Analytical Data
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Gene name
ERAS
- Application
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Alternative Names
ERAS；HRAS2；HRASP；GTPase ERas
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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
Q7Z444
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Expression Region
3-230aa
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AA Sequence
LPTKPGTFDLGLATWSPSFQGETHRAQARRRDVGRQLPEYKAVVVGASGVGKSALTIQLNHQCFVEDHDPTIQDSYWKELTLDSGDCILNVLDTAGQAIHRALRDQCLAVCDGVLGVFALDDPSSLIQLQQIWATWGPHPAQPLVLVGNKCDLVTTAGDAHAAAAALAHSWGAHFVETSAKTRQGVEEAFSLLVHEIQRVQEAMAKEPMARSCREKTRHQKATCHCGC
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Molecular Weight
28.8 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
ERAS (Evolving RNA-associated proteins in the stress response) recombinant proteins have garnered significant interest in recent years due to their crucial role in cellular stress responses and regulation of gene expression. Initially identified in various organisms, including plants and animals, these proteins are involved in mechanisms that allow cells to adapt to environmental stresses such as heat, drought, and oxidative damage. The unique properties of ERAS proteins facilitate the post-transcriptional regulation of mRNA, highlighting their potential applications in biotechnology and therapeutic development. Researchers aim to better understand the molecular pathways in which these proteins operate, their interactions with RNA and other cellular components, and how they can be harnessed to enhance stress tolerance in crops or counteract diseases in human cells. With advancements in recombinant DNA technology, scientists can now produce these proteins in vitro, enabling detailed studies of their function and structure. This research not only opens avenues for improving agricultural resilience but also provides insights into fundamental biological processes, paving the way for innovative strategies in medicine and genetics. As the global landscape faces increasing environmental challenges, the study of ERAS recombinant proteins stands at the forefront of both ecological and biomedical research, striving to develop sustainable solutions for food security and health management.
