Analytical Data
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Gene name
AES
- Application
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Alternative Names
AES；AES；GRG；GRG5；TLE family member 5
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q08117
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Expression Region
1-197aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMMFPQSRHSGSSHLPQQLKFTTSDSCDRIK DEFQLLQAQYHSLKLECDKLASEKSEMQRHYVMYYEMSYGLNIEMHKQAE IVKRLNGICAQVLPYLSQEHQQQVLGAIERAKQVTAPELNSIIRQQLQAH QLSQLQALALPLTPLPVGLQPPSLPAVSAGTGLLSLSALGSQAHLSKEDK NGHDGDTHQEDDGEKSD
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Molecular Weight
24 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
The study of AES (Amphiphysin 1) recombination proteins has garnered significant attention in the fields of molecular biology and medicine due to their essential roles in various cellular processes, including endocytosis, synaptic transmission, and nervous system development. AES is a member of the BAR (Bin/Amphiphysin/Rvs) domain-containing family of proteins, which are known for their ability to sense and generate membrane curvature, thus influencing membrane dynamics and vesicle formation. Abnormal expression or malfunctioning of AES proteins has been implicated in several neurological disorders, such as Alzheimer's disease and autism spectrum disorders. Research has increasingly focused on understanding the molecular mechanisms by which AES interacts with other proteins and membranes, as well as exploring potential therapeutic targets for modulating its activity. Furthermore, advances in methods for protein engineering and recombinant DNA technology have opened new avenues for the creation of modified AES proteins, allowing researchers to dissect their functional roles in a controlled manner. This has laid the groundwork for innovative strategies in drug discovery and the development of novel biotechnological applications, emphasizing the importance of AES recombination proteins in both basic research and clinical contexts.
