IGF1 Gilthead SeabreamRecombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 68 amino acids and having a molecular mass of 7545.4 Dalton, the predicted pI=7.72.
IGF-1 is purified by proprietary chromatographic techniques.
Insulin-like growth factors (IGFs), also known as somatomedins, are a family of peptides with crucial roles in mammalian growth and development. IGF1 is a key mediator of growth hormone's (GH) growth-promoting effects. Initial research revealed that GH didn't directly promote sulfate incorporation into cartilage; instead, it acted through a serum factor called 'sulfation factor,' later identified as somatomedin. Three primary somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2), and somatomedin B.
Recombinant IGF1 Gilthead Seabream, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 68 amino acids. It has a molecular weight of 7545.4 Daltons and a predicted isoelectric point (pI) of 7.72. The purification of IGF-1 is achieved using proprietary chromatographic methods.
For reconstitution, it is recommended to dissolve the lyophilized IGF-1 in sterile 0.4% NaHCO3, adjusted to a pH of 8-9, to a final concentration of at least 100 µg/ml. This solution can be further diluted into other aqueous solutions as needed.
Lyophilized IGF1 remains stable at room temperature for up to 3 weeks. However, for long-term storage, it's recommended to store it desiccated at a temperature below -18°C. After reconstitution, IGF1 should be stored at 4°C for 2-7 days. For extended storage, freezing at -18°C is recommended. To preserve stability during long-term storage, consider adding a carrier protein (0.1% HSA or BSA). Avoid repeated freeze-thaw cycles.
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Insulin-like Growth Factor 1 (IGF1) is a crucial growth factor in vertebrates, playing a significant role in growth and development. In fish, IGF1 is particularly important for regulating growth and development, mediating the effects of growth hormone. The gilthead seabream (Sparus aurata) is a prominent species in Mediterranean aquaculture, known for its economic value and biological significance .
IGF1 in gilthead seabream has been extensively studied due to its role in growth regulation. The recombinant form of IGF1 (IGF1 Gilthead Seabream Recombinant) is produced to study its effects on growth and development in controlled environments. This recombinant protein is a single, non-glycosylated polypeptide chain containing 68 amino acids, with a molecular mass of approximately 7545.4 Daltons .
The recombinant IGF1 for gilthead seabream is typically produced in Escherichia coli (E. coli) using recombinant DNA technology. The gene encoding IGF1 is inserted into a plasmid vector, which is then introduced into E. coli cells. These cells express the IGF1 protein, which is subsequently purified using chromatographic techniques .
Recombinant IGF1 from gilthead seabream has been shown to exhibit mitogenic activity, although it is significantly lower than that of human IGF1. This difference in activity is likely due to a lower affinity for the IGF1 receptor in certain cell types . Despite this, IGF1 remains a critical factor in the growth and development of gilthead seabream, influencing various physiological processes.
The use of recombinant IGF1 in aquaculture research helps in understanding the growth mechanisms in gilthead seabream. By studying the effects of IGF1, researchers can develop strategies to enhance growth rates, improve feed efficiency, and optimize aquaculture practices. This knowledge is essential for improving the sustainability and productivity of gilthead seabream farming .