Analytical Data
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Gene name
AD
- Application
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Alternative Names
AD；CINAP；Adenylate kinase isoenzyme 6
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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
P23793
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Expression Region
2-410aa
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AA Sequence
SVFDSKFKGIHVYSEIGELESVLVHEPGREIDYITPARLDELLFSAILES HDARKEHKQFVAELKANDINVVELIDLVAETYDLASQEAKDKLIEEFLED SEPVLSEEHKVVVRNFLKAKKTSRELVEIMMAGITKTDLGIEADHELIVD PMPNLYFTRDPFASVGNGVTIHYMRYKVRQRETLFSRFVFSNHPKLINTP WYYDPSLKLSIEGGDVFIYNNDTLVVGVSERTDLQTVTLLAKNIVANKEC EFKRIVAINVPKWTNLMHLDTWLTMLDKDKFLYSPIANDVFKFWDYDLVN GGAEPQPVENGLPLEGLLQSIINKKPVLIPIAGEGASQMEIERETHFDGT NYLAIRPGVVIGYSRNEKTNAALEAAGIKVLPFHGNQLSLGMGNARCMSM PLSRKDVKW
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Molecular Weight
46 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
AD (Alzheimer's Disease) is a progressive neurodegenerative disorder characterized by cognitive decline, memory loss, and behavioral changes. It is primarily associated with the accumulation of amyloid-beta (Aβ) plaques and tau protein tangles in the brain, leading to synaptic dysfunction and neuronal death. The complexity of AD pathology has driven researchers to explore various therapeutic strategies, including the development of recombinant proteins that target specific aspects of the disease. Recombinant proteins, engineered through genetic technology, can be designed to enhance the clearance of amyloid plaques, inhibit tau aggregation, or modulate neuroinflammation, thereby providing potential avenues for treatment. Additionally, these proteins can serve as valuable tools for understanding the underlying mechanisms of the disease and for screening drug candidates. Advances in molecular biology and biotechnology have significantly improved the production and characterization of these proteins, making it feasible to develop more effective interventions. As research progresses, the focus continues to be on optimizing the efficacy and safety of AD recombinant proteins, with the ultimate goal of modifying the disease's trajectory and improving patient outcomes.
