MDH1 (1-334, His-tag)

CAT#: AR09603PU-N

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Recombinant human MDH1 protein, fused to His-tag at C-terminus, was expressed in E.coli and purified by using conventional chromatography.


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USD 330.00


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2 Weeks

Size
    • 100 ug


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Product Data
Description Recombinant human MDH1 protein, fused to His-tag at C-terminus, was expressed in E.coli and purified by using conventional chromatography.
Species Human
Expression Host E. coli
Tag His-tag
Predicted MW 37.4 kDa
Concentration 1.0 mg/ml (determined by Bradford assay)
Purity > 95 % by SDS-PAGE
Buffer 20 mM Tris-HCl Buffer (pH 8.0) containing 10% Glycerol
Bioactivity Specific activity is > 8 units/mg, and is defined as the amount of enzyme that cleaves 1 umole of oxalacetate and beta-NADH to L-malate and beta-NAD per minute at pH 7.5 at 25°C (see "Protocols").
Preparation Liquid purified protein
Reference Data
RefSeq NP_001186040
Locus ID 4190
Cytogenetics 2p15
Synonyms HEL-S-32; MDH-s; MDHA; MGC:1375; MOR2
Summary This gene encodes an enzyme that catalyzes the NAD/NADH-dependent, reversible oxidation of malate to oxaloacetate in many metabolic pathways, including the citric acid cycle. Two main isozymes are known to exist in eukaryotic cells: one is found in the mitochondrial matrix and the other in the cytoplasm. This gene encodes the cytosolic isozyme, which plays a key role in the malate-aspartate shuttle that allows malate to pass through the mitochondrial membrane to be transformed into oxaloacetate for further cellular processes. Alternatively spliced transcript variants have been found for this gene. A recent study showed that a C-terminally extended isoform is produced by use of an alternative in-frame translation termination codon via a stop codon readthrough mechanism, and that this isoform is localized in the peroxisomes. Pseudogenes have been identified on chromosomes X and 6. [provided by RefSeq, Feb 2016]
Protein Families Druggable Genome
Protein Pathways Citrate cycle (TCA cycle), Glyoxylate and dicarboxylate metabolism, Metabolic pathways, Pyruvate metabolism

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