Analytical Data
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Gene name
XPAC
- Application
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Alternative Names
XPAC；XPAC；DNA repair Protein complementing XP-A cells
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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
P23025
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Expression Region
1-273aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAAADGA LPEAAALEQP AELPASVRAS IERKRQRALM LRQARLAARP YSATAAAATG GMANVKAAPK IIDTGGGFIL EEEEEEEQKI GKVVHQPGPV MEFDYVICEE CGKEFMDSYL MNHFDLPTCD NCRDADDKHK LITKTEAKQE YLLKDCDLEK REPPLKFIVK KNPHHSQWGD MKLYLKLQIV KRSLEVWGSQ EALEEAKEVR QENREKMKQK KFDKKVKELR RAVRSSVWKR ETIVHQHEYG PEENLEDDMY RKTCTMCGHE LTYEKM
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Molecular Weight
34 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
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Protein Description
XPAC, or x-protein from the Acanthamoeba genus, is a recombinant protein that has garnered significant attention in molecular biology and biotechnology research. The study of XPAC is primarily driven by its potential applications in various fields, including vaccine development, enzyme engineering, and therapeutic interventions. Research has revealed that XPAC possesses unique structural and functional properties that make it a valuable model for understanding protein interactions and cellular mechanisms. In particular, XPAC's ability to fold correctly and maintain stability under physiological conditions offers insights into protein misfolding diseases. Furthermore, the exploration of XPAC's interactions with other biomolecules can shed light on critical cellular pathways and contribute to advancements in drug design and delivery systems. As researchers continue to study this recombinant protein, the goal is to harness its properties for innovative applications that can address pressing challenges in health and disease. Thus, XPAC serves as an important subject of study in the broader context of protein engineering and therapeutic development.
