Human GNPDA 1 Antibody Conjugated to APC

Referencia B2015321

embalaje : 50ug

Marca : Molecular Depot

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Human GNPDA 1 Antibody Conjugated to APC

Catalog Number: B2015321 (50 ug)
Human GNPDA 1 Antibody Conjugated to APC is a high quality Human GNPDA 1 Antibody Conjugated to APC. This product has been used as a molecular tool for various biochemical applications. It has also been used in a wide array of other chemical and immunological applications. Custom bulk amounts of this product are available upon request.

Live enquiry about this product via Text/SMS: 1-858-900-3210.

SKU: B2015321 Categories: Antibodies, Conjugates Tag: MD 1000

Product Description

4.8/5 - (5 votes)

Human GNPDA 1 Antibody Conjugated to APC
Catalog number: B2015321
Lot number: Batch Dependent
Expiration Date: Batch dependent
Amount: 50 ug
Molecular Weight or Concentration: N/A
Supplied as: Solution
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: Natarajan K, Datta A. Molecular cloning and analysis of the NAG1 cDNA coding for glucosamine-6-phosphate deaminase from Candida albicans J Biol Chem. 1993 May 5;268(13):9206-14.
2: Álvarez-Añorve LI, Gaugué I, Link H, Marcos-Viquez J, Díaz-Jiménez DM, Zonszein S, Bustos-Jaimes I, Schmitz-Afonso I, Calcagno ML, Plumbridge J. Allosteric Activation of Escherichia coli Glucosamine-6-Phosphate Deaminase (NagB) In Vivo Justified by Intracellular Amino Sugar Metabolite Concentrations J Bacteriol. 2016 May 13;198(11):1610-1620.
3: Lara-Lemus R, Libreros-Minotta CA, Altamirano MM, Calcagno ML. Purification and characterization of glucosamine-6-phosphate deaminase from dog kidney cortex Arch Biochem Biophys. 1992 Sep;297(2):213-20.
4: Altamirano MM, Plumbridge JA, Calcagno ML. Identification of two cysteine residues forming a pair of vicinal thiols in glucosamine-6-phosphate deaminase from Escherichia coli and a study of their functional role by site-directed mutagenesis Biochemistry. 1992 Feb 4;31(4):1153-8.
5: COMB DG, ROSEMAN S. Glucosamine metabolism. IV. Glucosamine-6-phosphate deaminase J Biol Chem. 1958 Jun;232(2):807-27.
6: Lara-González S, Dixon HB, Mendoza-Hernández G, Altamirano MM, Calcagno ML. On the role of the N-terminal group in the allosteric function of glucosamine-6-phosphate deaminase from Escherichia coli J Mol Biol. 2000 Aug 4;301(1):219-27.
7: Montero-Morán GM, Lara-González S, Alvarez-Añorve LI, Plumbridge JA, Calcagno ML. On the multiple functional roles of the active site histidine in catalysis and allosteric regulation of Escherichia coli glucosamine 6-phosphate deaminase Biochemistry. 2001 Aug 28;40(34):10187-96.
8: Oliva G, Fontes MR, Garratt RC, Altamirano MM, Calcagno ML, Horjales E. Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from Escherichia coli at 2.1 A resolution Structure. 1995 Dec 15;3(12):1323-32.
9: Marcos-Viquez J, Rodríguez-Hernández A, Álvarez-Añorve LI, Medina-García A, Plumbridge J, Calcagno ML, Rodríguez-Romero A, Bustos-Jaimes I. Substrate binding in the allosteric site mimics homotropic cooperativity in the SIS-fold glucosamine-6-phosphate deaminases Protein Sci. 2023 Jun;32(6):e4651.
10: Erratum: Glucosamine-6-Phosphate Isomerase 1 Promotes Tumor Progression and Indicates Poor Prognosis in Hepatocellular Carcinoma [Corrigendum] Cancer Manag Res. 2020 Aug 5;12:6861-6862.

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Additional Information

Weight 0.15 oz
Dimensions 2 × 0.5 × 0.5 in