추천 제품
생물학적 소스
rabbit muscle
Quality Level
유형
Type XI
양식
lyophilized powder
특이 활성도
600-1,200 units/mg protein
분자량
140 kDa
구성
protein, 90-100%
저장 조건
(Keep container tightly closed in a dry and well-ventilated place)
기술
activity assay: suitable
색상
white
외래 활성
pyruvate kinase, myokinase, malic dehydrogenase, glutamic-pyruvic transaminase, glutamic-oxalacetic transaminase and α-glycerophosphate dehydrogenase ≤0.01%
저장 온도
−20°C
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일반 설명
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 .
애플리케이션
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
- in Trypanosoma congolense pyruvate kinase activity assay
- in pyruvate kinase (PK) assay with rice plastidic PK enzyme OsPK2
생화학적/생리학적 작용
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. 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.
단위 정의
One unit will reduce 1.0 μmole of pyruvate to L-lactate per min at pH 7.5 at 37 °C.
분석 메모
Protein determined by biuret.
관련 제품
저해제
제품 번호
설명
가격
항체
효소
제품 번호
설명
가격
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)
가장 최신 버전 중 하나를 선택하세요:
시험 성적서(COA)
Lot/Batch Number
이미 열람한 고객
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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문서
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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