Peptide Hormones

Cysteine-rich angiogenic inducer 61 (Cyr61) is a dynamically expressed, multifunctional matricellular protein of the CCN family encoded by the Cyr61 gene. Cyr61 is critical for cardiovascular development during embryogenesis and regulates inflammation, wound healing and fibrogenesis in the adult. It is involved in cell adhesion, cell migration, cell proliferation, and cell differentiation. Cyr61 consists of four domains: an IGFBP domain, a VWF type C domain, a TSP type I domain, and a cysteine knot domain.

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.

NOV is a dynamically expressed, multifunctional matricellular protein of the CCN (CTGF/CYR61/NOV) family encoded by the NOV gene. It is expressed in certain tumors, including Wilm’s tumor and most nephroblastomas. Expression of NOV has been reported to reduce tumorgenicity and reduce proliferation of certain cancer cell lines. It has also been shown to induce angiogenesis in endothelial cells and stimulate cell migration in many mesenchymal cell types. Recombinant human NOV is a 36.2 kDa protein containing 331 amino acid residues and it shares 80% and 81% amino acid identity with rat and murine NOV.

NOV is a dynamically expressed, multifunctional matricellular protein of the CCN (CTGF/CYR61/NOV) family encoded by the NOV gene. It is expressed in certain tumors, including Wilm’s tumor and most nephroblastomas. Expression of NOV has been reported to reduce tumorgenicity and reduce proliferation of certain cancer cell lines. It has also been shown to induce angiogenesis in endothelial cells and stimulate cell migration in many mesenchymal cell types. Recombinant murine NOV is a 36.4 kDa protein containing 333 amino acid residues and it shares 92% and 82% amino acid identity with rat and human NOV.

Murine Prolactin (PRL) is a peptide hormone that is secreted most notably from the pituitary gland where it acts in an endocrine fashion, but also from extra pituitary regions where it acts in an autocrine or paracrine fashion. PRL serves as a ligand for the prolactin receptor, PRLR. It is listed as having over 300 separate functions and is involved in more processes than any other pituitary hormone. PRL is most commonly known for its lactation stimulating effect, but also plays a role in reproductive behavior, homeostasis of electrolytes, growth and development, regulation of metabolism, immune system regulation, angiogenesis, and survival of cancer cells. Homozygous female knock-out mice lacking expression of PRL become infertile, whereas homozygous males were fully fertile.

Rat Prolactin (PRL) is a peptide hormone that is secreted most notably from the pituitary gland where it acts in an endocrine fashion, but also from extra pituitary regions where it acts in an autocrine or paracrine fashion. It is listed as having over 300 separate functions and is involved in more processes than any other pituitary hormone. PRL is most commonly known for its lactation stimulating effect, but also plays a role in reproductive behavior, homeostasis of electrolytes, growth and development, regulation of metabolism, immune system regulation, angiogenesis, and survival of cancer cells. PRL acts as a ligand for the prolactin receptor, PRLR.

Human Parathyroid Hormone (PTH) is a hormone expressed and secreted as preproPTH by chief cells of the parathyroid glands when extracellular calcium levels are low. It is coexpressed with furin, the enzyme believed to be responsible for processing proPTH to PTH. PTH is a ligand for two different receptors, PTH1R in bone and kidney and PTH2R found in the CNS, pancreas, and placenta. PTH plays a major role in bone metabolism and calcium homeostasis, as well as renal excretion. Recombinant PTH (1-34) has been used to stimulate bone formation and bone resorption, increasing or decreasing bone mass depending on the mode of administration.

Human Parathyroid Hormone (PTH) is a hormone expressed and secreted as preproPTH by chief cells of the parathyroid glands when extracellular calcium levels are low. It is coexpressed with furin, the enzyme believed to be responsible for processing proPTH to PTH. PTH is a ligand for two different receptors, PTH1R in bone and kidney and PTH2R found in the CNS, pancreas, and placenta. PTH plays a major role in bone metabolism and calcium homeostasis, as well as renal excretion. In osteoblasts, PTH stimulates glycogenesis and the uptake of [1-(14)C]-2-deoxy-D-glucose (2DG).

