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QPCT recombinant protein :: Glutaminyl-peptide cyclotransferase Recombinant Protein

Scan QR to view Datasheet Catalog #    MBS1485028
SDS-Page
Unit / Price
0.05 mg (E-Coli)  /  $740 +1 FREE 8GB USB
0.05 mg (Yeast)  /  $860 +1 FREE 8GB USB
0.2 mg (E-Coli)  /  $990 +1 FREE 8GB USB
0.05 mg (Baculovirus)  /  $995 +1 FREE 8GB USB
0.5 mg (E-Coli)  /  $1,095 +1 FREE 8GB USB
0.2 mg (Yeast)  /  $1,160 +1 FREE 8GB USB
0.05 mg (Mammalian-Cell)  /  $1,245 +1 FREE 8GB USB
0.1 mg (Baculovirus)  /  $1,265 +1 FREE 8GB USB
0.5 mg (Yeast)  /  $1,310 +1 FREE 8GB USB
1 mg (E-Coli)  /  $1,550 +1 FREE 8GB USB
0.5 mg (Baculovirus)  /  $1,820 +2 FREE 8GB USB
0.1 mg (Mammalian-Cell)  /  $1,885 +2 FREE 8GB USB
1 mg (Yeast)  /  $1,990 +2 FREE 8GB USB
1 mg (Baculovirus)  /  $2,420 +3 FREE 8GB USB
 
 Go to:   rightarrow  Product Names   rightarrow Product Info   rightarrow Accession #s   rightarrow Product Desc   rightarrow Diseases/Tissues/Pathways   rightarrow Applications   rightarrow References 
 Product Name   

Glutaminyl-peptide cyclotransferase (QPCT), Recombinant Protein

★Popular Item★
 Also Known As   

Recombinant Human Glutaminyl-peptide cyclotransferase

 Product Synonym Names    Glutaminyl cyclase; QC; sQC; Glutaminyl-tRNA cyclotransferase; Glutamyl cyclase; EC
 Product Gene Name   

QPCT recombinant protein

[Similar Products]
 Research Use Only    For Research Use Only. Not for use in diagnostic procedures.
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 MBS1485028 COA    COA PDF
 Sequence Positions    29-361aa; Full Length
 Sequence    VSPSASAWPE EKNYHQPAIL NSSALRQIAE GTSISEMWQN DLQPLLIERY PGSPGSYAAR QHIMQRIQRL QADWVLEIDT FLSQTPYGYR SFSNIISTLN PTAKRHLVLA CHYDSKYFSH WNNRVFVGAT DSAVPCAMML ELARALDKKL LSLKTVSDSK PDLSLQLIFF DGEEAFLHWS PQDSLYGSRH LAAKMASTPH PPGARGTSQL HGMDLLVLLD LIGAPNPTFP NFFPNSARWF ERLQAIEHEL HELGLLKDHS LEGRYFQNYS YGGVIQDDHI PFLRRGVPVL HLIPSPFPEV WHTMDDNEEN LDESTIDNLN KILQVFVLEY LHL
 OMIM    607065
 3D Structure    ModBase 3D Structure for Q16769
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 Host    E Coli or Yeast or Baculovirus or Mammalian Cell
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 Purity/Purification    Greater than 90% as determined by SDS-PAGE. (lot specific)
 Form/Format    Liquid containing glycerol
 Tag Information    This protein contains an N-terminal tag and may also contain a C-terminal tag. Tag types are determined by various factors including tag-protein stability, please inquire for tag information.
 Sterility    Sterile filter available upon request.
 Endotoxin    Low endotoxin available upon request.
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 Production Note    Special Offer: The E. coli host-expressed protein is manufactured from a stock plasmid containing the protein gene. E. coli host-expressed protein is stocked in different unit sizes ranging from as small as 10 ug to as large as 1 mg. Bulk inventory is also available. The E. coli host-expressed protein has been ordered over and over again by researchers and has stood the test of time as both a robust protein and important target for the research community. It is part of our new program to make our most popular protein targets and corresponding hosts available in expanded unit sizes and with a quick processing time. Select E. coli host-expressed protein for the fastest delivery among all hosts. Please contact us or email to support@mybiosource.com for more details.
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 Preparation and Storage    Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
 ISO Certification    Manufactured in an ISO 9001:2008 Certified Laboratory.
 Other Notes    Small volumes of QPCT recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.
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Related Product Information for QPCT recombinant protein

