Analytical Data
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Gene name
XERO2
- Application
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Alternative Names
XERO2；LTI30；Dehydrin Xero 2
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Species
E.coli
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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
P42758
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Expression Region
1-193aa
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AA Sequence
MNSHQNQTGVQKKGITEKIMEKLPGHHGPTNTGVVHHEKKGMTEKVMEQLPGHHGATGTGGVHHEKKGMTEKVMEQLPGHHGSHQTGTNTTYGTTNTGGVHHEKKSVTEKVMEKLPGHHGSHQTGTNTAYGTNTNVVHHEKKGIAEKIKEQLPGHHGTHKTGTTTSYGNTGVVHHENKSTMDKIKEKLPGGHH
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Molecular Weight
28.4 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
XERO2, a protein implicated in various cellular processes, has garnered significant attention in recent years due to its potential role in diverse biological functions and disease mechanisms. Research indicates that XERO2 is involved in RNA metabolism, including splicing and transport, which are crucial for maintaining cell homeostasis and regulating gene expression. Additionally, XERO2 has been linked to response mechanisms associated with cellular stress and disease conditions, such as cancer and neurodegeneration. The study of XERO2 recombinant protein is particularly important for elucidating its structural and functional properties, which can provide insights into its interactions within the cellular environment. Advances in recombinant DNA technology have allowed for the production of XERO2 at scale, enabling detailed biochemical and biophysical characterization. Understanding the mechanisms by which XERO2 operates at the molecular level could lead to novel therapeutic approaches, especially in targeting diseases where its dysregulation is evident. As research progresses, XERO2 may emerge as a significant biomarker or therapeutic target, highlighting the necessity for continuous investigation into its biological roles and applications in biomedicine.
