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Aldehyde Dehydrogenase Polyclonal Antiserum

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    Aldehyde Dehydrogenase Polyclonal Antiserum
  • Aldehyde Dehydrogenase Polyclonal Antiserum
Cat No: 160720
Cayman

Aldehyde dehydrogenase (ALDH) is an enzyme that catalyzes the oxidation of various aldehydes to their corresponding carboxylic acid.{60733} There are 19 human ALDH isozymes, which have varying expression levels, subcellular localization, tissue distri...

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Territorial Availability: Available through Bertin Technologies only in France
Correlated keywords:
  • Western blots blotting erythrocyte thromboxanes antisera antibodies antiserum WB atherosclerosis immunoblotting
Product Overview:
Aldehyde dehydrogenase (ALDH) is an enzyme that catalyzes the oxidation of various aldehydes to their corresponding carboxylic acid.{60733} There are 19 human ALDH isozymes, which have varying expression levels, subcellular localization, tissue distribution, cofactor preference, and substrate specificity.{60734} ALDH exists as a homodimer or homotetramer and is composed of a cofactor-binding domain, which binds NAD+ or NADP+, a catalytic domain, and an oligomerization domain. ALDH has protective roles in alcohol detoxification and oxidative stress, regulatory roles in the function of normal stem cells and tumor-initiating stem-like cells, and a biosynthetic role in the formation of retinoic acid.{60734,60733} It also catalyzes the catabolism of thromboxane B2 (TXB2; Item No. 19030) to 11-dehydro TXB2 (Item No. 19500).{20448} Mutations in the genes encoding ALDH isozymes are associated with a variety of human conditions, including alcohol intolerance, Parkinson's disease, and gout.{60733} Cayman's Aldehyde Dehydrogenase Polyclonal Antiserum can be used for Western blot (WB) applications. The antibody recognizes ALDH at 55 kDa from human and mouse samples.
Size 1 ea
Shipping dry ice
Host Rabbit
Antigen Human erythrocyte ALDH
Application(s)

WB

Formulation Polyclonal antiserum
Custom Code 3822.19
UNSPSC code 12352203

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Cayman Chemical's mission is to help make research possible by supplying scientists worldwide with the basic research tools necessary for advancing human and animal health. Our utmost commitment to healthcare researchers is to offer the highest quality products with an affordable pricing policy.

Our scientists are experts in the synthesis, purification, and characterization of biochemicals ranging from small drug-like heterocycles to complex biolipids, fatty acids, and many others. We are also highly skilled in all aspects of assay and antibody development, protein expression, crystallization, and structure determination.

Over the past thirty years, Cayman developed a deep knowledge base in lipid biochemistry, including research involving the arachidonic acid cascade, inositol phosphates, and cannabinoids. This knowledge enabled the production of reagents of exceptional quality for cancer, oxidative injury, epigenetics, neuroscience, inflammation, metabolism, and many additional lines of research.

Our organic and analytical chemists specialize in the rapid development of manufacturing processes and analytical methods to carry out clinical and commercial GMP-API production. Pre-clinical drug discovery efforts are currently underway in the areas of bone restoration and repair, muscular dystrophy, oncology, and inflammation. A separate group of Ph.D.-level scientists are dedicated to offering Hit-to-Lead Discovery and Profiling Services for epigenetic targets. Our knowledgeable chemists can be contracted to perform complete sample analysis for analytes measured by the majority of our assays. We also offer a wide range of analytical services using LC-MS/MS, HPLC, GC, and many other techniques.

Accreditations
ISO/IEC 17025:2005
ISO Guide 34:2009

Cayman is a leader in the field of emerging drugs of abuse, providing high-purity Schedule I-V Controlled Substances to federally-licensed laboratories and qualified academic research institutions for forensic analyses. We are certified by ACLASS Accreditation Services with dual accreditation to ISO/IEC 17025:2005 and ISO Guide 34:2009.

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