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Key Documents

SRP6103

Sigma-Aldrich

MDH1 human

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

Sinónimos:

MDH-s, MDHA, MOR2, Malate dehydrogenase cytoplasmic

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About This Item

Número de CAS:
Código UNSPSC:
12352204
NACRES:
NA.32

origen biológico

human

recombinante

expressed in E. coli

Análisis

≥95% (SDS-PAGE)

formulario

liquid

mol peso

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

envase

pkg of 100 μg

técnicas

activity assay: suitable

Nº de acceso NCBI

Condiciones de envío

dry ice

temp. de almacenamiento

−70°C

Información sobre el gen

human ... MDH1(4190)

Descripción general

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.

Aplicación

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

Acciones bioquímicas o fisiológicas

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.

Forma física

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

Nota de preparación

Centrifuge the vial prior to opening.

Otras notas

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

Código de clase de almacenamiento

11 - Combustible Solids

Clase de riesgo para el agua (WGK)

WGK 3

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable


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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)
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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