Other Proteins

Recombinant Human/Murine/Rat GDF-11 (Legacy Tebubio ref. 167120-11). GDF-11 is a myostatin-homologous protein that acts as an inhibitor of nerve tissue growth. GDF-11 has been shown to suppress neurogenesis through a myostatin-like pathway, which involves the arrest of the progenitor cell cycle in the G1 phase. Similarities between myostatin and GDF-11, which are 90% identical in their amino acid sequence, suggest that the regulatory mechanisms responsible for maintaining proper tissue size during neural and muscular development might be the same. Recombinant Human/Murine/Rat GDF-11 is a 25.0 kDa disulfide-linked homodimer containing two 109 amino acid polypeptide chains. It is highly homologous to myostatin/GDF-8, sharing 90% amino acid sequence identity.

Recombinant Human/Murine/Rat GDF-11 (Legacy Tebubio ref. 167120-11). GDF-11 is a myostatin-homologous protein that acts as an inhibitor of nerve tissue growth. GDF-11 has been shown to suppress neurogenesis through a myostatin-like pathway, which involves the arrest of the progenitor cell cycle in the G1 phase. Similarities between myostatin and GDF-11, which are 90% identical in their amino acid sequence, suggest that the regulatory mechanisms responsible for maintaining proper tissue size during neural and muscular development might be the same. Recombinant Human/Murine/Rat GDF-11 is a 25.0 kDa disulfide-linked homodimer containing two 109 amino acid polypeptide chains. It is highly homologous to myostatin/GDF-8, sharing 90% amino acid sequence identity.

Recombinant Human Myostatin-Propeptide (Legacy Tebubio ref. 167120-12). Mature myostatin is obtained by proteolytic processing of a biologically-inactive precursor protein, which contains an N-terminal propeptide of 243 amino acid residues. Myostatin-Propeptide exhibits high binding affinity for myostatin, and has been shown to be a potent inhibitor of myostatin. Over-expression of myostatin-propeptide in mice resulted in large increases (up to 200%) in skeletal muscle mass, similar to those observed in myostatin knockout mice. Recombinant Human Myostatin-Propeptide is a 27.8 kDa protein consisting of 244 amino acid residues.

Recombinant Human Myostatin-Propeptide (Legacy Tebubio ref. 167120-12). Mature myostatin is obtained by proteolytic processing of a biologically-inactive precursor protein, which contains an N-terminal propeptide of 243 amino acid residues. Myostatin-Propeptide exhibits high binding affinity for myostatin, and has been shown to be a potent inhibitor of myostatin. Over-expression of myostatin-propeptide in mice resulted in large increases (up to 200%) in skeletal muscle mass, similar to those observed in myostatin knockout mice. Recombinant Human Myostatin-Propeptide is a 27.8 kDa protein consisting of 244 amino acid residues.

Recombinant Human Follistatin (Legacy Tebubio ref. 167120-13). Follistatin is a secreted protein that binds to ligands of the TGF-beta family and regulates their activity by inhibiting their access to signaling receptors. It was originally discovered as an activin antagonist whose activity suppresses expression and secretion of the pituitary hormone FSH (follicle stimulating hormone). In addition to being a natural antagonist, follistatin can inhibit the activity of other TGF-beta ligands including BMP-2,-4,-6,-7, Myostatin, GDF-11, and TGF-beta1. Follistatin is expressed in the pituitary, ovaries, decidual cells of the endometrium, and in some other tissues. Recombinant Human Follistatin is a 31.5 kDa protein containing 288 amino acids. Its primary structure contains three cysteine-rich domains (called FS domains), each followed by a protease-inhibitory kazal domain.

Recombinant Human Follistatin (Legacy Tebubio ref. 167120-13). Follistatin is a secreted protein that binds to ligands of the TGF-beta family and regulates their activity by inhibiting their access to signaling receptors. It was originally discovered as an activin antagonist whose activity suppresses expression and secretion of the pituitary hormone FSH (follicle stimulating hormone). In addition to being a natural antagonist, follistatin can inhibit the activity of other TGF-beta ligands including BMP-2,-4,-6,-7, Myostatin, GDF-11, and TGF-beta1. Follistatin is expressed in the pituitary, ovaries, decidual cells of the endometrium, and in some other tissues. Recombinant Human Follistatin is a 31.5 kDa protein containing 288 amino acids. Its primary structure contains three cysteine-rich domains (called FS domains), each followed by a protease-inhibitory kazal domain.

Recombinant Human/Murine/Rat Activin A (Insect derived) (Legacy Tebubio ref. 167120-14). Activin A is a TGF-beta family member that exhibits a wide range of biological activities, including regulation of cellular proliferation and differentiation, and promotion of neuronal survival. Elevated levels of Activin A in human colorectal tumors and in postmenopausal women have been implicated in colorectal and breast cancers, respectively. The biological activities of Activin A can be neutralized by inhibins and by the diffusible TGF-beta antagonist, follistatin. Activin A binds to the two forms of activin receptor type I (Act RI-A and Act RI-B) and two forms of activin receptor type II (Act RII-A and Act RII-B). Activins are homodimers or heterodimers of different beta subunits. They are produced as precursor proteins with an amino terminal propeptide that is cleaved to release the C-terminal bioactive ligand. Recombinant Human/Murine/Rat Activin A is a 26.0 kDa disulfide-linked homodim

Recombinant Human/Murine/Rat Activin A (Insect derived) (Legacy Tebubio ref. 167120-14). Activin A is a TGF-beta family member that exhibits a wide range of biological activities, including regulation of cellular proliferation and differentiation, and promotion of neuronal survival. Elevated levels of Activin A in human colorectal tumors and in postmenopausal women have been implicated in colorectal and breast cancers, respectively. The biological activities of Activin A can be neutralized by inhibins and by the diffusible TGF-beta antagonist, follistatin. Activin A binds to the two forms of activin receptor type I (Act RI-A and Act RI-B) and two forms of activin receptor type II (Act RII-A and Act RII-B). Activins are homodimers or heterodimers of different beta subunits. They are produced as precursor proteins with an amino terminal propeptide that is cleaved to release the C-terminal bioactive ligand. Recombinant Human/Murine/Rat Activin A is a 26.0 kDa disulfide-linked homodim

Recombinant Human/Murine/Rat Activin A (E.coli derived) (Legacy Tebubio ref. 167120-14E). Activin A is a TGF-beta family member that exhibits a wide range of biological activities, including regulation of cellular proliferation and differentiation, and promotion of neuronal survival. Elevated levels of Activin A in human colorectal tumors and in postmenopausal women have been implicated in colorectal and breast cancers, respectively. The biological activities of Activin A can be neutralized by inhibins and by the diffusible TGF-beta antagonist, follistatin. Activin A binds to the two forms of activin receptor type I (Act RI-A and Act RI-B) and two forms of activin receptor type II (Act RII-A and Act RII-B). Activins are homodimers or heterodimers of different beta subunits. They are produced as precursor proteins with an amino terminal propeptide that is cleaved to release the C-terminal bioactive ligand. Recombinant Human/Murine/Rat Activin A is a 26.0 kDa disulfide-linked homodi