Other Proteins

Recombinant Human ROR1 (Legacy Tebubio ref. 167160-04). Receptor-tyrosine-kinase-like orphan receptor 1 (ROR1) is a tumor-associated, surface protein predominantly expressed during embryogenesis, where it is involved in organ morphogenesis, nervous system development, and neural progenitor cell maintenance and survival. Virtually absent from normal pediatric and adult tissues, with the exception of low-level expression in a subset of immature b cell precursors known as hematogones and adipocytes, ROR1 is notably overexpressed, and considered a survival factor, in a number of B lymphoid and epithelial malignancies: including chronic lymphocytic leukemia (CLL), mantle cell lymphoma (MCL), acute lymphoblastic leukemia (ALL), marginal zone lymphoma, lung adenocarcinoma. First identified during PCR-based cloning of a human neuroblastoma cell line in search of tyrosine kinases similar to tropomyosin-receptor-kinase (Trk) neurotropic receptors, ROR1, along with the related receptor tyrosine k

Recombinant Human ROR1 (Legacy Tebubio ref. 167160-04). Receptor-tyrosine-kinase-like orphan receptor 1 (ROR1) is a tumor-associated, surface protein predominantly expressed during embryogenesis, where it is involved in organ morphogenesis, nervous system development, and neural progenitor cell maintenance and survival. Virtually absent from normal pediatric and adult tissues, with the exception of low-level expression in a subset of immature b cell precursors known as hematogones and adipocytes, ROR1 is notably overexpressed, and considered a survival factor, in a number of B lymphoid and epithelial malignancies: including chronic lymphocytic leukemia (CLL), mantle cell lymphoma (MCL), acute lymphoblastic leukemia (ALL), marginal zone lymphoma, lung adenocarcinoma. First identified during PCR-based cloning of a human neuroblastoma cell line in search of tyrosine kinases similar to tropomyosin-receptor-kinase (Trk) neurotropic receptors, ROR1, along with the related receptor tyrosine k

Recombinant Human FGFR3 (IIIc) Fc (Legacy Tebubio ref. 167160-05). The FGF family plays a central role during prenatal development and postnatal growth, and the regeneration of a variety of tissues, by promoting cellular proliferation and differentiation. The FGF ligands bind to a family of type I transmembrane tyrosine kinase receptors, which leads to dimerization and activation by sequential autophosphorylation of specific tyrosine residues. Four genes encoding structurally related FGF receptors (FGFR-1 to -4) are known. Alternative splicing of the mRNAs generates numerous forms of FGFR-1 to -3. Alternate forms of FGF receptors can exhibit different specificities with respect to ligand binding. For example, the form designated as FGFR1a (IIc) interacts predominantly with FGF-acidic (FGF1) and FGF-basic (FGF2). A frequent splicing event involving FGFR-1 and -2 results in receptors containing all three Ig domains, referred to as the alpha isoform, or only IgII and IgIII, referred to as

Recombinant Human FGFR3 (IIIc) Fc (Legacy Tebubio ref. 167160-05). The FGF family plays a central role during prenatal development and postnatal growth, and the regeneration of a variety of tissues, by promoting cellular proliferation and differentiation. The FGF ligands bind to a family of type I transmembrane tyrosine kinase receptors, which leads to dimerization and activation by sequential autophosphorylation of specific tyrosine residues. Four genes encoding structurally related FGF receptors (FGFR-1 to -4) are known. Alternative splicing of the mRNAs generates numerous forms of FGFR-1 to -3. Alternate forms of FGF receptors can exhibit different specificities with respect to ligand binding. For example, the form designated as FGFR1a (IIc) interacts predominantly with FGF-acidic (FGF1) and FGF-basic (FGF2). A frequent splicing event involving FGFR-1 and -2 results in receptors containing all three Ig domains, referred to as the alpha isoform, or only IgII and IgIII, referred to as

Recombinant Human IL-1RA (Legacy Tebubio ref. 167200-01RA). Interleukin-1 receptor antagonist (IL-1RA) is a naturally-occurring, inflammatory-inhibitor protein. It inhibits the activity of IL-1alpha and IL-1beta by competitively blocking their binding to type I and type II receptors. IL-1RA is produced by corneal epithelial cells, monocytes, neutrophils, macrophages, and fibroblasts. Therapeutically, IL-1RA may help in the treatment of sepsis, cachexia, rheumatoid arthritis, chronic myelogenous leukemia, asthma, psoriasis, and inflammatory bowel disease. Recombinant Human IL-1RA is a 17.2 kDa protein consisting of 153 amino acid residues.

Recombinant Human IL-1RA (Legacy Tebubio ref. 167200-01RA). Interleukin-1 receptor antagonist (IL-1RA) is a naturally-occurring, inflammatory-inhibitor protein. It inhibits the activity of IL-1alpha and IL-1beta by competitively blocking their binding to type I and type II receptors. IL-1RA is produced by corneal epithelial cells, monocytes, neutrophils, macrophages, and fibroblasts. Therapeutically, IL-1RA may help in the treatment of sepsis, cachexia, rheumatoid arthritis, chronic myelogenous leukemia, asthma, psoriasis, and inflammatory bowel disease. Recombinant Human IL-1RA is a 17.2 kDa protein consisting of 153 amino acid residues.

Recombinant Human IL-2 (Legacy Tebubio ref. 167200-02). 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 Human IL-2 is a 15.5 kDa protein, containing 134 amino acid residues including one intrachain disulfide bond.

Recombinant Human IL-2 (Legacy Tebubio ref. 167200-02). 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 Human IL-2 is a 15.5 kDa protein, containing 134 amino acid residues including one intrachain disulfide bond.

Recombinant Human sIL-2 Receptor alpha (CHO derived) (Legacy Tebubio ref. 167200-02RC). The IL-2 receptor system consists of three non-covalently linked subunits termed IL-2Ralpha, IL-2Rbeta, and IL-2Rgamma. The IL-2Ralpha is a type I transmembrane protein consisting of a 219 amino acid extracellular domain, a 19 amino acid transmembrane domain and a 13 amino acid intracellular domain, which is not involved in the transduction of IL-2 signals. Proteolytic processing of IL-2Ralpha releases the entire extracellular domain of IL-2Ralpha, thereby generating a 219 amino acid soluble protein called soluble IL-2Ralpha (sIL-2Ralpha). The homodimeric form binds IL-2 (KD=10mM) and facilitates IL-2 signaling. The secreted sIL-2Ralpha is expressed on leukemia cells, lymphoma cells, and newly activated T and B cells, as well as on approximately 10% of NK cells. Recombinant Human sIL-2 Receptor alpha is a 24.8 kDa protein containing 219 amino acid residues consisting of only the extracellular d