Analytical Data
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Gene name
U22
- Application
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Alternative Names
U22；EJLF1；GlycoProtein U22
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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
Q69557
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Expression Region
21-202aa
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AA Sequence
SLHIINNENSVFIATHSETELRHWLIFVKMAQRNGTAWWRMASVPINAYFERDIAFLFNPRCVIETAMGSKILCRYNKNIGVVFVDNDTKCNVSFPSGVQLQLLNQSVMESIRTKTYVVDYARKTTERGDCFISVAFCRKERRRFLSRCERFVYYCISVYLFAVVVLCSCWFALDPLFNMWA
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Molecular Weight
24.1 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
The U22 protein, a key component in the study of protein folding and cellular function, has garnered significant attention in recent years due to its role in various biological processes. Originally identified in the context of eukaryotic cells, U22 is implicated in stress response, cellular signaling, and the maintenance of protein homeostasis. The reconstitution and characterization of U22 as a recombinant protein represent a crucial step in understanding its structure-function relationship. Utilizing techniques such as molecular cloning, expression in heterologous systems, and purification protocols, researchers aim to elucidate the protein's stability, interaction dynamics, and functional mechanisms. This research is particularly relevant given that misfolded proteins are associated with various diseases, including neurodegenerative disorders. Thus, studying U22 not only enhances our fundamental knowledge of protein biology but also opens avenues for potential therapeutic applications, ultimately contributing to advancements in biomolecular engineering and medicine.
