Other Proteins

Animal-Free Recombinant Human IL-5 (Legacy Tebubio ref. 167AF-05). IL-5 is a hematopoietic growth factor that stimulates the proliferation and activation of eosinophils. Produced by mast cells, T cells, and eosinophils, IL-5 plays an important role in inducing cell-mediated immunity against parasitic infections and certain tumors. Elevated levels of IL-5 lead to Eosinophilia, which may result in the induction of asthma and other allergic diseases. Human and murine IL-5 are cross-species reactive. Recombinant Human IL-5 is a 26.5 kDa disulfide-linked homodimeric protein containing two 116 amino acid chains.

Animal-Free Recombinant Human IL-5 (Legacy Tebubio ref. 167AF-05). IL-5 is a hematopoietic growth factor that stimulates the proliferation and activation of eosinophils. Produced by mast cells, T cells, and eosinophils, IL-5 plays an important role in inducing cell-mediated immunity against parasitic infections and certain tumors. Elevated levels of IL-5 lead to Eosinophilia, which may result in the induction of asthma and other allergic diseases. Human and murine IL-5 are cross-species reactive. Recombinant Human IL-5 is a 26.5 kDa disulfide-linked homodimeric protein containing two 116 amino acid chains.

Animal-Free Recombinant Human IL-7 (Legacy Tebubio ref. 167AF-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 Human IL-7 (Legacy Tebubio ref. 167AF-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 Human IL-36gamma (IL-1F9) (Legacy Tebubio ref. 167AF-36G). The IL-1 family is comprised of 11 structurally related ligands, including recently re-named IL-36 alpha (IL-1F6), beta (IL-1F8) and gamma (IL-1F9). IL-36gamma is highly expressed in psoriatic plaques and in tissues containing epithelial cells. IL-36gamma signals through the IL-1Rrp2 (IL-1R6) receptor, which is primarily expressed on certain dendritic cells. The interaction of the IL-1Rrp2 receptor with IL-36 ligands induces dendritic cell maturation and activation. IL-36gamma also functions as an agonist of NF-kappaB, and can stimulate the inflammatory response in bronchial epithelial cells. Recombinant Human IL-36gamma is a 17.0 kDa protein containing 152 amino acid residues.

Animal-Free Recombinant Human IL-36gamma (IL-1F9) (Legacy Tebubio ref. 167AF-36G). The IL-1 family is comprised of 11 structurally related ligands, including recently re-named IL-36 alpha (IL-1F6), beta (IL-1F8) and gamma (IL-1F9). IL-36gamma is highly expressed in psoriatic plaques and in tissues containing epithelial cells. IL-36gamma signals through the IL-1Rrp2 (IL-1R6) receptor, which is primarily expressed on certain dendritic cells. The interaction of the IL-1Rrp2 receptor with IL-36 ligands induces dendritic cell maturation and activation. IL-36gamma also functions as an agonist of NF-kappaB, and can stimulate the inflammatory response in bronchial epithelial cells. Recombinant Human IL-36gamma is a 17.0 kDa protein containing 152 amino acid residues.

Animal-Free Recombinant Murine Noggin (Legacy Tebubio ref. 167AF-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.

Animal-Free Recombinant Murine Noggin (Legacy Tebubio ref. 167AF-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.

Animal-Free Recombinant Murine BD-3 (Legacy Tebubio ref. 167AF-41). Defensins (alpha and beta) are cationic peptides with a broad spectrum of antimicrobial activity that comprise an important arm of the innate immune system. The alpha-defensins are distinguished from the beta-defensins by the pairing of their three disulfide bonds. To date, six human beta-defensins have been identified; BD-1, BD-2, BD-3, BD-4, BD-5 and BD-6. beta-defensins are expressed on some leukocytes and at epithelial surfaces. In addition to their direct antimicrobial activities, they can act as chemoattractants towards immature dendritic cells and memory T cells. The beta-defensin proteins are expressed as the C-terminal portion of precursors, and are released by proteolytic cleavage of a signal sequence and, in some cases, a propeptide sequence. Beta-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds. Recombinant Murine BD-3 is a 4.6 kDa protein containing 41 amino acid resi