Other Proteins

Recombinant Human Granzyme B (Legacy Tebubio ref. 167140-18). Recombinant Human Granzyme B is a 235 amino acid protein, which includes the mature 227 amino acid sequence, as well as an 8 amino acid C-terminal His-tag. Due to glycosylation, this protein migrates to an approximate molecular weight of 30-40 kDa, under reducing and non-reducing conditions.

Recombinant Human Agrin (Legacy Tebubio ref. 167160-08). Agrin is a molecule that resides in the basal lamina of muscle cells and directs key events in post synaptic differentiation. Most notably, Agrin is responsible for the clustering of acetylcholine receptors (AChRs) on the cell surface and their localization to the neuromuscular junction. Several Agrin variants have been identified which arise from alternative mRNA splicings. Agrin splice forms having inserts at two sites in the carboxy terminus designated "y" and "z" display a high affinity for AChRs, while splice forms lacking these inserts associate with AChRs weakly. Muscle alpha-dystroglycan has been postulated to be the receptor for the clustering activity of agrin; however, this is a point of contention. Tyrosine phosphorylation has been implicated as a required early step in AChR aggregation. Interestingly, a unique receptor tyrosine kinase, designated MuSK, has been discovered that interacts with Agrin and is specifically

Recombinant Human Agrin (Legacy Tebubio ref. 167160-08). Agrin is a molecule that resides in the basal lamina of muscle cells and directs key events in post synaptic differentiation. Most notably, Agrin is responsible for the clustering of acetylcholine receptors (AChRs) on the cell surface and their localization to the neuromuscular junction. Several Agrin variants have been identified which arise from alternative mRNA splicings. Agrin splice forms having inserts at two sites in the carboxy terminus designated "y" and "z" display a high affinity for AChRs, while splice forms lacking these inserts associate with AChRs weakly. Muscle alpha-dystroglycan has been postulated to be the receptor for the clustering activity of agrin; however, this is a point of contention. Tyrosine phosphorylation has been implicated as a required early step in AChR aggregation. Interestingly, a unique receptor tyrosine kinase, designated MuSK, has been discovered that interacts with Agrin and is specifically

Recombinant Human sIL-2 Receptor Beta Fc (Legacy Tebubio ref. 167200-02RB). CD122 (Interleukin 2 receptor) is involved in T cell-mediated immune responses, primarily expressed in the hematopoietic system and is present in 3 forms. The low affinity form of CD122 is a monomer of the alpha subunit and is not involved in signal transduction. The intermediate affinity form consists of an alpha/beta subunit heterodimer, while the high affinity form consists of an alpha/beta/gamma subunit heterotrimer. Both the intermediate and high affinity forms of the receptor are involved in receptor-mediated endocytosis and transduction of mitogenic signals from CD122. The protein encoded by the CD122 gene represents the beta subunit and is a type I membrane protein. Diseases associate with CD122 protein dysfunction include oligoarticular juvenile idiopathic arthritis and rheumatoid factor negative juvenile idiopathic arthritis. Recombinant Human sIL-2 Receptor Beta Fc is a 53.5 kDa protein of 473 amino

Recombinant Human sIL-2 Receptor Beta Fc (Legacy Tebubio ref. 167200-02RB). CD122 (Interleukin 2 receptor) is involved in T cell-mediated immune responses, primarily expressed in the hematopoietic system and is present in 3 forms. The low affinity form of CD122 is a monomer of the alpha subunit and is not involved in signal transduction. The intermediate affinity form consists of an alpha/beta subunit heterodimer, while the high affinity form consists of an alpha/beta/gamma subunit heterotrimer. Both the intermediate and high affinity forms of the receptor are involved in receptor-mediated endocytosis and transduction of mitogenic signals from CD122. The protein encoded by the CD122 gene represents the beta subunit and is a type I membrane protein. Diseases associate with CD122 protein dysfunction include oligoarticular juvenile idiopathic arthritis and rheumatoid factor negative juvenile idiopathic arthritis. Recombinant Human sIL-2 Receptor Beta Fc is a 53.5 kDa protein of 473 amino

