Analytical Data
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Gene name
UCN
- Application
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Alternative Names
UCN；Urocortin
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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
P55089
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Expression Region
1-124aa
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AA Sequence
MRQAGRAALLAALLLLVQLCPGSSQRSPEAAGVQDPSLRWSPGARNQGGGARALLLLLAERFPRRAGPGRLGLGTAGERPRRDNPSLSIDLTFHLLRTLLELARTQSQRERAEQNRIIFDSVGK
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Molecular Weight
13.4 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
The study of UCN (Urocortin) recombinant proteins has garnered significant attention due to their potential therapeutic applications in various physiological and pathological conditions. UCN is a member of the corticotropin-releasing factor (CRF) family and plays a critical role in the regulation of stress responses, appetite, and neuroendocrine functions. Research has indicated that UCN can modulate cardiovascular functions, promote neuroprotection, and influence metabolism, making it a promising candidate for treating stress-related disorders, anxiety, and obesity. The ability to produce UCN as a recombinant protein allows for the detailed study of its structure-function relationships and biological mechanisms, paving the way for the development of novel therapeutic strategies. As recombinant DNA technology continues to advance, the production of UCN in various expression systems, such as bacteria and yeast, has enabled researchers to obtain large quantities of high-purity protein for experimental analysis. Furthermore, understanding the interactions between UCN and its receptors could illuminate new pathways for drug development. Overall, the investigation of UCN recombinant proteins is a rapidly evolving field that intersects molecular biology, pharmacology, and clinical research, with the potential to yield innovative solutions for managing stress-related conditions and enhancing emotional well-being.
