IDH1
Isocitrate Dehydrogenase-1 Yeast Recombinant
Cat. No.
BT10274
Source
Yeast cells.
Synonyms
Isocitrate dehydrogenase [NADP] cytoplasmic, EC 1.1.1.42, Cytosolic NADP-isocitrate dehydrogenase, Oxalosuccinate decarboxylase, IDH, NADP(+)-specific ICDH, IDP, PICD.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 90% as determined by SDS-PAGE.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description
Recombinant Saccharomyces Cerevisiae ICDH (NADP) derived from yeast host cells by using over-expression system, is full length same as designated ICD1 from Saccharomyces Cerevisiae. The N-terminal amino acid Phenylalanine residue next to Met is substituted with Alanine for overexpression.
The ICDH is purified by proprietary chromatographic techniques.
The ICDH is purified by proprietary chromatographic techniques.
Product Specs
Introduction
Isocitrate dehydrogenase (IDH) is an enzyme that plays a crucial role in the citric acid cycle, a metabolic pathway essential for energy production within cells. IDH catalyzes the conversion of isocitrate to alpha-ketoglutarate, producing NADH and carbon dioxide in the process. This reaction is highly regulated and is influenced by factors like ADP, citrate, calcium ions, NADH, NADPH, and ATP. IDH is primarily found in the mitochondria of cells.
Description
This product consists of recombinant Saccharomyces Cerevisiae ICDH (NADP), a form of the enzyme derived from yeast cells specifically engineered for overexpression. This full-length protein is identical to the ICD1 enzyme found naturally in Saccharomyces Cerevisiae, with the exception of a single amino acid substitution (Phenylalanine to Alanine) near the N-terminal to enhance its production. The purification process involves advanced chromatographic methods to ensure high purity.
Physical Appearance
A clear solution that has been sterilized by filtration.
Formulation
Each milliliter of solution contains potassium phosphate buffer (0.075 mol/l, pH 7.1) and 50% glycerol.
Stability
For optimal storage, keep the product refrigerated at 4°C if you plan to use the entire vial within 2 to 4 weeks. For extended storage, freeze the product at -20°C. Adding a carrier protein like HSA or BSA (0.1%) is advisable for long-term storage. To maintain product integrity, avoid repeated freeze-thaw cycles.
Purity
The purity of this product is greater than 90% as assessed by SDS-PAGE analysis.
Biological Activity
The specific activity of this enzyme preparation is 115 units per milligram.
Unit Definition
One unit of enzyme activity is defined as the amount of enzyme required to catalyze the production of 1 micromole of NAD+ per minute under specific assay conditions (25°C, pH 7.5).
Synonyms
Isocitrate dehydrogenase [NADP] cytoplasmic, EC 1.1.1.42, Cytosolic NADP-isocitrate dehydrogenase, Oxalosuccinate decarboxylase, IDH, NADP(+)-specific ICDH, IDP, PICD.
Source
Yeast cells.
Product Science Overview
Isoforms and Localization
In humans, IDH exists in three isoforms: IDH1, IDH2, and IDH3. While IDH3 is involved in the citric acid cycle within the mitochondria and uses NAD+ as a cofactor, IDH1 and IDH2 operate outside the citric acid cycle and utilize NADP+ as a cofactor. These isoforms are found in the cytosol, mitochondria, and peroxisomes .
Recombinant Yeast Isocitrate Dehydrogenase-1
Recombinant yeast IDH1 is produced using yeast cells, typically Pichia pastoris, as the expression system. This recombinant enzyme retains the same catalytic properties as its native counterpart and is used extensively in research and industrial applications. The recombinant form is particularly valuable for studying the enzyme’s structure, function, and potential therapeutic applications .
Applications and Importance
- Research: Recombinant IDH1 is used to study metabolic pathways, enzyme kinetics, and the effects of mutations on enzyme function. It is also employed in structural biology to understand the enzyme’s three-dimensional structure and its interaction with other molecules.
- Industrial: In the biotechnology industry, recombinant IDH1 is used in the production of various biochemicals. Its ability to catalyze specific reactions makes it a valuable tool in the synthesis of compounds used in pharmaceuticals and other industries.
- Medical: Mutations in the IDH1 gene have been linked to various cancers, including gliomas and acute myeloid leukemia (AML). Studying recombinant IDH1 helps researchers understand the molecular mechanisms underlying these diseases and develop targeted therapies .
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