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The expression region of this recombinant Human ACLY covers amino acids 4-265. The calculated molecular weight for this ACLY protein is 45.5 kDa. This ACLY protein is produced using e.coli expression system. The N-terminal 6xHis-SUMO tag was fused into the coding gene segment of ACLY, making it easier to detect and purify the ACLY recombinant protein in the later stages of expression and purification.ATP-citrate synthase (ACLY) is an important metabolic enzyme involving lipid metabolism and cellular energy balance. In lipid metabolism, ACLY catalyzes the synthesis of acetyl-coenzyme A and citrate within the cell, critical steps in cholesterol synthesis and fatty acid biogenesis. In recent years, researchers have observed overexpression of ACLY in various cancers, particularly malignant tumors like breast cancer. This suggests its significant role in the onset and progression of cancer. One of the most important areas of research is exploring the mechanisms of ACLY in cancer metabolic reprogramming and its potential application as a drug target. What's more, ACLY is involved in regulating lipid-activated receptors and is associated with metabolic disorders such as diabetes.
The expression region of this recombinant Human ACLY covers amino acids 4-265. The calculated molecular weight for this ACLY protein is 45.5 kDa. This ACLY protein is produced using e.coli expression system. The N-terminal 6xHis-SUMO tag was fused into the coding gene segment of ACLY, making it easier to detect and purify the ACLY recombinant protein in the later stages of expression and purification.ATP-citrate synthase (ACLY) is an important metabolic enzyme involving lipid metabolism and cellular energy balance. In lipid metabolism, ACLY catalyzes the synthesis of acetyl-coenzyme A and citrate within the cell, critical steps in cholesterol synthesis and fatty acid biogenesis. In recent years, researchers have observed overexpression of ACLY in various cancers, particularly malignant tumors like breast cancer. This suggests its significant role in the onset and progression of cancer. One of the most important areas of research is exploring the mechanisms of ACLY in cancer metabolic reprogramming and its potential application as a drug target. What’s more, ACLY is involved in regulating lipid-activated receptors and is associated with metabolic disorders such as diabetes.
| Cat.No | ACP02450 | Target Name | ACLY |
|---|---|---|---|
| Form | Liquid or Lyophilized powder | Expression System | E.coli |
| Expression Range | 4-265aa | Mol Weight | 45.5kDa |
| Protein Length | Partial | Purity | Greater than 90% as determined by SDS-PAGE. |
| Storage Buffer | 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0. |
| Target Species | Human | Uniprot ID | P53396 |
|---|
Uniprot Id
P53396
Target Species
Human
Target Name
ACLY
Target Full Name
ATP-citrate synthase
Target 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.
Target Subcellular Location
Cytoplasm, cytosol.
Target Protein Families
Succinate/malate CoA ligase beta subunit family; Succinate/malate CoA ligase alpha subunit family
Target Research Area
Metabolism
Target Synonyms
ACL; Acly; ACLY_HUMAN; ATP citrate (pro-S) lyase; ATP citrate lyase; ATP citrate synthase; ATP-citrate (pro-S-)-lyase; ATP-citrate synthase; ATPcitrate synthase; ATPCL; Citrate cleavage enzyme; CLATP; OTTHUMP00000164773
Target Background
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. Multiple transcript variants encoding distinct isoforms have been identified for this gene.
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