Other Proteins

Recombinant Human BMP-4 (HeLa derived) (Legacy Tebubio ref. 167120-05). Bone morphogenetic proteins (BMPs) constitute a subfamily within the TGF-beta superfamily of structurally related signaling proteins. Members of this superfamily are widely distributed throughout the body, and are involved in diverse physiological processes during both pre- and postnatal life. Like BMP-7, BMP-4 is involved in the development and maintenance of bone and cartilage. Reduced expression of BMP-4 is associated with a number of bone diseases, including the heritable disorder Fibrodysplasia Ossificans Progressiva. Recombinant Human BMP-4, expressed in HeLa cells, is a 25.6 kDa homodimeric glycoprotein.

Recombinant Human BMP-4 (E.coli derived) (Legacy Tebubio ref. 167120-05ET). Bone morphogenetic proteins (BMPs) constitute a subfamily within the TGF-beta superfamily of structurally related signaling proteins. Members of this superfamily are widely distributed throughout the body, and are involved in diverse physiological processes during both pre- and postnatal life. Like BMP-7, BMP-4 is involved in the development and maintenance of bone and cartilage. Reduced expression of BMP-4 is associated with a number of bone diseases, including the heritable disorder Fibrodysplasia Ossificans Progressiva. PeproTech's E.coli-derived BMP-4 is a fully active homodimeric protein consisting of two 106 amino acid subunits, which correspond to amino acids 303-408 of the full length BMP-4 precursor. The calculated molecular weight of Recombinant Human BMP-4 (E.coli-derived) is 23.9 kDa.

Recombinant Human BMP-4 (E.coli derived) (Legacy Tebubio ref. 167120-05ET). Bone morphogenetic proteins (BMPs) constitute a subfamily within the TGF-beta superfamily of structurally related signaling proteins. Members of this superfamily are widely distributed throughout the body, and are involved in diverse physiological processes during both pre- and postnatal life. Like BMP-7, BMP-4 is involved in the development and maintenance of bone and cartilage. Reduced expression of BMP-4 is associated with a number of bone diseases, including the heritable disorder Fibrodysplasia Ossificans Progressiva. PeproTech's E.coli-derived BMP-4 is a fully active homodimeric protein consisting of two 106 amino acid subunits, which correspond to amino acids 303-408 of the full length BMP-4 precursor. The calculated molecular weight of Recombinant Human BMP-4 (E.coli-derived) is 23.9 kDa.

Recombinant Human BMP-6 (Legacy Tebubio ref. 167120-06). TGF-beta family members are key modulators of cell proliferation, differentiation, matrix synthesis, and apoptosis. As implied by their name, BMPs initiate, promote, and regulate the development, growth, and remodeling of bone and cartilage. In addition to this role, BMPs are also involved in prenatal development and postnatal growth, remodeling, and maintenance of a variety of other tissues and organs. Increasing evidence indicates that BMP-Smad signaling has a tumor suppressing activity, and that BMPs can inhibit tumor growth. BMP-6 is abnormally expressed in breast cancer cell lines, however, its function in promoting breast cancer development is unknown. The mature and functional form of BMP-6 is a homodimer of two identical 139 amino acid polypeptide chains linked by a single disulfide bond. Each monomer is expressed as the C-terminal part of a precursor polypeptide, which contains a 20 amino acid signal peptide and a 354 am

Recombinant Human BMP-6 (Legacy Tebubio ref. 167120-06). TGF-beta family members are key modulators of cell proliferation, differentiation, matrix synthesis, and apoptosis. As implied by their name, BMPs initiate, promote, and regulate the development, growth, and remodeling of bone and cartilage. In addition to this role, BMPs are also involved in prenatal development and postnatal growth, remodeling, and maintenance of a variety of other tissues and organs. Increasing evidence indicates that BMP-Smad signaling has a tumor suppressing activity, and that BMPs can inhibit tumor growth. BMP-6 is abnormally expressed in breast cancer cell lines, however, its function in promoting breast cancer development is unknown. The mature and functional form of BMP-6 is a homodimer of two identical 139 amino acid polypeptide chains linked by a single disulfide bond. Each monomer is expressed as the C-terminal part of a precursor polypeptide, which contains a 20 amino acid signal peptide and a 354 am

Recombinant Human TSG (Legacy Tebubio ref. 167120-09). Twisted Gastrulation Protein (TSG) is a secreted BMP-binding protein that is structurally related to the BMP antagonists Chordin and Noggin. TSG can inhibit BMP activity by binding directly to BMP proteins, and can act either as a BMP-4 agonist or antagonist (depending on the specific biochemical environment) by binding to the BMP-4/Chordin complex. Recombinant Human TSG is a 198 amino acid, 22.2 kDa protein containing the BMP/TGF-beta binding portion of the full length TSG protein.

Recombinant Human TSG (Legacy Tebubio ref. 167120-09). Twisted Gastrulation Protein (TSG) is a secreted BMP-binding protein that is structurally related to the BMP antagonists Chordin and Noggin. TSG can inhibit BMP activity by binding directly to BMP proteins, and can act either as a BMP-4 agonist or antagonist (depending on the specific biochemical environment) by binding to the BMP-4/Chordin complex. Recombinant Human TSG is a 198 amino acid, 22.2 kDa protein containing the BMP/TGF-beta binding portion of the full length TSG protein.

Recombinant Human Noggin (Legacy Tebubio ref. 167120-10C). Noggin belongs to a group of diffusible proteins that bind to ligands of the TGF-beta family, and regulate their activity by inhibiting their access to signaling receptors. The interplay between TGF-beta ligands and their natural antagonists has major biological significance during development processes, in which cellular response can vary considerably depending upon the local concentration of the signaling molecule. Noggin was originally identified as a BMP-4 antagonist whose action was critical for proper formation of the head and other dorsal structures. Consequently, noggin has been shown to modulate the activities of other BMPs including BMP-2,-7,-13, and -14. Targeted deletion of noggin in mice results in prenatal death, and a recessive phenotype displaying a severely malformed skeletal system. Conversely, transgenic mice over-expressing noggin in mature osteoblasts display impaired osteoblastic differentiation, reduced

Recombinant Human Noggin (Legacy Tebubio ref. 167120-10C). Noggin belongs to a group of diffusible proteins that bind to ligands of the TGF-beta family, and regulate their activity by inhibiting their access to signaling receptors. The interplay between TGF-beta ligands and their natural antagonists has major biological significance during development processes, in which cellular response can vary considerably depending upon the local concentration of the signaling molecule. Noggin was originally identified as a BMP-4 antagonist whose action was critical for proper formation of the head and other dorsal structures. Consequently, noggin has been shown to modulate the activities of other BMPs including BMP-2,-7,-13, and -14. Targeted deletion of noggin in mice results in prenatal death, and a recessive phenotype displaying a severely malformed skeletal system. Conversely, transgenic mice over-expressing noggin in mature osteoblasts display impaired osteoblastic differentiation, reduced