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Native Porcine Isocitrate Dehydrogenase Proteins Molecular Depot
Native Porcine Isocitrate Dehydrogenase Proteins Molecular Depot
Native Porcine Isocitrate Dehydrogenase Proteins Molecular Depot
Native Porcine Isocitrate Dehydrogenase Proteins Molecular Depot

Native Porcine Isocitrate Dehydrogenase

$2,795.00

    Catalog Number: B2017378 (1 KU)

    Native Porcine Isocitrate Dehydrogenase (IDH) is an enzyme derived from pigs. It plays a crucial role in the citric acid cycle, providing energy in the form of ATP. IDH catalyzes the oxidative decarboxylation of isocitrate, producing alpha-ketoglutarate and CO2 while reducing NAD+ to NADH or NADP+ to NADPH. It is used in research and industrial applications. 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.

    Products are for in vitro research use only (RUO).

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What's Included

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VR Headset

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2 Touch Controllers

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Charging Cable

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Power Adapter

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Glasses Spacer

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Native Porcine Isocitrate Dehydrogenase

Catalog number: B2017378
Lot number: Batch Dependent
Expiration Date: Batch dependent
Amount: 1 KU
Molecular Weight or Concentration: N/A
Supplied as: Solution
Applications: a molecular tool for various biochemical applications
Storage: 2-8°C
Keywords: ICDH, Threo-Ds-Isocitrate, IDH2, IDH, NADP+Oxidoreductase
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

  • Kim TK, Colman RF. Ser95, Asn97, and Thr78 are important for the catalytic function of porcine NADP-dependent isocitrate dehydrogenase Protein Sci. 2005 Jan;14(1):140-7.
  • Wrenger C, Müller S. Isocitrate dehydrogenase of Plasmodium falciparum Eur J Biochem. 2003 Apr;270(8):1775-83.
  • Karlström M, Stokke R, Steen IH, Birkeland NK, Ladenstein R. Isocitrate dehydrogenase from the hyperthermophile Aeropyrum pernix: X-ray structure analysis of a ternary enzyme-substrate complex and thermal stability J Mol Biol. 2005 Jan 21;345(3):559-77.
  • Huang YC, Soundar S, Colman RF. Affinity cleavage at the divalent metal site of porcine NAD-specific isocitrate dehydrogenase Protein Sci. 2000 Jan;9(1):104-11.
  • Ehrlich RS, Colman RF. Coenzyme binding by native and chemically modified pig heart triphosphopyridine nucleotide dependent isocitrate dehydrogenase Biochemistry. 1975 Nov 4;14(22):5008-16.
  • Huang YC, Bailey JM, Colman RF. Inactivation of NAD-dependent isocitrate dehydrogenase by affinity labeling of the allosteric ADP site by 2-(4-bromo-2,3-dioxobutylthio)adenosine 5′-diphosphate J Biol Chem. 1986 Oct 25;261(30):14100-7.
  • Leiros HK, Fedøy AE, Leiros I, Steen IH. The complex structures of isocitrate dehydrogenase from Clostridium thermocellum and Desulfotalea psychrophila suggest a new active site locking mechanism FEBS Open Bio. 2012 Jul 7;2:159-72.
  • Colman RF. Binding of substrates by native and chemically modified isocitrate dehydrogenase Biochim Biophys Acta. 1969 Nov 4;191(2):469-72.
  • Soundar S, Park JH, Huh TL, Colman RF. Evaluation by mutagenesis of the importance of 3 arginines in alpha, beta, and gamma subunits of human NAD-dependent isocitrate dehydrogenase J Biol Chem. 2003 Dec 26;278(52):52146-53.

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Product Resources:

Copy of Technical Specifications

FeatureDetails
Viewing Head Siedentopf type trinocular head, inclined at 30°, Interpupillary adjustment 53mm to 75mm, graduated diopter on left eyetube (30mm I.D. eyetubes)
Eyepieces SWH10X Widefield high eyepoint eyepiece, Field No. 22, tube O.D. 30.0 mm
Nosepiece Quintuple
Quintuple LWD Planachromat Phase 10x, 20x
Condenser TC Condenser N.A. 0.30, W.D. 73.0mm
Stage180mm(X) x 245mm(Y) plain stage with replaceable glass insert with 45mm opening, Glass Stage plate insert
IlluminationKoehler without iris, with phase slider, 3W LED
WarrantyLIMITED LIFETIME WARRANTY

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