Analytical Data
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Gene name
EIF2aK4
- Application
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Alternative Names
GCN2; GCN2-like protein
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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 90% as determined by SDS-PAGE.
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Uniprot
Q9P2K8
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Expression Region
Val296~Ile539
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Molecular Weight
31kDa
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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
EIF2A kinase 4 (EIF2AK4), also known as GCN2 (General Control Nonderepressible 2), is a crucial protein in the regulation of cellular responses to nutritional stress and amino acid deprivation. It is part of the eIF2 kinase family, which phosphorylates the alpha subunit of eIF2, thereby inhibiting global protein synthesis while selectively promoting the translation of specific mRNAs involved in stress responses. Research into EIF2AK4 has gained significant attention due to its implications in various physiological and pathological processes, including metabolism, cancer, and neurodegenerative diseases. Dysregulation of EIF2AK4 activity has been linked to diseases characterized by altered cellular stress responses, making it a potential therapeutic target. Studies utilizing recombinant EIF2AK4 proteins have facilitated the exploration of its functional mechanisms, interactions with other cellular pathways, and its role in regulating autophagy and apoptosis. Understanding the structure-function relationship of EIF2AK4 is vital, as it may provide new insights into the development of novel strategies for treating diseases associated with stress response dysregulation. Recent advances in biotechnology have enabled the production of recombinant EIF2AK4, allowing researchers to dissect its signaling pathways and investigate how its activity can be modulated for therapeutic benefit. Overall, the ongoing research in EIF2AK4 represents a promising frontier in cell biology, with the potential to yield significant contributions to our understanding of stress response mechanisms and their relevance in human health and disease.
