Analytical Data
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Gene name
INS
- Application
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Alternative Names
INS；Insulin
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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
P01308
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Expression Region
1-110aa
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AA Sequence
MALWMRLLPLLALLALWGPDPAAAFVNQHLCGSHLVEALYLVCGERGFFYTPKTRREAEDLQVGQVELGGGPGAGSLQPLALEGSLQKRGIVEQCCTSICSLYQLENYCN
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Molecular Weight
11.9 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
Insulin (INS) is a crucial hormone involved in glucose metabolism and homeostasis, and its dysfunction is a key factor in diabetes and metabolic disorders. The emergence of recombinant protein technology has revolutionized the production of insulin and insulin analogs, allowing for the synthesis of biologically active proteins in large quantities. Historically, insulin was extracted from animal pancreas, but this method posed ethical and supply chain issues. The development of recombinant DNA technology in the late 20th century enabled the expression of human insulin in microbial systems, such as Escherichia coli and yeast, ensuring a more reliable and safer source. Concurrently, research into insulin's structure and function has led to the design of modified insulin analogs with tailored pharmacokinetic properties, improving glycemic control for diabetes patients. These advancements are significant not only for therapeutic applications but also for understanding insulin's role in various physiological processes. Ongoing research focuses on optimizing production techniques, enhancing the efficacy of insulin therapies, and exploring novel approaches to insulin delivery, such as insulin pods and smart insulin pens. This collective effort aims to address the global diabetes epidemic by providing patients with more effective and accessible treatment options, highlighting the importance of continuous innovation in biotechnology related to INS recombinant protein research.
