IGF1 belongs to the insulin gene family. It is a mitogenic polypeptide growth factor that stimulates the proliferation and survival of various cell types including muscle, bone, and cartilage tissue in vitro. IGF1 DES is a truncated variant of human IGF1 with the tripeptide Gly-Pro-Glu absent from the N-terminus. It has been isolated from bovine colostrum, human brain, and porcine uterus. The IGF1 DES is believed to result from post-translational cleavage of IGF1 via protease activity. It is about 10-fold more potent than IGF1 at stimulating hypertrophy and proliferation of cultured cells, a consequence of much reduced binding to IGF-binding proteins, which is in turn caused by the absence of the glutamate at position 3. Clinical opportunities for IGF1-DES have not yet been evaluated, but could apply in catabolic states as well as for the treatment of inflammatory bowel diseases.

The Insulin-like growth factors (IGFs) are mitogenic polypeptide growth factors, predominantly produced in the liver, that stimulate the proliferation and survival of various cell types, including muscle, bone and cartilage tissue in vitro. IGFs belong to the Insulin gene family and are similar by structure and function to insulin, but have a much higher growth-promoting activity. IGF1 expression is regulated by growth hormone, while IGF2 expression is influenced by placenta lactogen. Both IGF1 and IGF2 signal through the tyrosine kinase type I receptor (IGFIR). Mature IGFs are generated through proteolytic processing of inactive precursor proteins. Recombinant human IGF1 is a globular protein containing 70 amino acids and 3 intra-molecular disulfide bonds. This particular product has been labeled with the stable 15N isotope to help track its activity.

The Insulin-like growth factors (IGFs) are mitogenic polypeptide growth factors that stimulate the proliferation and survival of various cell types, including muscle, bone and cartilage tissue in vitro. They are predominantly produced in the liver. IGFs belong to the Insulin gene family and are similar by structure and function to insulin, but have a much higher growth-promoting activity. IGF1 expression is regulated by growth hormone, while IGF2 expression is influenced by placenta lactogen. Both IGF1 and IGF2 signal through the tyrosine kinase type I receptor (IGF IR). Mature IGFs are generated through proteolytic processing of inactive precursor proteins. Recombinant human IGF1 is a globular protein containing 70 amino acids, and 3 intra-molecular disulfide bonds.

Sterile Filtered White lyophilized powder. Purified and tested for use in cell culture.

The Insulin-like growth factors (IGFs) are mitogenic polypeptide growth factors, predominantly produced in the liver, that stimulate the proliferation and survival of various cell types, including muscle, bone and cartilage tissue in vitro. IGFs belong to the Insulin gene family and are similar by structure and function to insulin, but have a much higher growth-promoting activity. IGF1 expression is regulated by growth hormone, while IGF2 expression is influenced by placenta lactogen. Both IGF1 and IGF2 signal through the tyrosine kinase type I receptor (IGFIR). Mature IGFs are generated through proteolytic processing of inactive precursor proteins. Recombinant murine IGF1 is a globular protein containing 70 amino acids, and 3 intra-molecular disulfide bonds.

The Insulin-like growth factors (IGFs) are mitogenic polypeptide growth factors that stimulate the proliferation and survival of various cell types including muscle, bone, and cartilage tissue in vitro. They are predominantly produced in the liver. IGFs belong to the Insulin gene family and are similar by structure and function to insulin, but have a much higher growth-promoting activity. IGF1 expression is regulated by growth hormone, while IGF2 expression is influenced by placenta lactogen. Both IGF1 and IGF2 signal through the tyrosine kinase type I receptor (IGF IR). Mature IGFs are generated through proteolytic processing of inactive precursor proteins. Recombinant human IGF1 is a globular protein containing 70 amino acids, and 3 intra-molecular disulfide bonds.

Insulin-like Growth Factor-Binding Protein 3 (IGFBP3) belongs to the IGFBP family, which are all proteins with conserved cysteine residues, an IGFBP domain, and a thyroglobulin type-I domain. IGFBP3 is expressed by most tissues and is the most abundant IGFBP protein. It has higher levels of expression during postnatal life, which peak during puberty. The expression of IGFBP3 in fibroblasts is stimulated by a number of mitogenic growth factors. The protein forms a ternary complex with IGFI or IGFII, and an acid-labile subunit, causing it to circulate in the plasma. As this complex, it prolongs the half-life of IGFs and alters their interaction with cell surface receptors. Decreased plasma levels of IGFBP3 often happen during the progression of prostate cancer from benign to metastatic disease.

IGFBP7 belongs to the superfamily of insulin-like growth factor (IGF) binding proteins and is encoded by the IGFBP7 gene in human. It is expressed in a wide range of normal human tissues and it generally shows reduced expression in cancer cell lines of prostate, breast, colon, and lung origin. IGFBP7 includes conserved cysteine residues. IGFBP7 modulates the biological activities of IGF proteins. It also suppresses growth and colony formation of prostate and breast cancer cell lines. Above all, IGFBP7 is a very important factor in skeletal myogenesis. Human IGFBP7 cDNA encodes a 282 amino acid (a.a.) residue precursor protein with a putative 26 a.a. signal peptide.