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L7016

Sigma-Aldrich

Monoclonal Anti-LDH (H-Subunit) antibody produced in mouse

clone HH-17, ascites fluid

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Synonym(s):
Anti-Lactic Dehydrogenase (H-Subunit)
MDL number:
NACRES:
NA.46

biological source

mouse

Quality Level

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)

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This Item
WH0003945M1SAB5700839L2420
biological source

mouse

biological source

mouse

biological source

rabbit

biological source

mouse

antibody form

ascites fluid

antibody form

purified immunoglobulin

antibody form

affinity isolated antibody

antibody form

purified immunoglobulin

Gene Information

human ... LDHB(3945)

Gene Information

human ... LDHB(3945)

Gene Information

human ... LDHB(3945)

Gene Information

human ... LRP1(4035)
mouse ... Lrp1(16971), Lrp1(299858)

species reactivity

human

species reactivity

human

species reactivity

rat, mouse, human

species reactivity

human, rat, mouse

clone

HH-17, monoclonal

clone

2H6, monoclonal

clone

polyclonal

clone

LRP1-11, monoclonal

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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.

Storage Class

12 - Non Combustible Liquids

wgk_germany

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable


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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
Lactate dehydrogenase-B is silenced by promoter hypermethylation in human prostate cancer
Leiblich A, et al.
Oncogene, 25(20), 2953-2953 (2006)
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)

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