L7016
Monoclonal Anti-LDH (H-Subunit) antibody produced in mouse
clone HH-17, ascites fluid
Synonim(y):
Anti-Lactic Dehydrogenase (H-Subunit)
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About This Item
pochodzenie biologiczne
mouse
białko sprzężone
unconjugated
forma przeciwciała
ascites fluid
rodzaj przeciwciała
primary antibodies
klon
HH-17, monoclonal
zawiera
15 mM sodium azide
reaktywność gatunkowa
human
metody
indirect ELISA: 1:5,000
izotyp
IgG1
numer dostępu UniProt
Warunki transportu
dry ice
temp. przechowywania
−20°C
docelowa modyfikacja potranslacyjna
unmodified
informacje o genach
human ... LDHB(3945)
Opis ogólny
Lactate dehydrogenase (LDH) is an NADH-dependent enzyme that catalyzes the reversible conversion of pyruvate to lactate. Human LDH has two known isoforms, the H isoform which is primarily found in heart tissues and the M isoform that occurs mostly in muscle tissues.
Monoclonal Anti-LDH (H-Subunit) (mouse IgG1 isotype) is derived from the hybridoma produced by the fusion of mouse myeloma cells and splenocytes from an immunized mouse.
Immunogen
Human LDH-H4 isoenzyme
Zastosowanie
Monoclonal Anti-LDH (H-Subunit) antibody produced in mouse has been used in:
- immunoblotting†
- immunohistochemistry
- microscopy
Działania biochem./fizjol.
Lactate dehydrogenase (LDH) is an NADH-dependent enzyme that catalyzes the reversible conversion of pyruvate to lactate.
Lactate dehydrogenase (LDH) is an NADH-dependent enzyme that catalyzes the reversible conversion of pyruvate to lactate. Human LDH has two known isoforms, the H isoform which is primarily found in heart tissues and the M isoform that occurs mostly in muscle tissues . Ratio of LDH isozymes H4 and H3M can be used as diagnostic and prognostic markers of myocardial infarction . Monoclonal Anti-Human Lactate Dehydrogenase is specific for human LDH isozymes containing the H-subunit. The antibody does not cross-react with the M4 isozyme.
Oświadczenie o zrzeczeniu się odpowiedzialności
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Kod klasy składowania
12 - Non Combustible Liquids
Klasa zagrożenia wodnego (WGK)
nwg
Temperatura zapłonu (°F)
Not applicable
Temperatura zapłonu (°C)
Not applicable
Certyfikaty analizy (CoA)
Poszukaj Certyfikaty analizy (CoA), wpisując numer partii/serii produktów. Numery serii i partii można znaleźć na etykiecie produktu po słowach „seria” lub „partia”.
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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.
Lactate dehydrogenase-B is silenced by promoter hypermethylation in human prostate cancer
Leiblich A, et al.
Oncogene, 25(20), 2953-2953 (2006)
N R Acharya et al.
Advances in myocardiology, 2, 407-414 (1980-01-01)
The isozyme profile of lactic dehydrogenase (LDH) is being studied in this laboratory, mainly for the diagnosis in the suspected cases of myocardial infarction (MI). The isozymes are separated by polyacrylamide gel electrophoresis and the quantitative assay of the isoenzymes
Takeshi Hashimoto et al.
PloS one, 3(8), e2915-e2915 (2008-08-14)
To evaluate the presence of components of a putative Intracellular Lactate Shuttle (ILS) in neurons, we attempted to determine if monocarboxylate (e.g. lactate) transporter isoforms (MCT1 and -2) and lactate dehydrogenase (LDH) are coexpressed in neuronal mitochondria of rat brains.
Decreased lactate dehydrogenase B expression enhances claudin 1-mediated hepatoma cell invasiveness via mitochondrial defects
Kim JH, et al.
Experimental Cell Research, 317(8), 1108-1118 (2011)
Sirtuin 1 (SIRT1) deacetylase activity is not required for mitochondrial biogenesis or peroxisome proliferator-activated receptor-gamma coactivator-1alpha (PGC-1alpha) deacetylation following endurance exercise
Philp A, et al.
The Journal of Biological Chemistry, 286(35), 30561-30570 (2011)
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