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Merck

SRP6103

Sigma-Aldrich

MDH1 human

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

Synonym(e):

MDH-s, MDHA, MOR2, Malate dehydrogenase cytoplasmic

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About This Item

CAS-Nummer:
UNSPSC-Code:
12352204
NACRES:
NA.32

Biologische Quelle

human

Rekombinant

expressed in E. coli

Assay

≥95% (SDS-PAGE)

Form

liquid

Mol-Gew.

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

Verpackung

pkg of 100 μg

Methode(n)

activity assay: suitable

NCBI-Hinterlegungsnummer

Versandbedingung

dry ice

Lagertemp.

−70°C

Angaben zum Gen

human ... MDH1(4190)

Allgemeine Beschreibung

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.

Anwendung

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

Biochem./physiol. Wirkung

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.

Physikalische Form

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

Angaben zur Herstellung

Centrifuge the vial prior to opening.

Sonstige Hinweise

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

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable


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Die Dokumentenbibliothek aufrufen

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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