   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.
 Product Categories/Family for QPCT recombinant protein    Neuroscience
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 SDS-Page of QPCT recombinant protein    QPCT recombinant protein SDS-Page image
(Note: Representative image, actual molecular weight may vary depending on Tag type and expression host)
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NCBI/Uniprot data below describe general gene information for QPCT. It may not necessarily be applicable to this product.
 NCBI GI #    6912618
 NCBI GeneID    25797
 NCBI Accession #    NP_036545.1 [Other Products]
 NCBI GenBank Nucleotide #    NM_012413.3 [Other Products]
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 UniProt Primary Accession #    Q16769 [Other Products]
 UniProt Secondary Accession #    Q16770; Q3KRG6; Q53TR4 [Other Products]
 UniProt Related Accession #    Q16769 [Other Products]
 Molecular Weight    53.9kD
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 NCBI Official Full Name    glutaminyl-peptide cyclotransferase
 NCBI Official Synonym Full Names    glutaminyl-peptide cyclotransferase
 NCBI Official Symbol    QPCT [Similar Products]
 NCBI Official Synonym Symbols   
QC; GCT; sQC
[Similar Products]
 NCBI Protein Information    glutaminyl-peptide cyclotransferase
 UniProt Protein Name    Glutaminyl-peptide cyclotransferase
 UniProt Synonym Protein Names   
Glutaminyl cyclase; QC; sQC; Glutaminyl-tRNA cyclotransferase; Glutamyl cyclase; EC
 Protein Family    Glutaminyl-peptide cyclotransferase
 UniProt Gene Name    QPCT [Similar Products]
 UniProt Synonym Gene Names    QC; sQC; EC [Similar Products]
 UniProt Entry Name    QPCT_HUMAN
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 NCBI Summary for QPCT    This gene encodes human pituitary glutaminyl cyclase, which is responsible for the presence of pyroglutamyl residues in many neuroendocrine peptides. The amino acid sequence of this enzyme is 86% identical to that of bovine glutaminyl cyclase. [provided by RefSeq, Jul 2008]
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 UniProt Comments for QPCT    QPCT: 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. Belongs to the glutaminyl-peptide cyclotransferase family. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: EC 2.3.2.5; Secreted, signal peptide; Secreted; Transferase

Chromosomal Location of Human Ortholog: 2p22.2

Molecular Function: glutaminyl-peptide cyclotransferase activity; zinc ion binding

Biological Process: peptidyl-pyroglutamic acid biosynthetic process, using glutaminyl-peptide cyclotransferase; protein modification process
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Product References and Citations for QPCT recombinant protein

   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) 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., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.Nat. Genet. 36:40-45(2004) 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., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.Nature 434:724-731(2005) Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. 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) 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) 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) 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) 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.Biochemistry 50:6280-6288(2011) 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)
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 Research Articles on QPCT    1. observations provide evidence for an involvement of QC in Alzheimer's disease pathogenesis and cognitive decline by QC-catalyzed pGlu-Abeta formation
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 Precautions    All of MyBioSource's Products are for scientific laboratory research purposes and are not for diagnostic, therapeutics, prophylactic or in vivo use. Through your purchase, you expressly represent and warrant to MyBioSource that you will properly test and use any Products purchased from MyBioSource in accordance with industry standards. MyBioSource and its authorized distributors reserve the right to refuse to process any order where we reasonably believe that the intended use will fall outside of our acceptable guidelines.
 Disclaimer    While every efforts were made to ensure the accuracy of the information provided in this datasheet, MyBioSource will not be liable for any omissions or errors contained herein. MyBioSource reserves the right to make changes to this datasheet at any time without prior notice.

It is the responsibility of the customer to report product performance issues to MyBioSource within 30 days of receipt of the product. Please visit our Terms & Conditions page for more information.
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Diseases associated with QPCT recombinant protein
 Disease Name  Pubmed Publications
 Brain Diseases Antibodies  >2 publications with QPCT and Brain Diseases
 Inflammation Antibodies  >2 publications with QPCT and Inflammation
 Hypertension Antibodies  >1 publications with QPCT and Hypertension
 Kidney Diseases Antibodies  >1 publications with QPCT and Kidney Diseases
 Disease Models, Animal Antibodies  >1 publications with QPCT and Disease Models, Animal
 Fibrosis Antibodies  >1 publications with QPCT and Fibrosis
 Cognition Disorders Antibodies  >1 publications with QPCT and Cognition Disorders
 Neoplasms, Experimental Antibodies  >1 publications with QPCT and Neoplasms, Experimental
 Hyperplasia Antibodies  >1 publications with QPCT and Hyperplasia
 Melanoma Antibodies  >1 publications with QPCT and Melanoma
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