Analytical Data
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Gene name
AK2
- Application
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Alternative Names
AK2;GCN2;KIAA1338;eIF-2-alpha kinase GCN2
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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
P54819
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Expression Region
1-239aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MAPSVPAAEP EYPKGIRAVL LGPPGAGKGT QAPRLAENFC VCHLATGDML RAMVASGSEL GKKLKATMDA GKLVSDEMVV ELIEKNLETP LCKNGFLLDG FPRTVRQAEM LDDLMEKRKE KLDSVIEFSI PDSLLIRRIT GRLIHPKSGR SYHEEFNPPK EPMKDDITGE PLIRRSDDNE KALKIRLQAY HTQTTPLIEY YRKRGIHSAI DASQTPDVVF ASILAAFSKA TCKDLVMFI
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Molecular Weight
29 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
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Protein Description
AK2, or adenylate kinase 2, is a crucial enzyme involved in cellular energy homeostasis as it plays a vital role in the ATP-ADP energy cycle. Research into AK2 has gained significance due to its involvement in various physiological and pathological processes, including mitochondrial function, cell proliferation, and apoptosis. Mutations or dysregulation of AK2 are implicated in several diseases, including tumorigenesis and mitochondrial disorders. Studies have shown that AK2 is predominantly localized in mitochondria, suggesting a pivotal role in bioenergetics and cellular metabolism. Furthermore, its expression levels can significantly influence cellular responses to stress and injury, making it a potential target for therapeutic interventions. Recent advances in recombinant protein technology have enabled researchers to produce AK2 in larger quantities and purify it for in-depth functional studies. This has facilitated the exploration of its biochemical properties, interactions with other cellular components, and the impact of post-translational modifications. Understanding AK2 at the molecular level may provide insights into its regulatory mechanisms and its potential role as a biomarker or therapeutic target for conditions associated with energy metabolism dysfunctions. Research initiatives focusing on AK2 also aim to elucidate its involvement in signaling pathways that govern cell survival and death, thereby bridging the gap between basic biochemistry and clinical applications in disease management. As studies continue to uncover the multifaceted roles of AK2, it stands as a promising candidate for future research in cellular bioenergetics and disease modeling.











