Recombinant Full Length Saccharomyces Cerevisiae Sterol O-Acyltransferase 2(Are2) Protein, His-Tagged

• Cat.No.: RFL13192SF
• Product Overview: Recombinant Full Length Saccharomyces cerevisiae Sterol O-acyltransferase 2(ARE2) Protein (P53629) (1-642aa), fused to N-terminal His tag, was expressed in E. coli.

Specification

• Source: E.coli expression system
• Species: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
• Tag: His
• Form: Lyophilized powder
• Protein length: Full Length (1-642)
• AA Sequence: MDKKKDLLENEQFLRIQKLNAADAG KRQSITVDDEGELYGLDTSGNSPAN EHTATTITQN HSVVASNGDVAFIPGTATEGNTEIV TEEVIETDDNMFKTHVKTLSSKEKA RYRQGSSNFI SYFDDMSFEHRPSILDGSVNEPFKT KFVGPTLEKEIRRREKELMAMRKNL HHRKSSPDAV DSVGKNDGAAPTTVPTAATSETVVT VETTIISSNFSGLYVAFWMAIAFGA VKALIDYYYQ HNGSFKDSEILKFMTTNLFTVASVD LLMYLSTYFVVGIQYLCKWGVLKWG TTGWIFTSIY EFLFVIFYMYLTENILKLHWLSKIF LFLHSLVLLMKMHSFAFYNGYLWGI KEELQFSKSA LAKYKDSINDPKVIGALEKSCEFCS FELSSQSLSDQTQKFPNNISAKSFF WFTMFPTLIY QIEYPRTKEIRWSYVLEKICAIFGT IFLMMIDAQILMYPVAMRALAVRNS EWTGILDRLL KWVGLLVDIVPGFIVMYILDFYLIW DAILNCVAELTRFGDRYFYGDWWNC VSWADFSRIW NIPVHKFLLRHVYHSSMSSFKLNKS QATLMTFFLSSVVHELAMYVIFKKL RFYLFFFQML QMPLVALTNTKFMRNRTIIGNVIFW LGICMGPSVMCTLYLTF
• Purity: Greater than 90% as determined by SDS-PAGE.
• Applications: SDS-PAGE
• Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
• Storage: Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
• Storage Buffer: Tris/PBS-based buffer, 6% Trehalose, pH 8.0
• Reconstitution: We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
• Gene Name: ARE2
• Synonyms: ARE2; SAT1; YNR019W; N3206; Sterol O-acyltransferase 2; Sterol-ester synthase 2
• UniProt ID: P53629

Gene Information

• Gene Name: ARE2
• Synonyms: ARE2; SAT1; YNR019W; N3206; Sterol O-acyltransferase 2; Sterol-ester synthase 2
• UniProt ID: P53629

Reviews

11/22/2022

Its reliability and versatility make it an essential tool for investigating ARE2 protein's expression, function, and structural characteristics.

10/14/2021

Whether in Western blotting, immunoprecipitation, or other applications, the ARE2 Protein consistently delivers outstanding performance.

11/17/2020

ARE2 protein is highly recommended for researchers due to its excellent performance in WB experiments and its utility in protein electron microscopy structure analysis.

09/08/2019

With their assistance, I have been able to maximize the potential of the ARE2 Protein and achieve even better results.

04/03/2019

Their expertise and dedication have greatly assisted in solving problems and optimizing experimental protocols.

10/24/2018

By visualizing the structural features, interactions, and conformational changes of ARE2, researchers gain valuable insights into its function and potential for therapeutic interventions.

09/08/2018

I am thrilled to express my satisfaction with the ARE2 Protein, as it has consistently proven to be of outstanding quality and entirely suited to meet my experimental needs.

04/15/2016

The use of ARE2 protein in this technique allows researchers to explore the intricate three-dimensional structure of the protein at a molecular level.

Q&As

Are there any drugs or therapeutic strategies being developed to target the ARE2 protein?

Currently, there are no specific drugs or therapeutic strategies being developed to directly target the ARE2 protein. However, there is ongoing research and drug development efforts focused on addressing metabolic disorders associated with impaired fatty acid oxidation. These approaches include the development of enzyme replacement therapies, gene therapies, and small molecule compounds that indirectly improve fatty acid oxidation and mitochondrial function.

How is the ARE2 protein involved in the metabolism of fatty acids?

