Analytical Data
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Gene name
ACLY
- Application
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Alternative Names
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
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Species
Human
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Source
E. coli
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Tag
N-6*His;N-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P53396
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Expression Region
K4-K265
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AA Sequence
KAISEQTGKELLYKFICTTSAIQNRFKYARVTPDTDWARLLQDHPWLLSQNLVVKPDQLIKRRGKLGLVGVNLTLDGVKSWLKPRLGQEATVGKATGFLKNFLIEPFVPHSQAEEFYVCIYATREGDYVLFHHEGGVDVGDVDAKAQKLLVGVDEKLNPEDIKKHLLVHAPEDKKEILASFISGLFNFYEDLYFTYLEINPLVVTKDGVYVLDLAAKVDATADYICKVKWGDIEFPPPFGREAYPEEAYIADLDAKSGASLK
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Protein Length
Partial
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Molecular Weight
45.5 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Acetyl-CoA lyase (ACLY) is an important enzyme involved in cellular metabolism, particularly in the conversion of citrate into acetyl-CoA and oxaloacetate, linking carbohydrate metabolism to lipid synthesis. It has garnered significant interest due to its role in various metabolic pathways and its potential implications in diseases such as cancer, obesity, and metabolic disorders. Research has shown that ACLY activity is often upregulated in tumor cells, facilitating anabolic processes necessary for uncontrolled cell proliferation. Consequently, ACLY has emerged as a promising therapeutic target for cancer treatment. Efforts to study ACLY have led to the development of recombinant protein techniques to produce and purify this enzyme, enabling detailed biochemical and structural characterization. The recombinant ACLY provides valuable insights into its enzymatic mechanisms, substrate specificity, and regulation, as well as the development of inhibitors that could potentially serve as novel anti-cancer agents. Furthermore, understanding the structure-function relationship of ACLY can assist in uncovering its regulatory mechanisms and influence on metabolic pathways, ultimately contributing to the design of targeted interventions in metabolic diseases. This research highlights the significance of ACLY in metabolic regulation and its potential as a target in therapeutic development, setting the stage for further exploration into its role in health and disease.
