ACLY Antibody
Purified Mouse Monoclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application ![]()
| WB, IHC, FC, ICC, E |
---|---|
Primary Accession | P53396 |
Reactivity | Human, Mouse, Rat, Monkey |
Host | Mouse |
Clonality | Monoclonal |
Clone Names | 5F8D11 |
Isotype | IgG1 |
Calculated MW | 125kDa |
Description | ATP citrate lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. The enzyme is a tetramer (relative molecular weight approximately 440,000) of apparently identical subunits. It catalyzes the formation of acetyl-CoA and oxaloacetate from citrate and CoA with a concomitant hydrolysis of ATP to ADP and phosphate. The product, acetyl-CoA, serves several important biosynthetic pathways, including lipogenesis and cholesterogenesis. In nervous tissue, ATP citrate-lyase may be involved in the biosynthesis of acetylcholine. Two transcript variants encoding distinct isoforms have been identified for this gene. |
Immunogen | Purified recombinant fragment of human ACLY (AA: 306-502 ) expressed in E. Coli. |
Formulation | Purified antibody in PBS with 0.05% sodium azide |
Gene ID | 47 |
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Other Names | ATP-citrate synthase, 2.3.3.8, ATP-citrate (pro-S-)-lyase, ACL, Citrate cleavage enzyme, ACLY |
Dilution | E~~1/10000 WB~~1/500 - 1/2000 IF~~1/50 FC~~1/200 - 1/400 IHC~~1/200 - 1/1000 |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | ACLY Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | ACLY |
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Function | Catalyzes the cleavage of citrate into oxaloacetate and acetyl-CoA, the latter serving as common substrate for de novo cholesterol and fatty acid synthesis. |
Cellular Location | Cytoplasm, cytosol. |

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Provided below are standard protocols that you may find useful for product applications.
References
1.J Biol Chem. 2010 Oct 15;285(42):32606-15. 2.Int J Cancer. 2010 May 15;126(10):2282-95.

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