Analytical Data
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Gene name
OXM
- Application
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Species
Mouse
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P55095
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Expression Region
His21~Lys180
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Molecular Weight
22kDa
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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
OXM (Oxytocin-like peptide) recombinant proteins have garnered significant interest in biomedical research due to their potential roles in various physiological and pathological processes. Initially identified as part of the oxytocin family, OXM is known for its involvement in metabolic regulation, appetite control, and cardiovascular functions. Recent studies have highlighted its potential therapeutic applications in obesity, diabetes, and even neuropsychiatric disorders. The ability to produce recombinant OXM proteins has facilitated detailed investigations into their structure-function relationships, receptor interactions, and biological activities. These advancements enable researchers to explore OXM's mechanisms of action in greater depth, paving the way for novel drug development. The reconstitution of OXM in research settings allows for controlled experiments, offering insights into its therapeutic windows and side effects, which are crucial for translational medicine. As the understanding of OXM's biological significance expands, it presents promising avenues for innovative treatments targeting metabolic and emotional disorders, marking a notable advancement in peptide-based therapeutics.