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

Human Parathyroid Hormone (PTH) is a hormone expressed and secreted as preproPTH by chief cells of the parathyroid glands when extracellular calcium levels are low. It is coexpressed with furin, the enzyme believed to be responsible for processing proPTH to PTH. PTH is secreted as a midregional peptide fragment (7-34) when extracellular calcium levels are high, offsetting the effects of PTH. PTH plays a major role in bone metabolism and calcium homeostasis, as well as renal excretion. PTH (7-34) is a PTH1R antagonist capable of stimulating proliferation and differentiation of hair follicles and epidermis while promoting cell survival by activation of Akt.

GoldBio growth factors are manufactured for RESEARCH USE ONLY and cannot be sold for human consumption!

Human Parathyroid Hormone (PTH) is a hormone expressed and secreted as preproPTH by chief cells of the parathyroid glands when extracellular calcium levels are low. PTH is coexpressed with furin, the enzyme believed to be responsible for processing proPTH to PTH. PTH is secreted as a C-terminal fragment (7-84) when extracellular calcium levels are high, offsetting the effects of PTH. PTH (7-84) acts as an antagonist for PTH1R, as well as a possible carboxy-terminus interacting PTH receptor. PTH and truncated PTH fragments play a major role in bone metabolism and calcium homeostasis, as well as renal excretion. This particular product has been labeled with the stable 15N isotope to help track its activity.

Human Parathyroid Hormone (PTH) is a hormone expressed and secreted as preproPTH by chief cells of the parathyroid glands when extracellular calcium levels are low. PTH is coexpressed with furin, the enzyme believed to be responsible for processing proPTH to PTH. PTH is secreted as a C-terminal fragment (7-84) when extracellular calcium levels are high, offsetting the effects of PTH. PTH (7-84) acts as an antagonist for PTH1R, as well as a possible carboxy-terminus interacting PTH receptor. PTH and truncated PTH fragments play a major role in bone metabolism and calcium homeostasis, as well as renal excretion.

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

Parathyroid hormone (PTH) is a single polypeptide of 84 amino acids. It is a critical hormone in the regulation of Ca2+ homeostasis and is secreted by the parathyroid glands. These glands promote the release of calcium from bone into the blood stream by activating osteoblasts and inhibiting osteoclasts. Secretion of PTH increases when the level of calcium in the extracellular fluid is low. When there is more Ca2+ in the blood, there is increased intestinal absorption of calcium, renal tubular reabsorption of calcium and increased renal excretion of phosphates. Therefore, PTH is a major regulator of bone metabolism.

Human parathyroid hormone-like hormone (PTHLH) is a hormone that is expressed in mammary glands, as well as cancer cells. Alternative splicing results in different length isoforms of PTHLH. It is involved in a diverse array of processes. PTHLH plays a key role during endochondral ossification by regulating chondrocyte proliferation, differentiation, and apoptosis. It also regulates epithelial-mesenchymal interactions during development of mammary glands and teeth and interacts with dermal fibroblasts to modulate routine skin cell growth and maintenance. PTHLH is a ligand for the PTH1 receptor that is also affected by PTH. This particular product has been labeled with the stable 15N isotope to help track its activity.

Human parathyroid hormone-like hormone (PTHLH) is expressed in mammary glands as well as cancer cells. Alternative splicing results in different length isoforms of PTHLH. It is involved in a diverse array of processes. PTHLH plays a key role during endochondral ossification by regulating chondrocyte proliferation, differentiation, and apoptosis. It also regulates epithelial-mesenchymal interactions during development of mammary glands and teeth and interacts with dermal fibroblasts to modulate routine skin cell growth and maintenance. PTHLH is a ligand for the PTH1 receptor that is also affected by PTH.