FGF1 is a member of the Fibroblast Growth Factor family of proteins. Also called FGF-acidic or aFGF, FGF1 lacks signal peptides and is believed to be secreted by a nonclassical mechanism. It has been detected in large amounts in the brain and is expressed in hepatocyte cells, vascular smooth muscle cells, CNS neurons, skeletal muscle cells, fibroblasts, keratinocytes, endothelial cells, intestinal columnar epithelial cells, and pituitary basophils and acidophils. FGF1 exhibits considerable species cross-reactivity and stimulates the proliferation of cells of mesodermal origin, as well as many cells of neuroectodermal, ectodermal, and endodermal origin. It is most closely associated with FGF2 (bFGF) (see additional information).

FGF1 is a member of the Fibroblast Growth Factor family of proteins. Also called FGF-acidic or aFGF, FGF1 lacks signal peptides and is believed to be secreted by a nonclassical mechanism. It has been detected in large amounts in the brain and is expressed in hepatocyte cells, vascular smooth muscle cells, CNS neurons, skeletal muscle cells, fibroblasts, keratinocytes, endothelial cells, intestinal columnar epithelial cells and pituitary basophils and acidophils. FGF1 exhibits considerable species cross-reactivity and stimulates the proliferation of cells of mesodermal origin as well as many cells of neuroectodermal, ectodermal, and endodermal origin. It is most closely associated with FGF2 (bFGF) (see additional information).

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.

FGF2 is a member of the fibroblast growth factor family of proteins. It is often called FGF-basic or bFGF. FGF2 is a single-chain polypeptide growth factor that plays a significant role in wound healing, it is a potent inducer of angiogenesis and it is essential for the growth of many stem and progenitor cells. FGF2 shares a 55% amino acid residue identity with FGF1 and interacts with heparin sulfate with nanomolar affinity. It is a potent inducer of DNA synthesis in a variety of cell types. FGF2 activates mesenchymal splice variants of FGF receptors (c splice variants) and also activates FGF Receptor 1b, but has little activity against FGFR2b or FGFR3b. It is most closely associated with FGF1 (aFGF) (see additional information).

FGF2 is a member of the fibroblast growth factor family of proteins. It is often called FGF-basic or bFGF. FGF2 is a single-chain polypeptide growth factor that plays a significant role in wound healing, it is a potent inducer of angiogenesis and it is essential for the growth of many stem and progenitor cells. FGF2 shares a 55% amino acid residue identity with FGF1 and interacts with heparin sulfate with nanomolar affinity. It is a potent inducer of DNA synthesis in a variety of cell types. FGF2 activates mesenchymal splice variants of FGF receptors (c splice variants) and also activates FGF Receptor 1b, but has little activity against FGFR2b or FGFR3b. It is most closely associated with FGF1 (aFGF).

FGF2 is a member of the Fibroblast Growth Factor family of proteins. It is often called FGF-basic or bFGF. FGF2 is a single-chain polypeptide growth factor that plays a significant role in wound healing, it is a potent inducer of angiogenesis and it is essential for the growth of many stem and progenitor cells. FGF2 shares a 55% amino acid residue identity with FGF1 and interacts with heparin sulfate with nanomolar affinity. It is a potent inducer of DNA synthesis in a variety of cell types. FGF2 activates mesenchymal splice variants of FGF receptors (c splice variants) and also activates FGF Receptor 1b, but has little activity against FGFR2b or FGFR3b. It is most closely associated with FGF1 (aFGF) (see additional information).

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

Recombinant Rat Fibroblast Growth Factor 2Fibroblast Growth Factor-basicbFGF, FGF-2basic FGF

FGF2 is a member of the Fibroblast Growth Factor family of proteins. It is often called FGF-basic or bFGF. FGF2 is a single-chain polypeptide growth factor that plays a significant role in wound healing, it is a potent inducer of angiogenesis and it is essential for the growth of many stem and progenitor cells. FGF2 shares a 55% amino acid residue identity with FGF1 and interacts with heparin sulfate with nanomolar affinity. It is a potent inducer of DNA synthesis in a variety of cell types. FGF2 activates mesenchymal splice variants of FGF receptors (c splice variants) and also activates FGF Receptor 1b, but has little activity against FGFR2b or FGFR3b. It is most closely associated with FGF1 (aFGF) (see additional information).

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

Source: Escherichia coli

Bone Morphogenetic Proteins (BMPs) belong to the TGF-β (Transforming Growth Factor) superfamily of structurally related signaling proteins. BMP2 is a potent osteoinductive cytokine, capable of inducing bone and cartilage formation in association with osteoconductive carriers such as collagen and synthetic hydroxyapatite. In addition, BMP2 plays an important role in cardiac morphogenesis and is expressed in a variety of tissues; including the lung, spleen, brain, liver, prostate, ovary and small intestine. The functional form of BMP2 is a 26kDa protein composed of two identical 115 amino acid polypeptide chains linked by a single disulfide bond.

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

Bone Morphogenetic Proteins (BMPs) belong to the TGF-β (Transforming Growth Factor) superfamily of structurally related signaling proteins. BMP7 is one of at least 15 structurally and functionally related BMPs, originally identified as protein regulators of cartilage and bone formation which have since been shown to be involved in embryogenesis and morphogenesis of various tissues and organs. BMPs have been shown to regulate the growth, differentiation, chemotaxis and apoptosis of a variety of cell types; including mesenchymal cells, epithelial cells, hematopoietic cells and neuronal cells. The active form of BMP7 can consist of a dimer of two identical proteins or a heterodimer of two related BMPs. BMP7 is expressed highest in the kidneys and is genetically linked in mice to eye, skeletal and kidney development.

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.