Analytical Data
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Gene name
AK3
- Application
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Alternative Names
AK3L1; AK6; AKL3L; Adenylate Kinase 3 Alpha-Like 1; GTP:AMP Phosphotransferase AK3, Mitochondrial
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
Q9UIJ7
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Expression Region
Leu8~Pro227
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Molecular Weight
29kDa
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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
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Protein Description
The AK3 protein, an important member of the adenylate kinase family, has garnered significant attention in recent years due to its crucial role in cellular energy metabolism and regulation. It is primarily responsible for the interconversion of adenine nucleotides, thereby maintaining the ATP/ADP energy balance within cells. Dysregulation of AK3 has been implicated in various pathological conditions, including cancer, neurodegenerative diseases, and metabolic disorders, underscoring its potential as a therapeutic target. Research efforts have focused on understanding its structure-function relationship, enzymatic mechanisms, and regulatory pathways. Advances in recombinant protein technology have facilitated the production of AK3 for in vitro studies, enabling the exploration of its biochemical properties and interactions with other cellular components. Furthermore, the development of specific inhibitors or modulators of AK3 activity could provide novel avenues for treatment, making this protein a focal point in metabolic research. Overall, the study of AK3 is essential not only for elucidating fundamental biological processes but also for developing innovative strategies to combat diseases associated with energy metabolism dysregulation.
