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Safety Information

SRP6103

Sigma-Aldrich

MDH1 human

recombinant, expressed in E. coli, ≥95% (SDS-PAGE)

Synonym(s):

MDH-s, MDHA, MOR2, Malate dehydrogenase cytoplasmic

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About This Item

CAS Number:
480083-12-3
UNSPSC Code:
12352204
NACRES:
NA.32

biological source

human

recombinant

expressed in E. coli

Assay

≥95% (SDS-PAGE)

form

liquid

mol wt

37.4 kDa (342 aa, 1-334 aa + CT His Tag)

packaging

pkg of 100 μg

technique(s)

activity assay: suitable

NCBI accession no.

P40925

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... MDH1(4190)

General description

MDH1 (malate dehydrogenase 1) is cytoplasmic protein belonging to the 2-hydroxy acid dehydrogenases protein family. Eukaryotes contain two forms of MDH proteins depending upon their subcellular localization, MDH1 and MDH2. MDH2 is present in the mitochondrial matrix and MDH1 is present in the cytoplasm. This gene is localized to human chromosome 2, and is composed of nine exons and eight introns.

Application

MDH1 (malate dehydrogenase 1) human has been used for measuring MDH1 enzyme activity.

Biochem/physiol Actions

MDH1 (malate dehydrogenase 1) is responsible for reversibly converting malate to oxaloacetate in cytoplasm. It participates in metabolism where it transports NADH equivalents and metabolites across the mitochondrial membrane, and regulates the TCA (tricarboxylic acid) cycle pool size. MDH1 is involved in malate/aspartate shuttle, which is involved in maintaining the balance of nitrogen, oxaloacetate, and the α-ketoglutarate intermediate shuttling between the cytosol and mitochondrial matrix. It is thought to function as an important checkpoint for energy balance between mitochondria and cytoplasm. MDH1 acts as a regulator of p53-dependent apoptosis in response to glucose deprivation, indicating that synergism between energy metabolism and p53 transactivation is linked with cell metabolic state and hence, determination of cell death.

Physical form

1 mg/mL solution in 20 mM Tris-HCl (pH 8.0) containing 10% glycerol.

Preparation Note

Centrifuge the vial prior to opening.

Other Notes

MSEPIRVLVT GAAGQIAYSL LYSIGNGSVF GKDQPIILVL LDITPMMGVL DGVLMELQDC ALPLLKDVIA TDKEDVAFKD LDVAILVGSM PRREGMERKD LLKANVKIFK SQGAALDKYA KKSVKVIVVG NPANTNCLTA SKSAPSIPKE NFSCLTRLDH NRAKAQIALK LGVTANDVKN VIIWGNHSST QYPDVNHAKV KLQGKEVGVY EALKDDSWLK GEFVTTVQQR GAAVIKARKL SSAMSAAKAI CDHVRDIWFG TPEGEFVSMG VISDGNSYGV PDDLLYSFPV VIKNKTWKFV EGLPINDFSR EKMDLTAKEL TEEKESAFEF LSSALEHHHH HH

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

JAN Code

SRP6103-100UG:

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Certificates of Analysis (COA)

Lot/Batch Number
5F05L63550
4G12L63550
4D10L63550

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A nucleocytoplasmic malate dehydrogenase regulates p53 transcriptional activity in response to metabolic stress.
Lee SM et al
Cell Death and Differentiation, 16(5), 738-748 (2009)
Ultra high throughput sequencing excludes MDH1 as candidate gene for RP28-linked retinitis pigmentosa.
Rio Frio T et al
Molecular Vision, 15, 2627-2633 (2009)
Tomohiro Yoshida et al.
Biochemical and biophysical research communications, 522(3), 633-638 (2019-12-04)
Metabolic programs are rewired in cancer cells to support survival and tumor growth. Among these, recent studies have demonstrated that glutamate-oxaloacetate transaminase 1 (GOT1) plays key roles in maintaining redox homeostasis and proliferation of pancreatic ductal adenocarcinomas (PDA). This suggests
Edouard Mullarky et al.
Proceedings of the National Academy of Sciences of the United States of America, 113(7), 1778-1783 (2016-02-03)
Cancer cells reprogram their metabolism to promote growth and proliferation. The genetic evidence pointing to the importance of the amino acid serine in tumorigenesis is striking. The gene encoding the enzyme 3-phosphoglycerate dehydrogenase (PHGDH), which catalyzes the first committed step
Eun Young Kim et al.
Journal of lipid research, 53(9), 1864-1876 (2012-06-14)
Acetylation is one of the most crucial post-translational modifications that affect protein function. Protein lysine acetylation is catalyzed by acetyltransferases, and acetyl-CoA functions as the source of the acetyl group. Additionally, acetyl-CoA plays critical roles in maintaining the balance between

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