Human GNPDA 1 Antibody RPE Conjugate

Human GNPDA 1 Antibody RPE Conjugate
Catalog number: B2015396
Lot number: Batch Dependent
Expiration Date: Batch dependent
Amount: 30 ug
Molecular Weight or Concentration: N/A
Supplied as: N/A
Applications: a molecular tool for various biochemical applications
Storage: -20°C
Keywords: Glucose-6-phosphate Isomerase 1, Glucose-6-phosphate Deaminase 1, GNPDA 1, GlcN6P Deaminase 1, GNPDA1, GNPI
Grade: Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity >18 MΩ-cm) and are filtered through 0.22 um.

References:
1: White RJ, Pasternak CA. The purification and properties of N-acetylglucosamine 6-phosphate deacetylase from Escherichia coli Biochem J. 1967 Oct;105(1):121-5.
2: Rogers MJ, Ohgi T, Plumbridge J, Söll D. Nucleotide sequences of the Escherichia coli nagE and nagB genes: the structural genes for the N-acetylglucosamine transport protein of the bacterial phosphoenolpyruvate: sugar phosphotransferase system and for glucosamine-6-phosphate deaminase Gene. 1988;62(2):197-207.
3: Sosa-Peinado A, González-Andrade M. Site-directed fluorescence labeling reveals differences on the R-conformer of glucosamine 6-phosphate deaminase of Escherichia coli induced by active or allosteric site ligands at steady state Biochemistry. 2005 Nov 22;44(46):15083-92.
4: Altamirano MM, Plumbridge JA, Hernández-Arana A, Calcagno M. Secondary structure of Escherichia coli glucosamine-6-phosphate deaminase from amino acid sequence and circular dichroism spectroscopy Biochim Biophys Acta. 1991 Jan 29;1076(2):266-72.
5: Chmara H, Milewski S, Andruszkiewicz R, Mignini F, Borowski E. Antibacterial action of dipeptides containing an inhibitor of glucosamine-6-phosphate isomerase Microbiology (Reading). 1998 May;144 ( Pt 5):1349-1358.
6: Eligio-García L, María del Pilar CV, Andrés FL, Apolinar CE, Adrián CC, Enedina JC. Giardia intestinalis: expression of ubiquitin, glucosamine-6-phosphate and cyst wall protein genes during the encystment process Exp Parasitol. 2011 Feb;127(2):382-6.
7: Montero-Morán GM, Horjales E, Calcagno ML, Altamirano MM. Tyr254 hydroxyl group acts as a two-way switch mechanism in the coupling of heterotropic and homotropic effects in Escherichia coli glucosamine-6-phosphate deaminase Biochemistry. 1998 May 26;37(21):7844-9.
8: Bustos-Jaimes I, Calcagno ML. Allosteric transition and substrate binding are entropy-driven in glucosamine-6-phosphate deaminase from Escherichia coli Arch Biochem Biophys. 2001 Oct 15;394(2):156-60.
9: Cisneros DA, Montero-Morán GM, Lara-González S, Calcagno ML. Inversion of the allosteric response of Escherichia coli glucosamine-6-P deaminase to N-acetylglucosamine 6-P, by single amino acid replacements Arch Biochem Biophys. 2004 Jan 1;421(1):77-84.
10: Schwenk RW, Vogel H, Schürmann A. Genetic and epigenetic control of metabolic health Mol Metab. 2013 Sep 25;2(4):337-47.

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