Abcam, ab202652, Alexa Fluor® 488 Anti-Lactate Dehydrogenase antibody [EP1566Y]

Size: 100µL
Rabbit Recombinant Monoclonal L-lactate dehydrogenase B antibody - conjugated to Alexa Fluor® 488. Suitable for ICC/IF and reacts with Human samples. Cited in 2 publications.
Key facts
Host species:Rabbit,
Clonality:Monoclonal,
Clone number:EP1566Y,
Isotype:IgG,
Conjugation:Alexa Fluor® 488,
Excitation/Emission:Ex: 495nm, Em: 519nm,
Carrier free:No,
Reacts with:Human,
Applications:ICC/IFSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Immunogen:The exact immunogen used to generate this antibody is proprietary information.,
Specificity:This antibody reacts with Lactate dehydrogenase; LDHA (79%), LDHB (100%) and LDHC (86%) based on the sequence homology with the immunogen.

Product details:
Patented technology
Our RabMAb
technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to
RabMAb® patents
Alexa Fluor® is a registered trademark of Molecular Probes, Inc, a Thermo Fisher Scientific Company. The Alexa Fluor® dye included in this product is provided under an intellectual property license from Life Technologies Corporation. As this product contains the Alexa Fluor® dye, the purchase of this product conveys to the buyer the non-transferable right to use the purchased product and components of the product only in research conducted by the buyer (whether the buyer is an academic or for-profit entity). As this product contains the Alexa Fluor® dye the sale of this product is expressly conditioned on the buyer not using the product or its components, or any materials made using the product or its components, in any activity to generate revenue, which may include, but is not limited to use of the product or its components: in manufacturing; (ii) to provide a service, information, or data in return for payment (iii) for therapeutic, diagnostic or prophylactic purposes; or (iv) for resale, regardless of whether they are sold for use in research. For information on purchasing a license to this product for purposes other than research, contact Life Technologies Corporation, 5781 Van Allen Way, Carlsbad, CA 92008 USA or outlicensing@thermofisher.com.

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Protein A, Storage buffer-pH: 7.4Preservative: 0.02% Sodium azideConstituents: PBS, 30% Glycerol (glycerin, glycerine), 1% BSA, Shipped at conditions-Blue Ice, Appropriate short-term storage duration-1-2 weeks, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions--20°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle, Store in the dark

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Lactate dehydrogenase (LDH) is an enzyme that catalyzes the interconversion of pyruvate and lactate along with the conversion of NADH to NAD+. LDH is known by other names such as lactic acid dehydrogenase and LDH-5. The enzyme has a molecular weight of approximately 36 kDa. LDH exists in almost all tissues having multiple isoforms that are expressed differently depending on the tissue type. It shows high expression in muscle tissue liver and heart indicating its extensive role in energy metabolism.
Biological function summary
Lactate dehydrogenase plays a critical role in anaerobic glycolysis. The enzyme helps in regenerating NAD+ from NADH allowing glycolysis to continue in the absence of oxygen. LDH is not a part of any larger protein complex working independently to fulfill its function in the glycolytic pathway. It serves in rapid energy production especially under hypoxic or exertional conditions where oxygen supply is limited.
Pathways
LDH is significantly involved in the glycolysis and gluconeogenesis pathways. Within glycolysis LDH helps facilitate the conversion of pyruvate to lactate during anaerobic conditions a step important for ATP production when oxygen is scarce. The enzyme is tied closely to phosphofructokinase-1 (PFK-1) in glycolysis given that both enzymes are central to maintaining the glycolytic flow. In gluconeogenesis though functionally reversed from its role in glycolysis LDH helps to manage lactate removal an important step for glucose synthesis from non-carbohydrate sources.
Lactate dehydrogenase levels often act as a biomarker for tissue damage or certain cancers as its release into the bloodstream signals cellular injury or death. Elevated LDH levels are associated with conditions like myocardial infarction and certain forms of anemia. In cancer such as lymphoma or leukemia LDH correlates with the progression of the disease and acts as a prognostic marker. LDH's connection to these conditions often leads to insights into disease severity and progression due to its association with proteins like p53 and HIF-1 which play roles in cellular metabolism and hypoxia response.