Other Proteins

Animal-Free Recombinant Human GDF-5 (BMP-14/CDMP-1) (Legacy Tebubio ref. 167AF-120-01). GDF-5 is expressed in long bones during embryonic development and postnatally in articular cartilage. Mutations in the GDF-5 gene have been implicated in Hunter-Thompson type dwarfism and in Grebe Syndrome, which is characterized by short stature, extra digits, and short and deformed extremities. The mature and functional form of GDF-5 is a homodimer of two 120 amino-acid polypeptide chain (monomers) linked by a single disulfide bond. Each GDF-5 monomer is expressed as the C-terminal part of a precursor polypeptide, which also contains a 27 amino acid signal peptide and a 354 amino acid propeptide. This precursor undergoes intracellular dimerization, and upon secretion it is processed by a furin-type protease. Recombinant Human GDF-5 (BMP-14/CDMP-1) is a 27.0 kDa homodimeric disulfide-linked protein consisting of two 120 amino acid polypeptide chains.

Animal-Free Recombinant Human GDF-5 (BMP-14/CDMP-1) (Legacy Tebubio ref. 167AF-120-01). GDF-5 is expressed in long bones during embryonic development and postnatally in articular cartilage. Mutations in the GDF-5 gene have been implicated in Hunter-Thompson type dwarfism and in Grebe Syndrome, which is characterized by short stature, extra digits, and short and deformed extremities. The mature and functional form of GDF-5 is a homodimer of two 120 amino-acid polypeptide chain (monomers) linked by a single disulfide bond. Each GDF-5 monomer is expressed as the C-terminal part of a precursor polypeptide, which also contains a 27 amino acid signal peptide and a 354 amino acid propeptide. This precursor undergoes intracellular dimerization, and upon secretion it is processed by a furin-type protease. Recombinant Human GDF-5 (BMP-14/CDMP-1) is a 27.0 kDa homodimeric disulfide-linked protein consisting of two 120 amino acid polypeptide chains.

Animal-Free Recombinant Human BMP-13/CDMP-2 (Legacy Tebubio ref. 167AF-120-04). BMP-13 is expressed in hypertrophic chondrocytes during embryonic development of long bones. Continued postnatal expression of BMP-13 in articular cartilage suggests that it plays a regulatory role in the growth and maintenance of articular cartilage. Adenovirus-mediated BMP-13 gene transfer to rabbit bone marrow stem cells have been reported to augment periosteal repair of osteochondral defects. The functional form of BMP-13/CDMP-2 is a disulfide-linked homodimer of two 120 amino-acid polypeptide chains. This 27.5 kDa protein is obtained by proteolytic processing of a biologically inactive precursor protein of 97.7kDa. Recombinant Human BMP-13/CDMP-2 is a 27.0 kDa homodimeric disulfide-linked protein consisting of two 120 amino acid polypeptide chains.

Animal-Free Recombinant Human BMP-13/CDMP-2 (Legacy Tebubio ref. 167AF-120-04). BMP-13 is expressed in hypertrophic chondrocytes during embryonic development of long bones. Continued postnatal expression of BMP-13 in articular cartilage suggests that it plays a regulatory role in the growth and maintenance of articular cartilage. Adenovirus-mediated BMP-13 gene transfer to rabbit bone marrow stem cells have been reported to augment periosteal repair of osteochondral defects. The functional form of BMP-13/CDMP-2 is a disulfide-linked homodimer of two 120 amino-acid polypeptide chains. This 27.5 kDa protein is obtained by proteolytic processing of a biologically inactive precursor protein of 97.7kDa. Recombinant Human BMP-13/CDMP-2 is a 27.0 kDa homodimeric disulfide-linked protein consisting of two 120 amino acid polypeptide chains.

Animal-Free Recombinant Human BMP-4 (E.coli derived) (Legacy Tebubio ref. 167AF-120-05ET). 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.

Animal-Free Recombinant Human BMP-4 (E.coli derived) (Legacy Tebubio ref. 167AF-120-05ET). 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.

Animal-Free Recombinant Human/Murine/Rat Activin A (E.coli derived) (Legacy Tebubio ref. 167AF-120-14E). 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 disulfi

Animal-Free Recombinant Human/Murine/Rat Activin A (E.coli derived) (Legacy Tebubio ref. 167AF-120-14E). 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 disulfi

Animal-Free Recombinant Human GDF-3 (Legacy Tebubio ref. 167AF-120-22). GDF-3 is a member of the TGF-beta superfamily of growth and differentiation factors, and is highly homologous to GDF-9. Unlike most TGF-beta family members, GDF-3 and GDF-9 are not disulfide-linked dimers. GDF-3 is expressed in adult bone marrow, spleen, thymus, and adipose tissue. The expression of GDF-3 is upregulated in high-fat-fed wild-type FABP4/aP2 null mice and was associated with obesity, but not with the related hyperglycemia/hyperinsulinemia that characterizes Type 2 diabetes. Recombinant Human GDF-3 is a 26.0 kDa non-disulfide-linked homodimer containing two 114 amino acid polypeptide chains.