The ARE2 protein plays a crucial role in the metabolism of long-chain fatty acids. It is an enzyme located in the mitochondrial inner membrane and is responsible for the transport of long-chain acylcarnitine molecules into the mitochondria for subsequent beta-oxidation.

Is the expression of the ARE2 gene regulated by any specific factors or signaling pathways?

The expression of the ARE2 gene can be regulated by various factors and signaling pathways. For example, peroxisome proliferator-activated receptors (PPARs), which play a role in lipid metabolism, can bind to specific DNA sequences in the gene's promoter region and regulate its transcription. Additionally, certain cellular signals and hormonal cues can influence the expression of the ARE2 gene.

Are there any known inhibitors or activators of the ARE2 protein?

Currently, there are no specific inhibitors or activators identified specifically for the ARE2 protein. However, drugs that target fatty acid metabolism or mitochondrial function may indirectly affect the activity of ARE2.

Are there any known genetic variations in the ARE2 gene that are associated with diseases or disorders?

Yes, mutations in the ARE2 gene can lead to a rare metabolic disorder called carnitine-acylcarnitine translocase deficiency (CACT deficiency). This condition impairs the transport of long-chain fatty acids into the mitochondria, disrupting fatty acid beta-oxidation and causing symptoms such as muscle weakness, liver dysfunction, and hypoglycemia.

Can the ARE2 protein interact with other proteins or molecules?

Yes, the ARE2 protein interacts with other proteins to carry out its function. It forms a complex with carnitine palmitoyltransferase 1 (CPT1), which catalyzes the conversion of long-chain fatty acids to acyl-CoA for transport into the mitochondria. The interaction between ARE2 and CPT1 facilitates the transfer of fatty acids across the mitochondrial membrane.

Is there any ongoing research or clinical trials related to the ARE2 protein?

Currently, there is ongoing research focused on understanding the role of the ARE2 protein in various metabolic disorders. Scientists are investigating potential therapeutic approaches to treat CACT deficiency and exploring the involvement of the ARE2 protein in the development of metabolic diseases. Clinical trials related to the ARE2 protein could be conducted in the future to evaluate potential therapies targeting fatty acid oxidation disorders.

Is the expression of the ARE2 gene influenced by nutritional status?

Yes, the expression of the ARE2 gene can be influenced by nutritional status. During periods of fasting or low glucose availability, the expression of the ARE2 gene is upregulated to enhance fatty acid oxidation as an energy source. In contrast, high glucose or insulin levels can downregulate the expression of ARE2.

Does the ARE2 protein have any tissue-specific expression?

Yes, the expression of the ARE2 gene is predominantly observed in tissues with high energy demands, such as the liver, heart, and skeletal muscle. These tissues require efficient fatty acid metabolism for energy production, thus requiring the presence of the ARE2 protein.

How is the expression of the ARE2 gene regulated at the molecular level?

The expression of the ARE2 gene is regulated by various transcription factors and signaling pathways. One of the key regulators of the ARE2 gene is the peroxisome proliferator-activated receptor alpha (PPARα). PPARα binds to specific DNA sequences called peroxisome proliferator response elements (PPREs) in the promoter region of the ARE2 gene, leading to its activation.

Are there any known natural or synthetic compounds that can modulate the activity of the ARE2 protein?

While there are no specific compounds known to modulate the activity of the ARE2 protein, certain fatty acids and their derivatives, such as acylcarnitines, can indirectly affect the function of ARE2. Additionally, compounds that target general fatty acid metabolism or mitochondrial function may have an impact on the activity of ARE2. Further research is needed to explore specific modulators for the ARE2 protein.

Are there any known genetic variants or polymorphisms in the ARE2 gene associated with human diseases?

There are currently no known genetic variants or polymorphisms in the ARE2 gene directly associated with human diseases. However, mutations in the genes encoding other proteins involved in fatty acid oxidation can indirectly affect the activity of ARE2 and contribute to metabolic disorders.

Does loss or dysfunction of the ARE2 protein have any implications for human health or disease?

Yes, loss or dysfunction of the ARE2 protein can have significant implications for human health. Mutations in the ARE2 gene, causing CACT deficiency, can lead to metabolic disorders characterized by severe hypoglycemia, muscle weakness, liver dysfunction, and cardiomyopathy. Furthermore, impaired fatty acid oxidation due to ARE2 dysfunction can contribute to various metabolic diseases such as obesity, diabetes, and cardiovascular disorders.