Glucokinase regulatory protein Recombinant Protein | GCKR recombinant protein

Recombinant Human Glucokinase regulatory protein

Cat. Num. AAA1285144

• Gene Names: GCKR; GKRP; FGQTL5
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Glucokinase regulatory protein; Recombinant Human Glucokinase regulatory protein; GCKR recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 1-625aa; Full Length
• Sequence: MPGTKRFQHVIETPEPGKWELSGYEAAVPITEKSNPLTQDLDKADAENIVRLLGQCDAEIFQEEGQALSTYQRLYSESILTTMVQVAGKVQEVLKEPDGGLVVLSGGGTSGRMAFLMSVSFNQLMKGLGQKPLYTYLIAGGDRSVVASREGTEDSALHGIEELKKVAAGKKRVIVIGISVGLSAPFVAGQMDCCMNNTAVFLPVLVGFNPVSMARNDPIEDWSSTFRQVAERMQKMQEKQKAFVLNPAIGPEGLSGSSRMKGGSATKILLETLLLAAHKTVDQGIAASQRCLLEILRTFERAHQVTYSQSPKIATLMKSVSTSLEKKGHVYLVGWQTLGIIAIMDGVECIHTFGADFRDVRGFLIGDHSDMFNQKAELTNQGPQFTFSQEDFLTSILPSLTEIDTVVFIFTLDDNLTEVQTIVEQVKEKTNHIQALAHSTVGQTLPIPLKKLFPSIISITWPLLFFEYEGNFIQKFQRELSTKWVLNTVSTGAHVLLGKILQNHMLDLRISNSKLFWRALAMLQRFSGQSKARCIESLLRAIHFPQPLSDDIRAAPISCHVQVAHEKEQVIPIALLSLLFRCSITEAQAHLAAAPSVCEAVRSALAGPGQKRTADPLEILEPDVQ
• Sequence Length: 625

• Production Note: Special Offer: The E Coli, Yeast host-expressed protein is manufactured from a stock plasmid containing the protein gene. E Coli, Yeasthost-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, Yeast 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, Yeast host-expressed protein for the fastest delivery among all hosts. Please contact our technical support team or email to [email protected] for more details.
• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-Page

Related Product Information for GCKR recombinant protein

Inhibits glucokinase (GCK) by forming an inactive complex with this enzyme. The affinity of GCKR for GCK is modulated by fructose metabolites: GCKR with bound fructose 6-phosphate has increased affinity for GCK, while GCKR with bound fructose 1-phosphate has strongly decreased affinity for GCK and does not inhibit GCK activity.

