AREG (Amphiregulin) is an EGF related growth factor containing 6 conserved cysteine residues, which form 3 intramolecular disulfide bonds essential for biological activity. It was originally isolated from the MCF-7 human breast carcinoma cell line and is expressed in numerous carcinoma cell lines, as well as the epithelial cells of various human tissues including colon, stomach, breast, ovary, and kidney. AREG participates in autocrine signaling and binds to an EGF/TGF-α receptor, stimulating growth of keratinocytes, epithelial cells and some fibroblasts. It also inhibits the growth of certain carcinoma cell lines. It is synthesized as a transmembrane protein and the ectodomain is cleaved by a protease to release the mature protein. Overexpression of AREG produces a cutaneous phenotype resembling psoriasis.

BTC (Betacellulin) is an EGF related growth factor containing 6 conserved cysteine residues, which form 3 intramolecular disulfide bonds essential for biological activity. It was originally isolated from the MCF-7 human breast carcinoma cell line and it is expressed in most tissues including kidney, uterus, liver and pancreas. BTC is also present in body fluids, including serum, milk, and colostrum. BTC is a ligand for the receptors erbB1 and erbB4. It is synthesized as a transmembrane protein and the ectodomain is cleaved by a protease to release the mature protein. BTC exhibits mitogenic activity for retinal pigment epithelial cells and vascular smooth muscle cells. It also exhibits growth-promoting activity that is similar to that of EGF.

BTC (Betacellulin) is an EGF related growth factor containing 6 conserved cysteine residues, which form 3 intramolecular disulfide bonds essential for biological activity. It was originally isolated from the MCF-7 human breast carcinoma cell line and it is expressed in most tissues including kidney, uterus, liver and pancreas. BTC is also present in body fluids, including serum, milk, and colostrum. BTC is a ligand for the receptors erbB1 and erbB4. It is synthesized as a transmembrane protein and the ectodomain is cleaved by a protease to release the mature protein. BTC exhibits mitogenic activity for retinal pigment epithelial cells and vascular smooth muscle cells. It also exhibits growth-promoting activity that is similar to that of EGF.

EGF (Epidermal Growth Factor) is a family of growth factors that are derived from membrane-anchored precursors. The family is characterized by the presence of at least one “EGF-like domain” (characterized by the presence of three disulfide bonds, formed from 6 conserved cysteine residues) in their extracellular domain. EGF was originally discovered as an activity that induced early eyelid opening, incisor eruption, hair growth inhibition and stunting of growth when injected into newborn mice. Mature human EGF shares 70% amino acid sequence identity with mature mouse and rat EGF. Human EGF was isolated from urine based on its inhibitory effect on gastric secretion and is sometimes called urogastrone.

EGF (Epidermal Growth Factor) is a family of growth factors that are derived from membrane-anchored precursors. The family is characterized by the presence of at least one “EGF-like domain” (characterized by the presence of three disulfide bonds, formed from 6 conserved cysteine residues) in their extracellular domain. EGF was originally discovered as an activity that induced early eyelid opening, incisor eruption, hair growth inhibition and stunting of growth when injected into newborn mice. Additionally, EGF has been shown to inhibit gastric secretion, is involved in wound healing and signals through a receptor known as c-erbB (a class I tyrosine kinase receptor).

EGF (Epidermal Growth Factor) is a family of growth factors that are derived from membrane-anchored precursors. The family is characterized by the presence of at least one “EGF-like domain” (characterized by the presence of three disulfide bonds, formed from 6 conserved cysteine residues) in their extracellular domain. EGF was originally discovered as an activity that induced early eyelid opening, incisor eruption, hair growth inhibition and stunting of growth when injected into newborn mice. Additionally, EGF has been shown to inhibit gastric secretion, is involved in wound healing and signals through a receptor known as c-erbB (a class I tyrosine kinase receptor).

EPGN is a member of the epidermal growth factor family and expression has been seen in several tissues, including the testis, liver, heart and certain tumor cells. It is a strong mitogen for fibroblasts and epithelial cells but has low affinity for its main receptor, ErbB1. The enhanced mitogenic potential is attributed to inefficient receptor ubiquitylation and endocytosis. EPGN stimulates phosphorylation of c- erbB-1 and MAP kinases in epithelial cells. The protein contains a conserved sequence of six cysteine residues and two N-linked glycosylation sites, with two hydrophobic regions comprised of a signal sequence and a transmembrane domain. Alternative splicing of the EPGN gene results in multiple isoforms.

EREG is a member of the epidermal growth factor (EGF) family and is expressed mainly in the placenta and peripheral blood leukocytes, as well as in certain carcinomas of the bladder, lung, kidney, and colon. EREG stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts and vascular smooth muscle cells. Additionally, it inhibits the growth of several tumor-derived epithelial cell lines. EREG is synthesized as a transmembrane protein and the ectodomain is cleaved by a protease to release the mature protein. The mature protein can bind to EGFR, as well as most members of the ERBB family of RTKs.

Heparin-binding epidermal growth factor-like growth factor (HBEGF) is synthesized as a transmembrane precursor that is cleaved by a protease to release HBEGF as the ectodomain. Its expression stimulates neurogenesis and is increased after the brain experiences cerebral hypoxia. HBEGF is known to participate in a variety of normal physiological processes such as blastocyst implantation and wound healing, as well as in pathological processes such as tumor growth, SMC hyperplasia and atherosclerosis. HBEGF is a glycoprotein exhibiting mitogenic and chemotactic activity in smooth muscle cells and fibroblasts.

Heparin-binding epidermal growth factor-like growth factor (HBEGF) is synthesized as a transmembrane precursor that is cleaved by a protease to release HBEGF as the ectodomain. Its expression stimulates neurogenesis and is increased after the brain experiences cerebral hypoxia. HBEGF is known to participate in a variety of normal physiological processes such as blastocyst implantation and wound healing, as well as in pathological processes such as tumor growth, SMC hyperplasia and atherosclerosis. HBEGF is a glycoprotein exhibiting mitogenic and chemotactic activity in smooth muscle cells and fibroblasts.

Heparin-binding epidermal growth factor-like growth factor (HBEGF) is synthesized as a transmembrane precursor that is cleaved by a protease to release HBEGF as the ectodomain. Its expression stimulates neurogenesis and is increased after the brain experiences cerebral hypoxia. HBEGF is known to participate in a variety of normal physiological processes such as blastocyst implantation and wound healing, as well as in pathological processes such as tumor growth, SMC hyperplasia and atherosclerosis. HBEGF is a glycoprotein exhibiting mitogenic and chemotactic activity in smooth muscle cells and fibroblasts.