Analytical Data
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Gene name
XERO2
- Application
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Alternative Names
Low-temperature-induced protein LTI30 (LTI30)
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Species
Arabidopsis thaliana
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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
P42758
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Expression Region
1-193aa
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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, also known as Xeroderma Pigmentosum Complementation Group E (XPE), is a protein that plays a crucial role in the nucleotide excision repair (NER) pathway, which is essential for the recognition and repair of DNA damage, particularly that caused by ultraviolet (UV) radiation. Individuals with mutations in the XERO2 gene are susceptible to skin cancers and exhibit symptoms of xeroderma pigmentosum, characterized by extreme sensitivity to sunlight and a high risk of skin lesions. Research into XERO2 recombinant proteins is vital for understanding the mechanisms of NER and the consequences of its dysfunction. By studying the structural and functional properties of XERO2, scientists aim to elucidate its interactions with other proteins involved in the DNA repair process. This knowledge can provide insights into the cellular responses to UV-induced DNA damage and may lead to the development of novel therapeutic strategies for conditions associated with defective DNA repair mechanisms, including certain cancers and skin disorders. Furthermore, recombinant XERO2 proteins can be used in biochemical assays and drug discovery efforts, enhancing our understanding of repair pathways and the development of pharmacological interventions that could potentially mitigate the effects of UV radiation on DNA. Overall, the study of XERO2 recombinant proteins is significant for both fundamental research in DNA repair mechanisms and the translation of this knowledge into clinical applications for patients with related genetic disorders.
