Analytical Data
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基因名
ACLY
- Application
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别名
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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种属
Human
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表达系统
E. coli
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标签
N-6*His;N-SUMO
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P53396
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表达区间
K4-K265
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氨基酸序列
KAISEQTGKELLYKFICTTSAIQNRFKYARVTPDTDWARLLQDHPWLLSQNLVVKPDQLIKRRGKLGLVGVNLTLDGVKSWLKPRLGQEATVGKATGFLKNFLIEPFVPHSQAEEFYVCIYATREGDYVLFHHEGGVDVGDVDAKAQKLLVGVDEKLNPEDIKKHLLVHAPEDKKEILASFISGLFNFYEDLYFTYLEINPLVVTKDGVYVLDLAAKVDATADYICKVKWGDIEFPPPFGREAYPEEAYIADLDAKSGASLK
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蛋白长度
Partial
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分子量
45.5 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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
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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.
