SRP6105
MDH from bacteria
recombinant, expressed in E. coli, ≥95% (SDS-PAGE)
Synonym(s):
ECK3225, JW3205, Malate dehydrogenase
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About This Item
NACRES:
NA.32
UNSPSC Code:
12352204
Form:
liquid
Assay:
≥95% (SDS-PAGE)
Biological source:
bacterial
Recombinant:
expressed in E. coli
Mol wt:
34.9 kDa (336 aa, 1-312 aa + NT His Tag)
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.
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.
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.
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
signalword
Warning
hcodes
Hazard Classifications
Eye Irrit. 2
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
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Priscila Pini Zenatti et al.
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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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