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Index > Protein center > QPCT(Gene name) > Human
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  • QPCT (Gene name),
  • Glutaminyl-peptide cyclotransferase (Protein name ),  QPCT_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:
    QPCT;
    Protein name:
    Glutaminyl-peptide cyclotransferase;
    Alternative:
    Glutaminyl-tRNA cyclotransferase;Glutaminyl cyclase(QC;sQC);Glutamyl cyclase(EC);
    Organism:
    Human (Homo sapiens). 
    General Annotation
    Sub Unit:
    N/A
    Function:
    Responsible for the biosynthesis of pyroglutamyl peptides. Has a bias against acidic and tryptophan residues adjacent to the N-terminal glutaminyl residue and a lack of importance of chain length after the second residue. Also catalyzes N-terminal pyroglutamate formation. In vitro, catalyzes pyroglutamate formation of N-terminally truncated form of APP amyloid-beta peptides [Glu-3]-beta-amyloid. May be involved in the N-terminal pyroglutamate formation of several amyloid-related plaque-forming peptides.
    Subcellular Location:
    Secreted
    Protein Attributes:
    Sequence length:
    361
    Sequence:
    50:
    MAGGRHRRVV | GTLHLLLLVA | ALPWASRGVS | PSASAWPEEK | NYHQPAILNS | 
    100:
    SALRQIAEGT | SISEMWQNDL | QPLLIERYPG | SPGSYAARQH | IMQRIQRLQA | 
    150:
    DWVLEIDTFL | SQTPYGYRSF | SNIISTLNPT | AKRHLVLACH | YDSKYFSHWN | 
    200:
    NRVFVGATDS | AVPCAMMLEL | ARALDKKLLS | LKTVSDSKPD | LSLQLIFFDG | 
    250:
    EEAFLHWSPQ | DSLYGSRHLA | AKMASTPHPP | GARGTSQLHG | MDLLVLLDLI | 
    300:
    GAPNPTFPNF | FPNSARWFER | LQAIEHELHE | LGLLKDHSLE | GRYFQNYSYG | 
    350:
    GVIQDDHIPF | LRRGVPVLHL | IPSPFPEVWH | TMDDNEENLD | ESTIDNLNKI | 
    361:
    LQVFVLEYLH | L
    3D Structure:
    N/A
    Predicted Eptitope:
    Please Sign in.
    EIAab Sequence  Vaild Sequence:
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    Related Databases
    UniGene:
    SMR:
    KEGG:
    String:
    MIM:
    Pfam:
    Uniprot:
     
    FOR
    ELISA Kit for Human Glutaminyl-peptide cyclotransferase
    Cat.:
    E2087m
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    MSDS:
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    Packing:
    96T
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    ELISA Kit for Human Glutaminyl-peptide cyclotransferase
    Cat.:
    E2087b
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    MSDS:
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    Packing:
    96T
    ELISA Kit for Human Glutaminyl-peptide cyclotransferase
    Cat.:
    E2087h
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    MSDS:
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    Packing:
    96T
    Range:
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    CLIA Kit for Human Glutaminyl-peptide cyclotransferase
    Cat.:
    U2087h
    Price:
    Please sign in first.
    MSDS:
    Please sign in first.
    Packing:
    96T
    Range:
    Please sign in first.
    CLIA Kit for Human Glutaminyl-peptide cyclotransferase
    Cat.:
    U2087m
    Price:
    Please sign in first.
    MSDS:
    Please sign in first.
    Packing:
    96T
    CLIA Kit for Human Glutaminyl-peptide cyclotransferase
    Cat.:
    U2087b
    Price:
    Please sign in first.
    MSDS:
    Please sign in first.
    Packing:
    96T
    Polyclonal Antibody for Human Glutaminyl-peptide cyclotransferase
    Cat.:
    P2087Rb-m
    Price:
    Please sign in first.
    Packing:
    40ug/0.2ml
    Polyclonal Antibody for Human Glutaminyl-peptide cyclotransferase
    Cat.:
    P2087Rb-h
    Price:
    Please sign in first.
    Packing:
    40ug/0.2ml
    Polyclonal Antibody for Human Glutaminyl-peptide cyclotransferase
    Monoclonal Antibody for Human Glutaminyl-peptide cyclotransferase
    Monoclonal Antibody for Human Glutaminyl-peptide cyclotransferase
    Monoclonal Antibody for Human Glutaminyl-peptide cyclotransferase
    Protein for Human Glutaminyl-peptide cyclotransferase
    Protein for Human Glutaminyl-peptide cyclotransferase
    Protein for Human Glutaminyl-peptide cyclotransferase

    R&D Technical Data
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    Precision
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    Recovery
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    Linearity
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    References
    1. 1.