Product Categories/Family for GCKR recombinant protein

Signal Transduction

References

Human glucokinase regulatory protein (GCKR) cDNA and genomic cloning, complete primary structure, and chromosomal localization.Warner J.P., Leek J.P., Intody S., Markham A.F., Bonthron D.T.Mamm. Genome 6:532-536(1995) Organization of the human glucokinase regulator gene GCKR.Hayward B.E., Dunlop N., Intody S., Leek J.P., Markham A.F., Warner J.P., Bonthron D.T.Genomics 49:137-142(1998) NIEHS SNPs programComplete 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) Glucokinase regulatory protein is essential for the proper subcellular localisation of liver glucokinase.de la Iglesia N., Veiga-da-Cunha M., Van Schaftingen E., Guinovart J.J., Ferrer J.C.FEBS Lett. 456:332-338(1999) The common P446L polymorphism in GCKR inversely modulates fasting glucose and triglyceride levels and reduces type 2 diabetes risk in the DESIR prospective general French population.Vaxillaire M., Cavalcanti-Proenca C., Dechaume A., Tichet J., Marre M., Balkau B., Froguel P.Diabetes 57:2253-2257(2008) The P446L variant in GCKR associated with fasting plasma glucose and triglyceride levels exerts its effect through increased glucokinase activity in liver.Beer N.L., Tribble N.D., McCulloch L.J., Roos C., Johnson P.R., Orho-Melander M., Gloyn A.L.Hum. Mol. Genet. 18:4081-4088(2009) Molecular basis for the role of glucokinase regulatory protein as the allosteric switch for glucokinase.Choi J.M., Seo M.H., Kyeong H.H., Kim E., Kim H.S.Proc. Natl. Acad. Sci. U.S.A. 110:10171-10176(2013) Crystal structure of glucokinase regulatory protein.Pautsch A., Stadler N., Lohle A., Rist W., Berg A., Glocker L., Nar H., Reinert D., Lenter M., Heckel A., Schnapp G., Kauschke S.G.Biochemistry 52:3523-3531(2013) Common missense variant in the glucokinase regulatory protein gene is associated with increased plasma triglyceride and C-reactive protein but lower fasting glucose concentrations.Orho-Melander M., Melander O., Guiducci C., Perez-Martinez P., Corella D., Roos C., Tewhey R., Rieder M.J., Hall J., Abecasis G., Tai E.S., Welch C., Arnett D.K., Lyssenko V., Lindholm E., Saxena R., de Bakker P.I., Burtt N., Voight B.F., Hirschhorn J.N., Tucker K.L., Hedner T., Tuomi T., Isomaa B., Eriksson K.F., Taskinen M.R., Wahlstrand B., Hughes T.E., Parnell L.D., Lai C.Q., Berglund G., Peltonen L., Vartiainen E., Jousilahti P., Havulinna A.S., Salomaa V., Nilsson P., Groop L., Altshuler D., Ordovas J.M., Kathiresan S.Diabetes 57:3112-3121(2008)

NCBI and Uniprot Product Information

• NCBI GI #: 221625433
• NCBI GeneID: 2646
• NCBI Accession #: NP_001477.2
• NCBI GenBank Nucleotide #: NM_001486.3
• UniProt Accession #: Q14397; Q53RY6; Q99522; A1L4C2; B4DPQ2
• Molecular Weight: 70.7 kDa
• NCBI Official Full Name: glucokinase regulatory protein
• NCBI Official Synonym Full Names: glucokinase (hexokinase 4) regulator
• NCBI Official Symbol: GCKR
• NCBI Official Synonym Symbols: GKRP; FGQTL5
• NCBI Protein Information: glucokinase regulatory protein
• UniProt Protein Name: Glucokinase regulatory protein
• Protein Family: Glucokinase regulatory protein
• UniProt Gene Name: GCKR
• UniProt Synonym Gene Names: GKRP; Glucokinase regulator
• UniProt Entry Name: GCKR_HUMAN

NCBI Description

This gene encodes a protein belonging to the GCKR subfamily of the SIS (Sugar ISomerase) family of proteins. The gene product is a regulatory protein that inhibits glucokinase in liver and pancreatic islet cells by binding non-covalently to form an inactive complex with the enzyme. This gene is considered a susceptibility gene candidate for a form of maturity-onset diabetes of the young (MODY). [provided by RefSeq, Jul 2008]

Uniprot Description

GCKR: a key regulator of glucokinase in the liver and pancreas. Not detected in muscle, brain, heart, thymus, intestine, uterus, adipose tissue, kidney, adrenal, lung or spleen. When expressed alone, both glucokinase and GCKR localize predominantly to the cytoplasm. Co-expression induces both proteins to localize in the nucleus.

Protein type: Inhibitor

Chromosomal Location of Human Ortholog: 2p23

Cellular Component: cytoplasm; cytosol; nucleoplasm

Molecular Function: carbohydrate binding; protein binding

Biological Process: carbohydrate metabolic process; glucose transport; hexose transport; negative regulation of glucokinase activity; protein import into nucleus, translocation; response to fructose stimulus; transmembrane transport; urate metabolic process

Disease: Fasting Plasma Glucose Level Quantitative Trait Locus 5