Recombinant Full Length Saccharomyces Cerevisiae Sterol O-Acyltransferase 1(Are1) Protein, His-Tagged
Cat.No. : | RFL33565SF |
Product Overview : | Recombinant Full Length Saccharomyces cerevisiae Sterol O-acyltransferase 1(ARE1) Protein (P25628) (1-610aa), fused to N-terminal His tag, was expressed in E. coli. |
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Source : | E.coli expression system |
Species : | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Tag : | His |
Form : | Lyophilized powder |
Protein length : | Full Length (1-610) |
AA Sequence : | MTETKDLLQDEEFLKIRRLNSAEAN KRHSVTYDNVILPQESMEVSPRSST TSLVEPVEST EGVESTEAERVAGKQEQEEEYPVDA HMQKYLSHLKSKSRSRFHRKDASKY VSFFGDVSFD PRPTLLDSAINVPFQTTFKGPVLEK QLKNLQLTKTKTKATVKTTVKTTEK TDKADAPPGE KLESNFSGIYVFAWMFLGWIAIRCC TDYYASYGSAWNKLEIVQYMTTDLF TIAMLDLAMF LCTFFVVFVHWLVKKRIINWKWTGF VAVSIFELAFIPVTFPIYVYYFDFN WVTRIFLFLH SVVFVMKSHSFAFYNGYLWDIKQEL EYSSKQLQKYKESLSPETREILQKS CDFCLFELNY QTKDNDFPNNISCSNFFMFCLFPVL VYQINYPRTSRIRWRYVLEKVCAII GTIFLMMVTA QFFMHPVAMRCIQFHNTPTFGGWIP ATQEWFHLLFDMIPGFTVLYMLTFY MIWDALLNCV AELTRFADRYFYGDWWNCVSFEEFS RIWNVPVHKFLLRHVYHSSMGALHL SKSQATLFTF FLSAVFHEMAMFAIFRRVRGYLFMF QLSQFVWTALSNTKFLRARPQLSNV VFSFGVCSGP SIIMTLYLTL |
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 : | ARE1 |
Synonyms : | ARE1; SAT2; YCR048W; YCR48W; Sterol O-acyltransferase 1; Sterol-ester synthase 1 |
UniProt ID : | P25628 |
Gene Name : | ARE1 |
Synonyms : | ARE1; SAT2; YCR048W; YCR48W; Sterol O-acyltransferase 1; Sterol-ester synthase 1 |
UniProt ID : | P25628 |
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For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.
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Q&As (19)
Ask a questionYes, there are drugs targeting lipid metabolism that can indirectly affect the activity of the ARE1 protein. For example, statins, which are commonly prescribed for managing hypercholesterolemia, can downregulate the expression of the ARE1 protein. Other medications targeting lipid metabolism, such as fibrates or cholesterol-lowering agents, may also have an impact on the activity or expression of the ARE1 protein.
Yes, there are animal models available for studying the function of the ARE1 protein. For example, knockout mouse models lacking the ARE1 gene have been generated to study the impact of its absence on lipid metabolism and related disorders. These animal models provide valuable insights into the role of the ARE1 protein in vivo.
Yes, the ARE1 protein is considered a potential target for therapeutic intervention in lipid-related disorders. Modulating the activity or expression of the ARE1 protein may help regulate cellular lipid levels and treat conditions like hypercholesterolemia or dyslipidemias.
Yes, genetic variations in the gene encoding the ARE1 protein can impact its function and activity. Single nucleotide polymorphisms (SNPs) or mutations in the ARE1 gene have been shown to influence cholesterol metabolism and may contribute to the development of dyslipidemias or other lipid-related disorders.
Currently, there is no evidence to suggest that the ARE1 protein can serve as a direct biomarker for any specific disease. However, its dysregulation and involvement in lipid metabolism-related disorders make it a potential candidate for further investigation as a biomarker.
Yes, the ARE1 protein is highly conserved across species, indicating its fundamental role in cellular lipid metabolism. Homologs of the ARE1 protein can be found in a wide range of organisms, from yeast to humans, implying its evolutionary significance in maintaining lipid homeostasis.
Currently, no specific diseases or disorders have been directly linked to mutations in the ARE1 gene. However, genetic variations or polymorphisms in the gene have been associated with an increased risk of metabolic disorders, such as dyslipidemia and non-alcoholic fatty liver disease (NAFLD). These variations may influence the function or expression of the protein, contributing to the development of these conditions. Further research is still needed to fully understand the implications of ARE1 gene mutations on human health.