Recombinant Human sIL-7 Receptor Alpha Fc (Legacy Tebubio ref. 167200-07RA). CD127 (Interleukin-7, IL-7) is a glycoprotein involved in the regulation of lymphopoiesis. The response of cells to CD127 is dependent on the presence of the interleukin 7 receptor (IL7R); the active receptor is an alpha/gamma chain heterodimer. CD127 consists of an alpha chain and a gamma chain. The gamma(c) chain, which also associates with the interleukin-2 receptor, serves primarily to activate signal transduction by the IL7R complex, while the alpha chain of IL7R determines specific signaling events through its association with cytoplasmic signaling molecules. CD127 promotes the proliferation of precursor B cells, thymocytes, T cell progenitors, and mature CD4+ and CD8+ T cells. The biological effects of IL7 are mediated by the binding of IL7 to the specific cell surface receptor. Diseases associated with CD127 dysfunction include severe combined immunodeficiency and T cell negative/B cell negative/NK pos

Recombinant Human sIL-7 Receptor Alpha Fc (Legacy Tebubio ref. 167200-07RA). CD127 (Interleukin-7, IL-7) is a glycoprotein involved in the regulation of lymphopoiesis. The response of cells to CD127 is dependent on the presence of the interleukin 7 receptor (IL7R); the active receptor is an alpha/gamma chain heterodimer. CD127 consists of an alpha chain and a gamma chain. The gamma(c) chain, which also associates with the interleukin-2 receptor, serves primarily to activate signal transduction by the IL7R complex, while the alpha chain of IL7R determines specific signaling events through its association with cytoplasmic signaling molecules. CD127 promotes the proliferation of precursor B cells, thymocytes, T cell progenitors, and mature CD4+ and CD8+ T cells. The biological effects of IL7 are mediated by the binding of IL7 to the specific cell surface receptor. Diseases associated with CD127 dysfunction include severe combined immunodeficiency and T cell negative/B cell negative/NK pos

Recombinant Human sIL-12 Receptor Beta-2 Fc (Legacy Tebubio ref. 167200-12RB-2). The IL-12 structurally related family of heterodimeric proteins plays an important role in activating, regulating, and modulating the immune response. This family of proteins transmits its activity through receptors, which, when stimulated by ligand binding, generally activate JAK proteins that subsequently phosphorylate STAT transcription factors. IL-12R β-2 is a single pass membrane protein expressed primarily on certain naive T cells. By itself, IL-12R β-2 appears to exert minimal activity but when paired with IL-12R β-1, forms a high affinity IL-12 receptor. IL-12R β-2 can also pair with gp130 to form a high affinity receptor for IL-35. Recombinant Human IL-12 Receptor β-2 Fc has a calculated molecular weight of 94.9 kDa, and contains 839 amino acid residues, which consists of the extracellular domain of IL-12R β-2 fused to the Fc portion of human IgG and contains a C-terminal His-tag. Due to glycosyla

Recombinant Human sIL-12 Receptor Beta-2 Fc (Legacy Tebubio ref. 167200-12RB-2). The IL-12 structurally related family of heterodimeric proteins plays an important role in activating, regulating, and modulating the immune response. This family of proteins transmits its activity through receptors, which, when stimulated by ligand binding, generally activate JAK proteins that subsequently phosphorylate STAT transcription factors. IL-12R β-2 is a single pass membrane protein expressed primarily on certain naive T cells. By itself, IL-12R β-2 appears to exert minimal activity but when paired with IL-12R β-1, forms a high affinity IL-12 receptor. IL-12R β-2 can also pair with gp130 to form a high affinity receptor for IL-35. Recombinant Human IL-12 Receptor β-2 Fc has a calculated molecular weight of 94.9 kDa, and contains 839 amino acid residues, which consists of the extracellular domain of IL-12R β-2 fused to the Fc portion of human IgG and contains a C-terminal His-tag. Due to glycosyla