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BRAND / VENDOR: Abcam

Abcam, ab227996, Anti-ATP citrate lyase antibody [EP704Y] - BSA and Azide free

CATALOG NUMBER: ab227996
Regular price$0.99
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Product Description

Size: 100µg / 1mg
Rabbit Recombinant Monoclonal ATP citrate lyase antibody. Carrier free. Suitable for IP, WB, IHC-P, ICC/IF, Flow Cyt (Intra) and reacts with Human, Mouse, Rat samples. Cited in 14 publications.
Key facts
Host species:Rabbit,
Clonality:Monoclonal,
Clone number:EP704Y,
Isotype:IgG,
Carrier free:Yes,
Reacts with:Mouse, Rat, Human,
Applications:IHC-P, IP, Flow Cyt (Intra), ICC/IF, WBSee 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 recognises ATP citrate lyase (ACL). The mouse and rat recommendation is based on the WB results. We do not guarantee IHC-P for mouse and rat.

Product details:
ab227996 is the carrier-free version of
ab40793
Conjugation ready
Our carrier-free antibodies are typically supplied in a PBS-only formulation, purified and free of BSA, sodium azide and glycerol. This conjugation-ready format is designed for use with fluorochromes, metal isotopes, oligonucleotides, and enzymes, which makes them ideal for antibody labelling, functional and cell-based assays, flow-based assays (e.g. mass cytometry) and Multiplex Imaging applications.
Use our
conjugation kits
for antibody conjugates that are ready-to-use in as little as 20 minutes with 1 minute hands-on-time and 100% antibody recovery: available for fluorescent dyes, HRP, biotin and gold.
Compatibility
This product is compatible with the Maxpar
Antibody Labeling Kit from Fluidigm, without the need for antibody preparation. Maxpar
is a trademark of Fluidigm Canada Inc.

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Protein A, Storage buffer-pH: 7.2 - 7.4Constituents: PBS, Shipped at conditions-Blue Ice, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions-+4°C, Storage information-Do Not Freeze

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
ATP citrate lyase (ACL ACLY) is an enzyme responsible for converting citrate and coenzyme A into acetyl-CoA and oxaloacetate using ATP in the process. This reaction is key for lipid and cholesterol biosynthesis. ACLY's alternate name is ATP citrate (pro-S)-lyase and it has a molecular weight of approximately 120 kDa. The enzyme is expressed mainly in the cytoplasm with substantial amounts found in liver and adipose tissues.
Biological function summary
ATP citrate lyase plays an important role in lipid metabolism and energy production. It drives the conversion of citrate-derived acetyl-CoA a central metabolite in lipogenesis providing substrates for fatty acid and cholesterol synthesis. ACLY functions as a homotetramer complex to facilitate its enzymatic activity. This mechanism supports energy homeostasis linking carbohydrate metabolism with lipid biosynthesis.
Pathways
The enzyme ATP citrate lyase is instrumental in the citric acid cycle and fatty acid synthesis pathways. It is a central player in the cholesterol biosynthesis pathway which tightly connects to acetyl-CoA and citrate shuttle processes. In these pathways it interacts functionally with other enzymes such as acetyl-CoA carboxylase which further processes acetyl-CoA into malonyl-CoA serving as a precursor for fatty acid elongation.
ATP citrate lyase becomes significant in metabolic syndrome and cancer. Elevated expression and activity are linked to an increased risk of metabolic diseases including obesity and type 2 diabetes due to its role in excessive lipid accumulation. Moreover cancer cells often exhibit upregulated ACLY activity encouraging tumor growth by supplying acetyl-CoA for lipid biosynthesis. Its activity is intricately linked to proteins such as fatty acid synthase which also contribute to altered lipid profiles in these conditions.


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Collaboration

Tony Tang

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