L7016
Monoclonal Anti-LDH (H-Subunit) antibody produced in mouse
clone HH-17, ascites fluid
Synonym(s):
Anti-Lactic Dehydrogenase (H-Subunit)
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About This Item
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biological source
mouse
conjugate
unconjugated
antibody form
ascites fluid
antibody product type
primary antibodies
clone
HH-17, monoclonal
contains
15 mM sodium azide
species reactivity
human
technique(s)
indirect ELISA: 1:5,000
isotype
IgG1
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... LDHB(3945)
General description
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
Application
Monoclonal Anti-LDH (H-Subunit) antibody produced in mouse has been used in:
- immunoblotting†
- immunohistochemistry
- microscopy
Biochem/physiol Actions
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.
Disclaimer
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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Storage Class
12 - Non Combustible Liquids
wgk_germany
nwg
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Disarmed anthrax toxin delivers antisense oligonucleotides and siRNA with high efficiency and low toxicity
Dyer PDR, et al.
Journal of Controlled Release : Official Journal of the Controlled Release Society, 220, 316-328 (2015)
NAD-dependent lactate dehydrogenase catalyses the first step in respiratory utilization of lactate by Lactococcus lactis
Zhao R, et al.
FEBS Open Bio, 3, 379-386 (2013)
Andrei Seluanov et al.
DNA repair, 6(12), 1740-1748 (2007-08-10)
Aging is associated with accumulation of genomic rearrangements consistent with aberrant repair of DNA breaks. We have shown previously that DNA repair by non-homologous end joining (NHEJ) becomes less efficient and more error-prone in senescent cells. Here, we show that
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)
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
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