Human GNPDA 1 Antibody Conjugated to FITC

Référence B2015319

Conditionnement : 50ug

Marque : Molecular Depot

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Human GNPDA 1 Antibody Conjugated to FITC

Catalog Number: B2015319 (50 ug)
Human GNPDA 1 Antibody Conjugated to FITC is a high quality Human GNPDA 1 Antibody Conjugated to FITC. 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: B2015319 Categories: Antibodies, Conjugates Tag: MD 1000

Product Description

5/5 - (3 votes)

Human GNPDA 1 Antibody Conjugated to FITC
Catalog number: B2015319
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: Altamirano MM, Hernandez-Arana A, Tello-Solis S, Calcagno ML. Spectrochemical evidence for the presence of a tyrosine residue in the allosteric site of glucosamine-6-phosphate deaminase from Escherichia coli Eur J Biochem. 1994 Mar 1;220(2):409-13.
2: Zonszein S, Álvarez-Añorve LI, Vázquez-Núñez RJ, Calcagno ML. The tertiary origin of the allosteric activation of E. coli glucosamine-6-phosphate deaminase studied by sol-gel nanoencapsulation of its T conformer PLoS One. 2014 May 2;9(5):e96536.
3: Van Keulen H, Steimle PA, Bulik DA, Borowiak RK, Jarroll EL. Cloning of two putative Giardia lamblia glucosamine 6-phosphate isomerase genes only one of which is transcriptionally activated during encystment J Eukaryot Microbiol. 1998 Nov-Dec;45(6):637-42.
4: Singh B, Datta A. Regulation of glucosamine-6-phosphate deaminase synthesis in yeast Biochim Biophys Acta. 1979 Feb 19;583(1):28-35.
5: Altamirano MM, Plumbridge JA, Barba HA, Calcagno ML. Glucosamine-6-phosphate deaminase from Escherichia coli has a trimer of dimers structure with three intersubunit disulphides Biochem J. 1993 Nov 1;295 ( Pt 3)(Pt 3):645-8.
6: Horjales E, Altamirano MM, Calcagno ML, Garratt RC, Oliva G. The allosteric transition of glucosamine-6-phosphate deaminase: the structure of the T state at 2.3 A resolution Structure. 1999 May;7(5):527-37.
7: Kim KJ, Kim MH, Kim GH, Kang BS. The crystal structure of a novel glucosamine-6-phosphate deaminase from the hyperthermophilic archaeon Pyrococcus furiosus Proteins. 2007 Jul 1;68(1):413-7.
8: White RJ, Pasternak CA. N-acetylglucosamine-6-phosphate deacetylase and glucosamine-6-phosphate deaminase from Escherichia coli Methods Enzymol. 1975;41:497-502.
9: Bustos-Jaimes I, Sosa-Peinado A, Rudiño-Piñera E, Horjales E, Calcagno ML. On the role of the conformational flexibility of the active-site lid on the allosteric kinetics of glucosamine-6-phosphate deaminase J Mol Biol. 2002 May 24;319(1):183-9.
10: Bustos-Jaimes I, Ramírez-Costa M, De Anda-Aguilar L, Hinojosa-Ocaña P, Calcagno ML. Evidence for two different mechanisms triggering the change in quaternary structure of the allosteric enzyme, glucosamine-6-phosphate deaminase Biochemistry. 2005 Feb 1;44(4):1127-35.

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Additional Information

Weight 0.15 oz
Dimensions 2 × 0.5 × 0.5 in