      "Molecular cloning, sequence analysis and expression of human pituitary glutaminyl cyclase."
      Song I. , Chuang C.Z. , Bateman R.C. Jr.
      J. Mol. Endocrinol.13:77-86(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] (ISOFORM 1)
      tissue: Pituitary.
    2. 2.
      "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T. , Suzuki Y. , Nishikawa T. , Otsuki T. , Sugiyama T. , Irie R. , Wakamatsu A. , Hayashi K. , Sato H. , Nagai K. , Kimura K. , Makita H. , Sekine M. , Obayashi M. , Nishi T. , Shibahara T. , Tanaka T. , Ishii S. , more...
      Nat. Genet.36:40-45(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] (ISOFORM 1)
      tissue: Heart.
    3. 3.
      "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W. , Graves T.A. , Fulton R.S. , Fulton L.A. , Pepin K.H. , Minx P. , Wagner-McPherson C. , Layman D. , Wylie K. , Sekhon M. , Becker M.C. , Fewell G.A. , Delehaunty K.D. , Miner T.L. , Nash W.E. , Kremitzki C. , Oddy L. , Du H. , more...
      Nature434:724-731(2005) [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 GENOMIC DNA]
    4. 4.
      [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]
    5. 5.
      "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] (ISOFORM 1);VARIANT PRO-360
      tissue: Lung.
      tissue: Pancreas.
    6. 6.
      "Glutaminyl cyclases unfold glutamyl cyclase activity under mild acid conditions."
      Schilling S. , Hoffmann T. , Manhart S. , Hoffmann M. , Demuth H.U.
      FEBS Lett.563:191-196(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: FUNCTION AS GLUTAMYL CYCLASE
    7. 7.
      "Isolation of an isoenzyme of human glutaminyl cyclase: retention in the Golgi complex suggests involvement in the protein maturation machinery."
      Cynis H. , Rahfeld J.U. , Stephan A. , Kehlen A. , Koch B. , Wermann M. , Demuth H.U. , Schilling S.
      J. Mol. Biol.379:966-980(2008) [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: FUNCTION;CATALYTIC ACTIVITY;SUBCELLULAR LOCATION
    8. 8.
      "Crystal structures of human glutaminyl cyclase, an enzyme responsible for protein N-terminal pyroglutamate formation."
      Huang K.-F. , Liu Y.-L. , Cheng W.-J. , Ko T.-P. , Wang A.H.-J.
      Proc. Natl. Acad. Sci. U.S.A.102:13117-13122(2005) [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 (1.66 ANGSTROMS) OF 33-361;CATALYTIC ACTIVITY;MUTAGENESIS OF LYS-144; PHE-146; GLU-201; TRP-207; ASP-248; GLN-304; ASP-305; PHE-325 AND TRP-329;CHARACTERIZATION OF VARIANT TRP-54
    9. 9.
      "A conserved hydrogen-bond network in the catalytic centre of animal glutaminyl cyclases is critical for catalysis."
      Huang K.F. , Wang Y.R. , Chang E.C. , Chou T.L. , Wang A.H.
      Biochem. J.411:181-190(2008) [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 (1.66 ANGSTROMS) OF 33-361 OF MUTANTS ALA-160; GLY-160; ASP-201; LEU-201; GLN-201; ALA-248; GLN-248; ALA-305; GLU-305 AND LEU-319 IN COMPLEX WITH ZINC IONS;CATALYTIC ACTIVITY;COFACTOR;ACTIVE SITE;MUTAGENESIS OF SER-160; GLU-201; ASP-248; ASP-305 AND HIS-319
    10. 10.
      "Structures of glycosylated mammalian glutaminyl cyclases reveal conformational variability near the active center."
      Ruiz-Carrillo D. , Koch B. , Parthier C. , Wermann M. , Dambe T. , Buchholz M. , Ludwig H.H. , Heiser U. , Rahfeld J.U. , Stubbs M.T. , Schilling S. , Demuth H.U.
      Biochemistry50:6280-6288(2011) [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 (2.1 ANGSTROMS) OF 38-361;GLYCOSYLATION AT ASN-49;DISULFIDE BOND
    11. 11.
      "Structures of human Golgi-resident glutaminyl cyclase and its complexes with inhibitors reveal a large loop movement upon inhibitor binding."
      Huang K.F. , Liaw S.S. , Huang W.L. , Chia C.Y. , Lo Y.C. , Chen Y.L. , Wang A.H.
      J. Biol. Chem.286:12439-12449(2011) [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 (1.95 ANGSTROMS) OF 33-361 IN COMPLEX WITH ZINC IONS;CATALYTIC ACTIVITY;FUNCTION;COFACTOR
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