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SRP6105

Sigma-Aldrich

MDH from bacteria

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

Sinónimos:

ECK3225, JW3205, Malate dehydrogenase

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About This Item

UNSPSC Code:
12352204
NACRES:
NA.32
En este momento no podemos mostrarle ni los precios ni la disponibilidad

biological source

bacterial

recombinant

expressed in E. coli

assay

≥95% (SDS-PAGE)

form

liquid

mol wt

34.9 kDa (336 aa, 1-312 aa + NT His Tag)

packaging

pkg of 100 μg

technique(s)

activity assay: suitable

UniProt accession no.

P61889

shipped in

dry ice

storage temp.

−70°C

Gene Information

Escherichia coli ... MDH(947854)

General description

Malate dehydrogenase (MDH) belongs to the LDH/MDH superfamily and MDH type 1 family. It exists as a homodimer and tetramer in prokaryotes.[1]

Biochem/physiol Actions

Malate dehydrogenase (MDH) catalyzes the conversion of malate into oxaloacetate (using NAD+) and vice versa (reversible reaction). This reaction is part of many metabolic pathways, including the citric acid cycle. MDH has a key role in the central oxidative pathway. Malate dehydrogenase is also involved in gluconeogenesis, the synthesis of glucose from smaller molecules.[1]

Physical form

1 mg/mL solution in 20 mM Tris-HCl (pH 8.0) containing 1 mM DTT, 50 mM NaCl and 10% glycerol.

Preparation Note

Centrifuge the vial prior to opening.

Other Notes

MGSSHHHHHH SSGLVPRGSH MGSHMKVAVL GAAGGIGQAL ALLLKTQLPS GSELSLYDIA PVTPGVAVDL SHIPTAVKIK GFSGEDATPA LEGADVVLIS AGVARKPGMD RSDLFNVNAG IVKNLVQQVA KTCPKACIGI ITNPVNTTVA IAAEVLKKAG VYDKNKLFGV TTLDIIRSNT FVAELKGKQP GEVEVPVIGG HSGVTILPLL SQVPGVSFTE QEVADLTKRI QNAGTEVVEA KAGGGSATLS MGQAAARFGL SLVRALQGEQ GVVECAYVEG DGQYARFFSQ PLLLGKNGVE ERKSIGTLSA FEQNALEGML DTLKKDIALG EEFVNK

pictograms

Exclamation mark
GHS07

signalword

Warning

hcodes

H319

Hazard Classifications

Eye Irrit. 2

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

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Function, kinetic properties, crystallization, and regulation of microbial malate dehydrogenase*
Toshiko T
Journal of Zhejiang University. Science. B, 17(4), 247-261 (2016)

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