Recombinant Human MDH1 Protein (C-6His)

Beta LifeScience SKU/CAT #: BL-0299NP
BL-0299NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
BL-0299NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Recombinant Human MDH1 Protein (C-6His)

Beta LifeScience SKU/CAT #: BL-0299NP
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Product Overview

Description Recombinant Human Malate Dehydrogenase, Cytoplasmic is produced by our E.coli expression system and the target gene encoding Ser2-Ala334 is expressed with a 6His tag at the C-terminus.
Accession P40925
Synonym Malate Dehydrogenase Cytoplasmic; Cytosolic Malate Dehydrogenase; Diiodophenylpyruvate Reductase; MDH1; MDHA
Gene Background Malate Dehydrogenase, Cytoplasmic (MDH1) is an enzyme which belongs to the MDH Type 2 sub-family of LDH/MDH superfamily. MDH1 is involved in the Citric Acid Cycle that catalyzes the conversion of Malate into Oxaloacetate (using NAD+) and vice versa. MDH1 should not be confused with Malic Enzyme, which catalyzes the conversion of Malate to Pyruvate, producing NADPH. MDH1 also participates in Gluconeogenesis, the synthesis of Glucose from smaller molecules. Pyruvate in the mitochondria is acted upon by Pyruvate Carboxylase to form Pxaloacetate, a Citric Acid Cycle intermediate. In order to transport the Oxaloacetate out of the Mitochondria, Malate Dehydrogenase reduces it to Malate, and it then traverses the inner Mitochondrial membrane. Once in the cytosol, the Malate is oxidized back to Oxaloacetate by MDH1. Finally, Phosphoenol-Pyruvate Carboxy Kinase (PEPCK) converts Oxaloacetate to Phosphoenol Pyruvate.
Molecular Mass 37.5 KDa
Apmol Mass 36 KDa, reducing conditions
Formulation Supplied as a 0.2 μm filtered solution of 20mM Tris-HCl, 150mM NaCl, pH 8.0.
Endotoxin Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity Not tested
Storage Store at ≤-70°C, stable for 6 months after receipt. Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.
Shipping The product is shipped on dry ice/polar packs. Upon receipt, store it immediately at the temperature listed below.
Usage For Research Use Only

Target Details

Target Function Catalyzes the reduction of aromatic alpha-keto acids in the presence of NADH. Plays essential roles in the malate-aspartate shuttle and the tricarboxylic acid cycle, important in mitochondrial NADH supply for oxidative phosphorylation.
Subcellular Location Cytoplasm.
Protein Families LDH/MDH superfamily, MDH type 2 family
Database References

Gene Functions References

  1. expression of miR-126-5p suppresses the enzymatic activity of MDH1, mitochondrial respiration and caused cell death in non-small cell lung carcinoma cell lines. PMID: 29574159
  2. Data show that in the endogenous readthrough of the human MDH1 stop codon, the stop codon can encode tryptophan and arginine, and is tissue-specific. PMID: 27881739
  3. Proliferating cells rely on both MDH1 and LDH to replenish cytosolic NAD. PMID: 28263970
  4. Arginine methylation of MDH1 by CARM1 regulates cellular redox homeostasis and suppresses glutamine metabolism of pancreatic cancer. PMID: 27840030
  5. adipogenic differentiation may be regulated by the acetylation of MDH1 PMID: 22693256
  6. The MDH1 gene is not the cause of RP28-linked autosomal recessive retinitis pigmentosa. PMID: 20011630
  7. expression of MDH1 is maintained in the adult heart but is not present in levels as high as in the fetus PMID: 15565635
  8. Malate Dehydrogenase directly regulates the Tumor Suppressor Protein p53-dependent apoptosis upon glucose deprivation and involved in maintaining cellular metabolic state and further determining cell death. PMID: 19229245


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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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