Human, Mouse IGF-I-LR3 Recombinant Protein (Animal Free) Lyophilized

IHUMSIGFILR3RAFLY200UG

Human, Mouse IGF-I-LR3 Recombinant Protein (Animal Free) Lyophilized

Human, Mouse IGF-I-LR3 Recombinant Protein (Animal Free) Lyophilized

689.5 €

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Human, Mouse IGF-I-LR3 Recombinant Protein (Animal Free) Lyophilized

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40-711

IGF-I-LR3 Recombinant Protein (Animal Free)

The IGFs are mitogenic, polypeptide growth factors that stimulate the proliferation and survival of various cell types, including muscle, bone, and cartilage tissue in vitro. IGFs are predominantly produced by the liver, although a variety of tissues produce the IGFs at distinctive times. The IGFs belong to the Insulin gene family, which also contains insulin and relaxin. The IGFs are similar to insulin by structure and function, but have a much higher growth-promoting activity than insulin. IGF-II expression is influenced by placenta lactogen, while IGF-I expression is regulated by growth hormone. Both IGF-I and IGF-II signal through the tyrosine kinase type I receptor (IGF-IR), but IGF-II can also signal through the IGF-II/Mannose-6-phosphate receptor. Mature IGFs are generated by proteolytic processing of inactive precursor proteins, which contain N-terminal and C-terminal propeptide regions. Recombinant human IGF-I and IGF-II are globular proteins containing 70 and 67 amino acids, respectively, and 3 intra-molecular disulfide bonds. IGF-I LR3 is a recombinant analog of human IGF-I comprised of the complete IGF-I sequence, with an Arginine substitution for the third position Glutamic acid, and a 13 amino acid length N terminus peptide extension. Specifically engineered for higher biological potency in vitro, IGF-I LR3 has an increased half-life and a binding aversion to native proteins within the body that make it ideal for both research and large-scale culturing. Recombinant Human IGF-I LR3 is a 9.1 kDa, single, non-glycosylated polypeptide chain containing 83 amino acid residues.

615.55 €

100-199S-AF

Human IGF-BP3 (Animal Free) Recombinant Protein

IGF-BP3 is a 30 kDa, cysteine-rich secreted protein.  It is the major IGF binding protein present in the plasma of human and animals, and it is also found in α-granules of platelets.  In addition to its ability to modulate the activity of IGF-I and IGF-II, IGF-BP3 exerts inhibitory effects on follicle stimulating hormone (FSH) activity.  Decreased plasma levels of IGF-BP3 often results in dwarfism, whereas elevated levels of IGF-BP3 may lead to acromegaly.  The expression of IGF-BP3 in fibroblasts is stimulated by mitogenic growth factors, such as Bombesin, Vasopressin, PDGF, and EGF.  Recombinant Human IGF-BP3 is a 28.8 kDa protein consisting of 264 amino acid residues.

351.6 €

100-203-AF

Human IGF-BP7 (Animal Free) Recombinant Protein

IGF-BPs control the distribution, function and activity of IGFs in various cell tissues and body fluids.  Currently, there are seven named IGF-BPs that form high affinity complexes with both IGF-I and IGF-II.  IGF-BP7 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.  It plays a role in skeletal myogenesis by binding to IGF in a manner that inhibits IGF-induced differentiation of skeletal myoblasts, without affecting IGF-induced proliferation.  Additionally, IGF-BP7 suppresses growth and colony formation of prostate and breast cancer cell lines through an IGF-independent mechanism, which causes a delay in the G1 phase of the cell cycle and increased apoptosis. Recombinant Human IGF-BP7 is a 26.4 kDa protein consisting of 256 amino acid residues.

494.92 €

100-203S-AF

Human IGF-BP7 (Animal Free) Recombinant Protein

IGF-BPs control the distribution, function and activity of IGFs in various cell tissues and body fluids.  Currently, there are seven named IGF-BPs that form high affinity complexes with both IGF-I and IGF-II.  IGF-BP7 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.  It plays a role in skeletal myogenesis by binding to IGF in a manner that inhibits IGF-induced differentiation of skeletal myoblasts, without affecting IGF-induced proliferation.  Additionally, IGF-BP7 suppresses growth and colony formation of prostate and breast cancer cell lines through an IGF-independent mechanism, which causes a delay in the G1 phase of the cell cycle and increased apoptosis. Recombinant Human IGF-BP7 is a 26.4 kDa protein consisting of 256 amino acid residues.

351.6 €