Beta-enolase (ENO3) Recombinant Protein | ENO3 recombinant protein

Recombinant Human Beta-enolase (ENO3), partial

Cat. Num. AAA957968

• Gene Names: ENO3; MSE; GSD13
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Beta-enolase (ENO3); Recombinant Human Beta-enolase (ENO3); partial; 2-phospho-D-glycerate hydro-lyase; Enolase 3; Muscle-specific enolase; MSE; Skeletal muscle enolase; ENO3 recombinant protein

• Host: E Coli
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Liquid containing glycerol
• Sequence Positions: 7-432. partial.
• Sequence: FAREILDSRGNPTVEVDLHTAKGRFRAAVPSGASTGIYEALELRDGDKGRYLGKGVLKAVENINNTLGPALLQKKLSVVDQEKVDKFMIELDGTENKSKFGANAILGVSLAVCKAGAAEKGVPLYRHIADLAGNPDLILPVPAFNVINGGSHAGNKLAMQEFMILPVGASSFKEAMRIGAEVYHHLKGVIKAKYGKDATNVGDEGGFAPNILENNEALELLKTAIQAAGYPDKVVIGMDVAASEFYRNGKYDLDFKSPDDPARHITGEKLGELYKSFIKNYPVVSIEDPFDQDDWATWTSFLSGVNIQIVGDDLTVTNPKRIAQAVEKKACNCLLLKVNQIGSVTESIQACKLAQSNGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYNQLMRIEEALGDKAIFAGRKFRNPK

• 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 ENO3 recombinant protein

Appears to have a function in striated muscle development and regeneration.

Product Categories/Family for ENO3 recombinant protein

Metabolism

References

Structure of human muscle (beta) enolase mRNA and protein deduced from a genomic clone.Peshavaria M., Hinks L.J., Day I.N.M.Nucleic Acids Res. 17:8862-8862(1989) Nucleotide sequence of a cDNA encoding the human muscle-specific enolase (MSE) .Cali L., Feo S., Oliva D., Giallongo A.Nucleic Acids Res. 18:1893-1893(1990) Molecular structure of the human muscle-specific enolase gene (ENO3) .Peshavaria M., Day I.N.M.Biochem. J. 275:427-433(1991) Structural features of the human gene for muscle-specific enolase. Differential splicing in the 5'-untranslated sequence generates two forms of mRNA.Giallongo A., Venturella S., Oliva D., Barbieri G., Rubino P., Feo S.Eur. J. Biochem. 214:367-374(1993) 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) DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage.Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.Nature 440:1045-1049(2006) 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. Characterization of MR-1, a novel myofibrillogenesis regulator in human muscle.Li T.-B., Liu X.-H., Feng S., Hu Y., Yang W.-X., Han Y., Wang Y.-G., Gong L.-M.Acta Biochim. Biophys. Sin. 36:412-418(2004) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011) N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014) Beta-enolase deficiency, a new metabolic myopathy of distal glycolysis.Comi G.P., Fortunato F., Lucchiari S., Bordoni A., Prelle A., Jann S., Keller A., Ciscato P., Galbiati S., Chiveri L., Torrente Y., Scarlato G., Bresolin N.Ann. Neurol. 50:202-207(2001)

NCBI and Uniprot Product Information

• NCBI GI #: 301897479
• NCBI GeneID: 2027
• NCBI Accession #: NP_001180432.1
• NCBI GenBank Nucleotide #: NM_001193503.1
• UniProt Accession #: P13929; Q96AE2; B4DUI6; B4DUM6; D3DTL2; E7ENK8
• Molecular Weight: 50.1 kDa
• NCBI Official Full Name: beta-enolase isoform 2
• NCBI Official Synonym Full Names: enolase 3 (beta, muscle)
• NCBI Official Symbol: ENO3
• NCBI Official Synonym Symbols: MSE; GSD13
• NCBI Protein Information: beta-enolase
• UniProt Protein Name: Beta-enolase
• Protein Family: Beta-enolase
• UniProt Gene Name: ENO3
• UniProt Synonym Gene Names: MSE
• UniProt Entry Name: ENOB_HUMAN

NCBI Description

This gene encodes one of the three enolase isoenzymes found in mammals. This isoenzyme is found in skeletal muscle cells in the adult where it may play a role in muscle development and regeneration. A switch from alpha enolase to beta enolase occurs in muscle tissue during development in rodents. Mutations in this gene have be associated glycogen storage disease. Alternatively spliced transcript variants encoding different isoforms have been described.[provided by RefSeq, Jul 2010]

Uniprot Description

ENO3: Appears to have a function in striated muscle development and regeneration. Defects in ENO3 are the cause of glycogen storage disease type 13 (GSD13). A metabolic disorder that results in exercise-induced myalgias, generalized muscle weakness and fatigability. It is characterized by increased serum creatine kinase and decreased enolase 3 activity. Dramatically reduced protein levels with focal sarcoplasmic accumulation of glycogen- beta particles are detected on ultrastructural analysis. Belongs to the enolase family. 3 isoforms of the human protein are produced by alternative splicing.

Protein type: EC 4.2.1.11; Carbohydrate Metabolism - glycolysis and gluconeogenesis; Lyase

Chromosomal Location of Human Ortholog: 17p13.2

Cellular Component: cytoplasm; cytosol; extracellular space; phosphopyruvate hydratase complex; plasma membrane

Molecular Function: magnesium ion binding; phosphopyruvate hydratase activity; protein heterodimerization activity; protein homodimerization activity

Biological Process: aging; carbohydrate metabolic process; gluconeogenesis; glucose metabolic process; response to drug; skeletal muscle regeneration

Disease: Glycogen Storage Disease Xiii