Analytical Data
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Gene name
INS
- 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
P01326
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Expression Region
Phe25~Ser54 and Gly90~Asn110 linked by GGGGS
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Molecular Weight
10kDa
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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
Insulin-like signaling pathways play a crucial role in regulating various biological processes, including glucose homeostasis, growth, and metabolism. In recent years, research focused on insulin-like proteins, especially insulin-like growth factor (IGF) and insulin-like neuropeptides, has gained momentum due to their significant implications in human health and disease. These proteins are of particular interest in the study of metabolic disorders, such as obesity and diabetes, as well as in cancer research, where they can influence cell proliferation and survival. The recombinant production of insulin-like proteins has facilitated the investigation of their structure-function relationships and therapeutic potential. Advancements in biotechnology, particularly in expression systems such as bacteria, yeast, and mammalian cells, have enabled the efficient synthesis of high-quality recombinant proteins. This has paved the way for detailed functional assays and the development of novel therapeutic agents that target these pathways. Overall, the study of recombinant insulin-like proteins holds great promise for improving our understanding of metabolic regulation and for developing innovative strategies to combat diseases associated with insulin resistance and growth factor signaling dysregulation.
