Recombinant Human AES protein, GST-tagged
Cat.No. : | AES-301324H |
Product Overview : | Recombinant Human AES (1-81 aa) protein, fused to GST tag, was expressed in E. coli. |
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Source : | E. coli |
Species : | Human |
Tag : | GST |
Form : | The purified protein was Lyophilized from sterile PBS (58mM Na2HPO4,17mM NaH2PO4, 68mM NaCl, pH8.). 5 % trehalose and 5 % mannitol are added as protectant before lyophilization. |
Protein length : | Met1-Leu81 |
AA Sequence : | MCHKNGFPQEGGITAAFLQKRKLRL SKNHRPARAKVTEHVRGTRPGRATA GPAASTRAAGSLFFDRWGNRGPAGC RGSSHL |
Purity : | 85%, by SDS-PAGE with Coomassie Brilliant Blue staining. |
Stability : | Store for up to 12 months at -20°C to -80°C as lyophilized powder. |
Storage : | Short-term storage: Store at 2-8°C for (1-2 weeks). Long-term storage: Aliquot and store at -20°C to -80°C for up to 3 months, buffer containing 50% glycerol is recommended for reconstitution. Avoid repeat freeze-thaw cycles. |
Gene Name : | AES amino-terminal enhancer of split [ Homo sapiens ] |
Official Symbol : | AES |
Synonyms : | AES; amino-terminal enhancer of split; GRG5; TLE5; gp130-associated protein GAM; GRG; ESP1; AES-1; AES-2; |
Gene ID : | 166 |
mRNA Refseq : | NM_001130 |
Protein Refseq : | NP_001121 |
MIM : | 600188 |
UniProt ID : | Q08117 |
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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 (10)
Ask a questionPost-translational modifications, such as phosphorylation or acetylation, and regulatory factors can modulate the activity or stability of AES protein, influencing its function in gene regulation and cellular processes.
Experimental techniques such as gene expression analysis, chromatin immunoprecipitation, or functional genomics approaches have been employed to investigate the functional significance of AES protein in gene regulation and cellular processes.
AES protein could be a potential pharmacological target to modulate gene expression, cellular processes, or serve as a therapeutic target for diseases associated with dysregulated gene expression or abnormal cell growth. Further research is needed to explore its therapeutic potential and develop targeted interventions.
Dysregulation or dysfunction of AES protein can disrupt cellular functions, developmental processes, and contribute to disease development, such as cancer, neurodegenerative disorders, or developmental disorders.
The cellular and subcellular localization patterns of AES protein can vary across different cell types and developmental stages. Experimental techniques such as immunofluorescence microscopy or subcellular fractionation can be used to determine its localization.
The expression of AES protein is regulated at the transcriptional level by specific promoters and transcription factors. Cellular signaling pathways and environmental cues can influence its expression in a context-dependent manner.
Genetic variations or mutations in the AES gene may impact the expression or function of AES protein, potentially leading to dysregulated gene expression, altered cellular processes, or disease susceptibility.
AES protein may interact with specific molecules, such as transcription factors or chromatin modifiers, forming protein complexes that modulate gene expression and cellular processes.
AES protein modulates gene expression and transcriptional activity by interacting with transcriptional regulators, co-repressors, or chromatin remodeling complexes, potentially leading to transcriptional repression or modulation of target genes.
AES protein plays a role in cellular processes such as cell proliferation, differentiation, or apoptosis, potentially through its interactions with transcription factors or modulation of gene expression. Experimental approaches including loss-of-function studies or functional assays can assess its function.
Customer Reviews (3)
Write a reviewUnderstanding protein-protein interaction networks in oxidative stress responses.
Detecting protein-protein interactions in ion transport and homeostasis.
Exploring protein-protein interactions involved in cytoskeleton organization.
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