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L1254
L-Lactic Dehydrogenase from rabbit muscle
Type XI, lyophilized powder, 600-1,200 units/mg protein
Sinonimo/i:
Anaerobic Lactate Dehydrogenase, Lactate, NAD-lactate dehydrogenase, (S)-Lactate: NAD+ oxidoreductase, L-LDH, LAD, LD
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About This Item
Prezzi e disponibilità al momento non sono disponibili
Prodotti consigliati
Origine biologica
rabbit muscle
Tipo
Type XI
Stato
lyophilized powder
Attività specifica
600-1,200 units/mg protein
PM
140 kDa
Composizione
protein, 90-100%
Condizioni di stoccaggio
(Keep container tightly closed in a dry and well-ventilated place)
tecniche
activity assay: suitable
Colore
white
Attività estranea
pyruvate kinase, myokinase, malic dehydrogenase, glutamic-pyruvic transaminase, glutamic-oxalacetic transaminase and α-glycerophosphate dehydrogenase ≤0.01%
Temperatura di conservazione
−20°C
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Descrizione generale
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 .
Applicazioni
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]
Azioni biochim/fisiol
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.
Definizione di unità
One unit will reduce 1.0 μmole of pyruvate to L-lactate per min at pH 7.5 at 37 °C.
Risultati analitici
Protein determined by biuret.
Anticorpo
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N° Catalogo
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Avvertenze
Danger
Indicazioni di pericolo
Consigli di prudenza
Classi di pericolo
Resp. Sens. 1
Codice della classe di stoccaggio
11 - Combustible Solids
Classe di pericolosità dell'acqua (WGK)
WGK 1
Dispositivi di protezione individuale
Eyeshields, Gloves, type N95 (US)
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Certificati d'analisi (COA)
Lot/Batch Number
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I clienti hanno visto anche
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
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Articoli
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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