IGF1 Human, A67T
Greater than 95.0% as determined by SDS-PAGE.
Description
IGF1 A67T Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 70 amino acids and having a molecular mass of Approximately 7.7 kDa.
The IGF1 A67T is purified by proprietary chromatographic techniques.
Product Specs
GPETLCGAEL VDALQFVCGD RGFYFNKPTG YGSSSRRAPQ TGIVDECCFR SCDLRRLEMY CAPLKPTKSA.
Product Science Overview
Insulin-Like Growth Factor-1 (IGF-1) is a protein that plays a crucial role in growth and development, particularly during childhood. It is structurally similar to insulin and is part of the insulin gene family. IGF-1 is produced primarily in the liver and acts as an endocrine hormone, but it is also synthesized in various tissues in a paracrine/autocrine manner . The mutant A67T variant of IGF-1 refers to a specific alteration in the amino acid sequence where alanine (A) at position 67 is replaced by threonine (T).
IGF-1 is a potent mitogen that stimulates the proliferation and survival of various cell types, including muscle, bone, and cartilage tissues . It mediates many of the growth-promoting effects of growth hormone (GH) and is involved in cellular differentiation, transformation, and apoptosis. The A67T mutation in IGF-1 has been studied for its potential impact on the protein’s function and its implications in various diseases and therapeutic applications.
Recombinant human IGF-1, including the A67T mutant, is typically produced using bacterial expression systems such as Escherichia coli . The gene encoding the IGF-1 protein is inserted into a plasmid vector, which is then introduced into the bacterial cells. The bacteria are cultured, and the recombinant protein is expressed and subsequently purified through various chromatographic techniques. The final product is often lyophilized for stability and ease of storage.
The A67T mutation in IGF-1 can affect the protein’s structure and function. Analytical techniques such as mass spectrometry, nuclear magnetic resonance (NMR) spectroscopy, and X-ray crystallography are employed to study the structural changes induced by the mutation . Functional assays, including cell proliferation and receptor binding studies, are conducted to assess the biological activity of the mutant protein compared to the wild-type IGF-1.
Recombinant IGF-1, including the A67T mutant, has significant therapeutic potential. It has been investigated for its role in improving insulin sensitivity and glycemic control in patients with type II diabetes . Additionally, IGF-1 is being explored for its potential in treating growth deficiencies, muscle wasting diseases, and certain cancers. The A67T mutation, in particular, may offer insights into the protein’s function and its role in disease mechanisms.
