추천 제품
생물학적 소스
Porcine heart
형태
ammonium sulfate suspension
특이 활성도
≥200 units/mg protein
UniProt 수납 번호
외래 활성
glutamic-oxalacetic transaminase ≤0.1%
malic dehydrogenase, glutamic-pyruvic transaminase and pyruvate kinase ≤0.06%
저장 온도
2-8°C
유전자 정보
pig ... LDHA(407245)
일반 설명
Research area: Cell Signaling
Lactic Dehydrogenase (LDH) is a cytoplasmic enzyme encoded by LDHA, LDHB, LDHC, and LDHD genes, and categorized as an oxidoreductase. It is widely distributed throughout the body, particularly in muscle, liver, and kidney. LDH demonstrates five isomeric forms that form tetramers with two types of subunits: muscle (M) and heart (H).
Lactic Dehydrogenase (LDH) is a cytoplasmic enzyme encoded by LDHA, LDHB, LDHC, and LDHD genes, and categorized as an oxidoreductase. It is widely distributed throughout the body, particularly in muscle, liver, and kidney. LDH demonstrates five isomeric forms that form tetramers with two types of subunits: muscle (M) and heart (H).
애플리케이션
L-Lactic Dehydrogenase from porcine heart has been used:
- as a component of the reaction buffer to measure the GTPase activity of EngA bound to the bacterial 50S subunit to study its structure and function.
- as a component of the enzyme solutions to test the sensitivity of multiphoton NAD(P)H fluorescence lifetime imaging (FLIM) in key enzymatic steps controlling the path of carbon from glucose uptake to electron transport chain (ETC) activity.
생화학적/생리학적 작용
Lactate dehydrogenase (LDH) enzyme is responsible for the conversion of pyruvate to lactate, during glycolysis under hypoxic conditions, while also converting NADH to NAD+. Moreover it acts as a crucial regulator of gluconeogenesis and DNA metabolism. Increased serum LDH levels are detected in conditions such as cancer, HIV infection, muscular dystrophy, megaloblastic anemia, extreme hypothermia, hepatitis, meningitis, hypoxia, etc.
Also catalyzes the oxidation of other L-2-hydroxymonocarboxylic acids.
단위 정의
One unit will reduce 1.0 μmole of pyruvate to L-lactate per min at pH 7.5 at 37 °C.
물리적 형태
Suspension in ammonium sulfate and 0.1 M potassium phosphate, pH 7.0
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)
시험 성적서(COA)
제품의 로트/배치 번호를 입력하여 시험 성적서(COA)을 검색하십시오. 로트 및 배치 번호는 제품 라벨에 있는 ‘로트’ 또는 ‘배치’라는 용어 뒤에서 찾을 수 있습니다.
이미 열람한 고객
Biochemistry, Lactate Dehydrogenase
StatPearls [Internet] (2023)
Clinical Biochemistry and Hematology
Journal of Separation Science, 57-116 (2012)
Scientific reports, 8(1), 5456-5456 (2018-04-05)
While NAD(P)H fluorescence lifetime imaging (FLIM) can detect changes in flux through the TCA cycle and electron transport chain (ETC), it remains unclear whether NAD(P)H FLIM is sensitive to other potential fates of glucose. Glucose carbon can be diverted from
Proceedings of the National Academy of Sciences of the United States of America, 70(7), 1968-1972 (1973-07-01)
The binding of coenzyme and substrate are considered in relation to the known primary and tertiary structure of lactate dehydrogenase (EC 1.1.1.27). The adenine binds in a hydrophobic crevice, and the two coenzyme phosphates are oriented by interactions with the
Hoppe-Seyler's Zeitschrift fur physiologische Chemie, 360(7), 795-807 (1979-07-01)
Lactate dehydrogenases from thermophilic bacilli (Bacillus stearothermophilus, Bacillus caldotenax) and from mesophilic bacilli (Bacillus X1, Bacillus subtilis) have been isolated by a two-step purification procedure. Only one type (LDH-P4) composed of four identical subunits (Mr 34 000 or 36 000)
문서
Instructions for working with enzymes supplied as ammonium sulfate suspensions
프로토콜
This procedure applies to all products from heart muscle that have a specification for L-Lactic Dehydrogenase activity.
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