Description: Insulin-like growth factor 1 (IGF-1) is a primary mediator of the effects of growth hormone (GH) and has growth-promoting effects on almost every cell in the body. IGF-1 can also regulate cell growth and development, especially in nerve cells, as well as cellular DNA synthesis. Canine IGF-1 Recombinant Protein is purified insulin-like growth factor 1 (IGF-1) produced in yeast.

Description: Insulin-like Growth Factor-II (IGF-II) is a polypeptide endocrine hormone structurally similar to insulin and belongs to insulin-like growth factor family.

Description: The IGF-1 ELISA is an enzyme immunoassay for the quantitative in vitro diagnostic measurement of Insulin-like Growth Factor 1 (IGF-1) in serum.

Description: For quantitative detection of human IGF-1 in cell culture supernates, serum and plasma (heparin, EDTA).

Description: 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 by structure and function to insulin, 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.

Description: 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 by structure and function to insulin, 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.

Description: IGF-BPs controls 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-BP1 is a 25.4 kDa cysteine-rich secreted protein expressed in liver, deciduas, and kidneys and is the most abundant IGF-BP in amniotic fluid. Levels of IGF-BP1 in serum are lowest after food. IGF-BP1 binds to both IGF-I and IGF-II with equal affinity. Phosphorylated IGF-BP1 hinders IGF actions, where as nonphosphorylated IGF-BP1 is stimulatory. Recombinant human IGF-BP1 is a 25.4 kDa protein consisting of 235 amino acid residues (Isoform A).

Description: IGF-BPs control the distribution, function and activity of IGFs in various cell tissues and body fluids. IGF-BP4 is the major IGF-BP produced by osteoblasts, and is also found in the epidermis, ovarian follicles, and other tissues. IGF-BP4 inhibits the activity of IGF-I and IGF-II by binding in a manner that results in the formation of complexes with reduced ability to signal through cell surface IGF receptors. IGF-BP4 can inhibit the growth of chick pelvis cartilage and HT29 colon adenocarcinoma cells by blocking the mitogenic actions of IGFs, and has also been shown to reduce colony formation by colorectal cancer cells via an IGF independent pathway. The biological effects of IGF-BP4 can be regulated by Pregnancy Associated Plasma Protein A (PAPP-A), which reduces IGF-BP4/IGF binding affinity by proteolytically cleaving IGF-BP4. The modulation of IGF-BP4 activity by PAPP-A is an important component in the regulation of ovarian folliculogenesis and in the growth inhibition of responding ovarian cancer cells. Recombinant human IGF-BP4 is a 25.8 kDa protein consisting of 237 amino acid residues including the IGF-BP domain and thyroglobulin type-I domain.

*Manufactured using (BTI-Tn-5B1-4) cells under license from the Boyce Thompson Institute for Plant Research, Inc.

Description: IGF-BPs controls 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-BP5 is a 28.6 kDa cysteine-rich secreted protein produced by vascular smooth muscle cells. It is the major IGF-binding protein present in bone tissue and helps potentiate the action of IGF-I on smooth muscle cells, fibroblasts or osteoblasts. Data shows that IGFBP-5 acts as a growth inhibitor and pro-apoptotic agent in breast cancer cells. IGFBP-5 overexpressing mice show an increase in neonatal mortality, reduced female fertility, whole-body growth inhibition and retarded muscle development. Recombinant human IGF-BP5 is a 28.6 kDa protein consisting of 253 amino acid residues.