Post-translational modifications (PTMs) of the ARE1 protein can influence its function. Some identified PTMs include phosphorylation, ubiquitination, and palmitoylation. These modifications can regulate its activity, stability, cellular localization, and interactions with other proteins.
The expression of the ARE1 protein is not restricted to a specific tissue but is widely expressed in various tissues and cell types. It is found in tissues that are involved in lipid metabolism, such as the liver, adipose tissue, and intestine, but it is also present in other tissues where it may have additional functions.
Yes, the ARE1 protein has been found to interact with other proteins involved in lipid metabolism. For example, it interacts with Diacylglycerol O-acyltransferase (DGAT) enzymes, which are responsible for triglyceride synthesis. This suggests a coordinated action of these proteins in cellular lipid processing and storage.
Yes, the ARE1 protein can interact with other proteins and molecules to carry out its function in lipid metabolism. It has been found to interact with various enzymes and transporters involved in lipid synthesis, transport, and storage. These interactions help regulate the flow of lipids within cells and ensure proper lipid homeostasis.
Dysregulation or dysfunction of the ARE1 protein can lead to numerous health complications. Excessive ARE1 activity can result in pathological conditions like atherosclerosis, obesity, and metabolic syndrome due to increased cellular lipid accumulation. On the other hand, diminished ARE1 function may impair lipid metabolism and lead to disorders like Tangier disease characterized by low levels of HDL cholesterol.
Targeting the ARE1 protein may hold potential for addressing obesity-related issues. By inhibiting or modulating the activity of ARE1, it may be possible to limit the accumulation of excess lipids and improve obesity-related metabolic dysfunctions. However, further research is needed to explore the efficacy and safety of targeting ARE1 in obesity treatment.
Yes, there are known post-translational modifications of the ARE1 protein. One such modification is phosphorylation, which can affect its activity and subcellular localization. Phosphorylation of the ARE1 protein has been observed in response to certain cellular signals or stress conditions, suggesting a regulatory role for this modification.
There is limited research suggesting a potential role of the ARE1 protein in cancer development. Studies have found altered expression of the ARE1 protein in certain cancer types, but its exact contribution to cancer progression or development is still not fully understood. Further research is needed to explore its involvement in cancer biology.
While the primary function of the ARE1 protein lies in lipid metabolism, it can also have an impact on certain signaling pathways. For instance, studies suggest that ARE1 is involved in the regulation of the mammalian target of rapamycin (mTOR) signaling pathway, which plays a key role in cell growth and metabolism.
Currently, there are no known specific inhibitors or activators that have been identified for the ARE1 protein. However, ongoing research aims to identify small molecules or compounds that can modulate its activity or expression, which could potentially be used as therapeutic agents.
Currently, no specific drugs or inhibitors targeting the ARE1 protein are available for clinical use. However, some studies have explored potential therapeutic strategies, such as small molecule inhibitors, to regulate ARE1 activity and treat conditions associated with dyslipidemia.
Genetic variations in the ARE1 gene, also known as the SLC25A9 gene, have been associated with certain diseases. For example, some variations have been linked to increased risk of developing metabolic disorders like dyslipidemia and non-alcoholic fatty liver disease (NAFLD). These variations may affect the function or expression of the protein, leading to altered lipid metabolism and disease susceptibility.
Customer Reviews (8)
Write a reviewThe use of ARE1 protein in such analyses provides valuable structural insights that contribute to the elucidation of ANO2's functional mechanisms and potential drug targeting sites.
The team has been exceptionally knowledgeable and responsive, promptly addressing any inquiries or issues that have arisen during my work.
Meeting my experimental needs with utmost precision, it has surpassed my expectations.
I highly recommend it to fellow researchers looking for a high-quality protein and excellent technical assistance.
ARE1 protein is highly recommended for researchers due to its excellent performance in various assays, particularly in Western blotting (WB) experiments, and its applicability in protein electron microscopy structure analysis.
ARE1 protein has shown great utility in protein electron microscopy structure analysis.
the technical support provided by the manufacturer is extraordinary.
It enables accurate detection and quantification of ARE1 protein levels in samples, providing crucial insights into its expression, regulation, and potential functional changes under different experimental conditions.
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