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L1254
L-Lactic Dehydrogenase from rabbit muscle
Type XI, lyophilized powder, 600-1,200 units/mg protein
Sinônimo(s):
Anaerobic Lactate Dehydrogenase, Lactate, NAD-lactate dehydrogenase, (S)-Lactate: NAD+ oxidoreductase, L-LDH, LAD, LD
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1000 UNITS
R$ 498,00
5000 UNITS
R$ 839,00
25000 UNITS
R$ 2.703,00
50000 UNITS
R$ 4.651,00
100000 UNITS
R$ 8.212,00
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1000 UNITS
R$ 498,00
5000 UNITS
R$ 839,00
25000 UNITS
R$ 2.703,00
50000 UNITS
R$ 4.651,00
100000 UNITS
R$ 8.212,00
About This Item
Produtos recomendados
fonte biológica
rabbit muscle
tipo
Type XI
Formulário
lyophilized powder
atividade específica
600-1,200 units/mg protein
peso molecular
140 kDa
composição
protein, 90-100%
condição de armazenamento
(Keep container tightly closed in a dry and well-ventilated place)
técnica(s)
activity assay: suitable
cor
white
atividade externa
pyruvate kinase, myokinase, malic dehydrogenase, glutamic-pyruvic transaminase, glutamic-oxalacetic transaminase and α-glycerophosphate dehydrogenase ≤0.01%
temperatura de armazenamento
−20°C
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Descrição geral
Research area: Cell Signaling
Lactic Dehydrogenase (LDH) has a total molecular weight of 140 kDa and is composed of 4 subunits which are designated M subunit (muscle) and H subunit (heart). These subunits may be mixed in any of 5 combinations (M4, M3H1, M2H2, MH3, and H4). Skeletal muscle contains LDH that is predominately M4 with some small amounts of M3H and traces of H2H2. The H and M subunits are quite similar in molecular weight, but differ substantially in amino acid composition. Rabbit muscle LDH dissociates into dimeric species (MW = ~70 kDa) in acetate-chloride at pH 5.0, the dissociation is reversible. Biochemistry, 13, 3527-3531 (1974). Oxidizes glyoxylate and lactate.
Isoelectric point: 8.4-8.6
Optimal pH : 7.5 .
Isoelectric point: 8.4-8.6
Optimal pH : 7.5 .
Aplicação
L-Lactic Dehydrogenase from rabbit muscle has been used:
- as a component of activation and relaxing solution in ATPase activity and isometric steady-state tension measurements with muscle fiber[1]
- in Trypanosoma congolense pyruvate kinase activity assay[2]
- in pyruvate kinase (PK) assay with rice plastidic PK enzyme OsPK2[3]
Ações bioquímicas/fisiológicas
Also catalyzes the oxidation of other L-2-hydroxymonocarboxylic acids.
Muscle-type Lactic Dehydrogenase (LDH) participates in metabolic pathways and its activity is essential for anaerobic glycolysis. LDH activity is inhibited by ascorbate. LDH regenerates nicotinamide adenine dinucleotide (NAD+) from NADH and is industrially useful in poly(lactic acid) production.[4] In the absence of oxygen, LDH participates in a fermentation reaction, catalyzes pyruvate into lactic acid, and oxidizes nicotinamide adenine dinucleotide (NADH) to NAD+. Therefore, LDH mediates the production of NAD+ essential anaerobic glycolysis pathway. Through this LDH helps maintain the physiological and biochemical functions of the cell in the absence of oxygen.
Definição da unidade
One unit will reduce 1.0 μmole of pyruvate to L-lactate per min at pH 7.5 at 37 °C.
Nota de análise
Protein determined by biuret.
Inibidor
Nº do produto
Descrição
Preços
anticorpo
enzima
Nº do produto
Descrição
Preços
produto relacionado
Palavra indicadora
Danger
Frases de perigo
Declarações de precaução
Classificações de perigo
Resp. Sens. 1
Código de classe de armazenamento
11 - Combustible Solids
Classe de risco de água (WGK)
WGK 1
Equipamento de proteção individual
Eyeshields, Gloves, type N95 (US)
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Matthew Warren Eggert et al.
Applied biochemistry and biotechnology, 165(2), 676-686 (2011-06-01)
In order to evaluate the effectiveness of L: -lactate dehydrogenase (LDH) from rabbit muscle as a regenerative catalyst of the biologically important cofactor nicotinamide adenine dinucleotide (NAD), the kinetics over broad concentrations were studied to develop a suitable kinetic rate
Percy J Russell et al.
Journal of enzyme inhibition and medicinal chemistry, 19(1), 91-98 (2004-06-19)
Muscle-type LDH (LDH-m4) activity is critical for efficient anaerobic glycolysis. The results here show that rabbit LDH-M4 is inhibited by concentrations of ascorbate normally found in tissues. Aldolase and muscle G-actin were found to protect and to reverse inhibitions of
Artigos
For use as a marker in SDS-PAGE; Albumin from chicken egg white, For use as a marker in SDS-PAGE; L-Lactic Dehydrogenase from rabbit muscle, Type XI, lyophilized powder, 600-1,200 units/mg protein
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What are products that only have the quality release date on the COA and do not have an expiration or retest date?
1 answer-
Helpful?
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In the assay, the UV-Vis absorbance at 340 nm is always showing negative. If lactate continues to form over time, shouldn't the absorbance become more positive?
1 answer-
In this assay, the activity of L-Lactic Dehydrogenase is determined by observing the decrease in absorbance at 340 nm for NADH, rather than the formation of NAD+. The method utilizes a continuous spectrophotometric rate determination to monitor the absorbance decrease at 340 nm, corresponding to NADH absorbance.
Helpful?
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is the substrate given for the enzyme lactate or lactic form, and may I know why it is L-lactic dehydrogenase and not L-lactate dehydrogenase?
1 answer-
The terms tend to be used interchangeably. Lactate is the anion of the conjugate base lactic acid.
https://www.sigmaaldrich.com/deepweb/assets/sigmaaldrich/product/documents/216/153/l1254enz.pdfHelpful?
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