Other Proteins

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.

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.

Animal-Free Recombinant Human Vitronectin (Legacy Tebubio ref. 167AF-140-09). Vitronectin is a secreted glycoprotein that is synthesized in the liver. It circulates primarily in monomeric form, but can undergo conformational change to a structure that forms disulfide-linked multimers. The multimeric vitronectin can efficiently bind to, and incorporate into, the extracellular matrix. Within the matrix, vitronectin can support cell adhesion through binding to various integrins and other proteoglycans. Additionally, recombinant vitronectin can function as a chemically-defined matrix component in human embryonic stem cell renewal media. Recombinant Human Vitronectin is a 459 amino acid, single-chain, monomeric protein, which migrates at an apparent molecular weight of 75 kDa by SDS-PAGE under reducing conditions. The calculated molecular weight of Recombinant Human Vitronectin is 52.2 kDa.

Animal-Free Recombinant Human Vitronectin (Legacy Tebubio ref. 167AF-140-09). Vitronectin is a secreted glycoprotein that is synthesized in the liver. It circulates primarily in monomeric form, but can undergo conformational change to a structure that forms disulfide-linked multimers. The multimeric vitronectin can efficiently bind to, and incorporate into, the extracellular matrix. Within the matrix, vitronectin can support cell adhesion through binding to various integrins and other proteoglycans. Additionally, recombinant vitronectin can function as a chemically-defined matrix component in human embryonic stem cell renewal media. Recombinant Human Vitronectin is a 459 amino acid, single-chain, monomeric protein, which migrates at an apparent molecular weight of 75 kDa by SDS-PAGE under reducing conditions. The calculated molecular weight of Recombinant Human Vitronectin is 52.2 kDa.

Animal-Free Recombinant Human IL-7 (Legacy Tebubio ref. 167AF-200-07). IL-7 is a hematopoietic growth factor that primarily affects early B and T cells. Produced by thymic stromal cells, spleen cells and keratinocytes, IL-7 can also co-stimulate the proliferation of mature T cells in combination with other factors, such as ConA and IL-2. Human and murine IL-7 are cross-species reactive. Recombinant Human IL-7 is a 17.5 kDa protein containing 153 amino acid residues.

Animal-Free Recombinant Murine IL-2 (Legacy Tebubio ref. 167AF-212-12). IL-2 is a powerful immunoregulatory lymphokine produced by T-cells in response to antigenic or mitogenic stimulation. IL-2/IL-2R signaling is required for T-cell proliferation and other fundamental functions that are essential for the immune response. IL-2 stimulates growth and differentiation of B-cells, NK cells, lymphokine-activated killer cells, monocytes, macrophages and oligodendrocytes. Recombinant Murine IL-2 is a 17.2 kDa protein containing 148 amino acid residues.

Animal-Free Recombinant Murine IL-2 (Legacy Tebubio ref. 167AF-212-12). IL-2 is a powerful immunoregulatory lymphokine produced by T-cells in response to antigenic or mitogenic stimulation. IL-2/IL-2R signaling is required for T-cell proliferation and other fundamental functions that are essential for the immune response. IL-2 stimulates growth and differentiation of B-cells, NK cells, lymphokine-activated killer cells, monocytes, macrophages and oligodendrocytes. Recombinant Murine IL-2 is a 17.2 kDa protein containing 148 amino acid residues.

Animal-Free Recombinant Murine SCF (Legacy Tebubio ref. 167AF-250-03). SCF is a hematopoietic growth factor that exerts its activity by signaling through the c-Kit receptor. SCF and c-Kit are essential for the survival, proliferation and differentiation of hematopoietic cells committed to the melanocyte and germ cell lineages. Human SCF manifests low activity on murine cells, while murine and rat SCF are fully active on human cells. The human SCF gene encodes for a 273 amino acid transmembrane protein, which contains a 25 amino acid N-terminal signal sequence, a 189 amino acid extracellular domain, a 23 amino acid transmembrane domain, and a 36 amino acid cytoplasmic domain. The secreted soluble form of SCF is generated by proteolytic processing of the membrane anchored precursor. Recombinant Murine SCF is an 18.3 kDa polypeptide containing 165 amino acid residues, which corresponds to the sequence of the secreted soluble form of SCF.

Animal-Free Recombinant Murine Noggin (Legacy Tebubio ref. 167AF-250-38). 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. 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 bone formation, and severe osteoporosis. Recombinant Murine Noggin is a 46.4 kDa disulfide-linked homodimer consisting of two 206 amino acid polypeptide chains.