Analytical Data
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Gene name
JUN
- Application
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Alternative Names
(Activator protein 1)(AP1)(Proto-oncogene c-Jun)(Transcription factor AP-1 subunit Jun)(V-jun avian sarcoma virus 17 oncogene homolog)(p39)
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Species
Human
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P05412
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Expression Region
1-331aa
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Molecular Weight
43.1 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
Research on JUN recombinant proteins focuses on understanding the role of the JUN proto-oncogene, a vital component of the AP-1 transcription factor complex, which is crucial in regulating gene expression, cell proliferation, differentiation, and apoptosis. The JUN protein, particularly in its phosphorylated form, is implicated in various cellular processes and is associated with numerous pathological conditions, including cancer, inflammation, and tissue repair. Studies often investigate how overexpression or mutation of the JUN gene can lead to oncogenic transformations, making it a significant target for therapeutic intervention. The ability to produce JUN recombinant proteins enables researchers to explore the protein's biochemical properties, interaction with other cellular factors, and its involvement in signaling pathways. By utilizing techniques such as molecular cloning, expression in suitable host systems, and purification processes, scientists can delve into the functions and mechanisms of JUN in greater detail. Furthermore, understanding its dynamics can offer insights into potential drug development aimed at modulating JUN activity for treating diseases where its dysregulation is a contributing factor. As such, examining JUN recombinant proteins is a critical aspect of cancer research and regenerative medicine, providing a foundation for innovations in targeted therapies and biologic treatments.
