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관련 카테고리
일반 설명
LDH (lactic dehydrogenase), a glycolytic enzyme, particularly present in skeletal muscle, heart, liver, kidneys, brain, lungs and red blood cells. It has five isoenzyme forms. LDH possess a tetrameric structure.
애플리케이션
Lactic Dehydrogenase, recombinant from E. coli has been used:
- in lactate dehydrogenase (LDH) and malate dehydrogenase 1 (MDH1)assays and cross-linking assays
- to prepare assay buffer to measure pyruvate kinase (PYK) by coupled assay
- in in vitro DltC D-alanylation assay
생화학적/생리학적 작용
L-lactic dehydrogenase catalyzes the conversion of L-lactate into L-pyruvate while reducing NAD+ to NADH and H+.
Conversion of L-lactate into L-pyruvate is crucial in hypoxic and anaerobic conditions, especially when synthesis of adenosine triphosphate (ATP) by oxidative phosphorylation is interrupted.
단위 정의
One unit corresponds to the amount of enzyme which reduces 1 μmol pyruvate per minute at pH 7.4 and 25°C (NADH as cofactor)
신호어
Danger
유해 및 위험 성명서
예방조치 성명서
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
개인 보호 장비
Eyeshields, Gloves, type N95 (US)
이미 열람한 고객
Glycolysis without pyruvate kinase in Clostridium thermocellum
Olson DG, et al.
Metabolic engineering, 39, 169-180 (2017)
A partial reconstitution implicates DltD in catalyzing lipoteichoic acid D-alanylation
Wood BM, et al.
The Journal of Biological Chemistry, 293(46), 17985-17996 (2018)
Cardiac, Vascular, and Skeletal Muscle Systems
Haschek and Rousseaux's Handbook of Toxicologic Pathology (2013)
Circulating biomarkers in malignant melanoma
Advances in Clinical Chemistry, 69, 47-89 (2015)
An atypical glycolysis in Clostridium thermocellum
Zhou J, et al.
Applied and Environmental Microbiology, 39, AEM-04037 (2013)
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