Adachi H. , Kubota I. , Okamura N. , Iwata H. , Tsujimoto M. , Nakazato H. , Nishihara T. , Noguchi T.
      J. Biochem.105:957-961(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: PROTEIN SEQUENCE OF 17-39
    9. 9.
      "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
      Zhang Z. , Henzel W.J.
      Protein Sci.13:2819-2824(2004) [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 17-31
    10. 10.
      "Identification of membrane anchoring site of human renal dipeptidase and construction and expression of a cDNA for its secretory form."
      Adachi H. , Katayama T. , Inuzuka C. , Oikawa S. , Tsujimoto M. , Nakazato H.
      J. Biol. Chem.265:15341-15345(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: GPI-ANCHOR AT SER-385
    11. 11.
      "Importance of Glu-125 in the catalytic activity of human renal dipeptidase."
      Adachi H. , Katayama T. , Nakazato H. , Tsujimoto M.
      Biochim. Biophys. Acta1163:42-48(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: INHIBITION BY CHEMICAL MODIFICATION
    12. 12.
      "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R. , Jiang X. , Sun D. , Han G. , Wang F. , Ye M. , Wang L. , Zou H.
      J. Proteome Res.8:651-661(2009) [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: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-57 AND ASN-279
      tissue: Liver.
    13. 13.
      "Crystal structure of human renal dipeptidase involved in beta-lactam hydrolysis."
      Nitanai Y. , Satow Y. , Adachi H. , Tsujimoto M.
      J. Mol. Biol.321:177-184(2002) [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 (2.00 ANGSTROMS) OF 17-385 IN COMPLEX WITH ZINC AND CILASTATIN;SUBUNIT;COFACTOR;DISULFIDE BONDS;GLYCOSYLATION AT ASN-57 AND ASN-332
    14. 14.
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-246
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