Cytokines & Chemokines

Recombinant Human TWEAK (Legacy Tebubio ref. 167310-06). TWEAK belongs to the TNF family of ligands, and signals through TWEAKR, also known as TNFRSF12A. TWEAK is expressed in a variety of tissues, including the adult heart, pancreas, skeletal muscle, small intestine, spleen and peripheral blood lymphocytes. TWEAK has the ability to induce NF-kappaB activation and chemokine secretion, and to exert an apoptotic activity in certain cells, such as HT-29 human adenocarcinoma cells when cultured in the presence of IFN-gamma. TWEAK also promotes proliferation and migration of endothelial cells. The human TWEAK gene encodes for a 249 amino acid type II transmembrane protein, which contains a 21 amino acid cytoplasmic domain, a 21 amino acid transmembrane domain, and a 207 amino acid extracellular domain. Recombinant Human TWEAK is a soluble 17.0 kDa polypeptide (154 amino acid residues) comprising the TNF-homologous region of TWEAK, and is generated by proteolytic processing of the full lengt

Recombinant Human sCD23 (Legacy Tebubio ref. 167310-26). CD23, the low affinity receptor for IgE, belongs to the C-type lectin structural family and plays a role in the regulation of IgE synthesis and IgE mediated activities. It is found both as a transmembrane receptor protein and in a soluble form, which is generated by proteolytic cleavage of membrane bound CD23. The predominant soluble form of CD23 (sCD23) consists of 172 amino acids corresponding to the extracellular domain of the full length precursor. sCD23, in addition to binding IgE, also exerts a number of IgE-independent activities, such as promoting the activation and differentiation of B cells and stimulating the release of pro-inflammatory cytokines from monocytes. Recombinant Human sCD23 is a 19.2 kDa non-glycosylated protein containing 172 amino-acid residues.

Recombinant Human sCD23 (Legacy Tebubio ref. 167310-26). CD23, the low affinity receptor for IgE, belongs to the C-type lectin structural family and plays a role in the regulation of IgE synthesis and IgE mediated activities. It is found both as a transmembrane receptor protein and in a soluble form, which is generated by proteolytic cleavage of membrane bound CD23. The predominant soluble form of CD23 (sCD23) consists of 172 amino acids corresponding to the extracellular domain of the full length precursor. sCD23, in addition to binding IgE, also exerts a number of IgE-independent activities, such as promoting the activation and differentiation of B cells and stimulating the release of pro-inflammatory cytokines from monocytes. Recombinant Human sCD23 is a 19.2 kDa non-glycosylated protein containing 172 amino-acid residues.

Recombinant Human PD-L1 Fc (Legacy Tebubio ref. 167310-35). Programmed death-ligand 1 (PD-L1), or B7-H1, is a transmembrane, co-stimulatory ligand of programmed cell death protein 1 (PD-1) that, along with B7-1 and B7-2, belongs to the B7 family and immunoglobulin superfamily. Though more notably expressed on activated T cells, B cells, myeloid cells, and a subset of thymocytes, PD-L1 is also expressed constitutively by nonlymphoid, parenchymal organs, including the heart, placenta, skeletal muscle, and lung; with the marked exception of the small intestine. As a member of the B7 family, PD-L1 plays a principal role in immunity: suppressing immune response against autoantigens and tumors, maintaining T cell homeostasis, maintaining peripheral immune tolerance, and regulating T-cell-mediated cytokine secretion. Unlike B7-1 and B7-2, PD-L1 has not been shown to influence immunity through interaction with CD28, CTLA-4 or ICOS, but rather through interaction with PD-1, a weak structural ho

Recombinant Human PD-L1 Fc (Legacy Tebubio ref. 167310-35). Programmed death-ligand 1 (PD-L1), or B7-H1, is a transmembrane, co-stimulatory ligand of programmed cell death protein 1 (PD-1) that, along with B7-1 and B7-2, belongs to the B7 family and immunoglobulin superfamily. Though more notably expressed on activated T cells, B cells, myeloid cells, and a subset of thymocytes, PD-L1 is also expressed constitutively by nonlymphoid, parenchymal organs, including the heart, placenta, skeletal muscle, and lung; with the marked exception of the small intestine. As a member of the B7 family, PD-L1 plays a principal role in immunity: suppressing immune response against autoantigens and tumors, maintaining T cell homeostasis, maintaining peripheral immune tolerance, and regulating T-cell-mediated cytokine secretion. Unlike B7-1 and B7-2, PD-L1 has not been shown to influence immunity through interaction with CD28, CTLA-4 or ICOS, but rather through interaction with PD-1, a weak structural ho

Recombinant Human TREM-1 Fc (Legacy Tebubio ref. 167310-36). Triggering receptor expressed on myeloid cells-1 (TREM-1) is a type 1 transmembrane glycoprotein belonging to the immunoglobulin superfamily of cell surface receptors that is constitutively expressed on the surface of monocytes, neutrophils and macrophages. The first identified member of the TREM family of receptors, TREM-1 is a proponent of amplified inflammatory responses triggered by bacterial and fungal infection, and functions in association with the signal transduction adaptor molecule DAP12. TREM-1 activation induces the sustained secretion of proinflammatory chemokines (IL-8 and MCP-1) and cytokines (TNF-alpha, IL-1beta, and IL-6), the respiratory burst and degranulation of neutrophils, the upregulation of adhesion molecules involved in leukocyte extravasation, and tissue degradation. Involvement and increased expression of TREM-1, or soluble TREM-1, in infectious, as well as some non-infectious, inflammatory conditio

Recombinant Human TREM-1 Fc (Legacy Tebubio ref. 167310-36). Triggering receptor expressed on myeloid cells-1 (TREM-1) is a type 1 transmembrane glycoprotein belonging to the immunoglobulin superfamily of cell surface receptors that is constitutively expressed on the surface of monocytes, neutrophils and macrophages. The first identified member of the TREM family of receptors, TREM-1 is a proponent of amplified inflammatory responses triggered by bacterial and fungal infection, and functions in association with the signal transduction adaptor molecule DAP12. TREM-1 activation induces the sustained secretion of proinflammatory chemokines (IL-8 and MCP-1) and cytokines (TNF-alpha, IL-1beta, and IL-6), the respiratory burst and degranulation of neutrophils, the upregulation of adhesion molecules involved in leukocyte extravasation, and tissue degradation. Involvement and increased expression of TREM-1, or soluble TREM-1, in infectious, as well as some non-infectious, inflammatory conditio

Recombinant Human PD-L2 Fc (Legacy Tebubio ref. 167310-38). Programmed death-ligand 2 (PD-L2), or B7-DC, is a member of the B7 ligand family within the immunoglobulin superfamily that, along with programmed death-ligand 1 (PD-L1), acts as a ligand for programmed cell death protein 1 (PD-1). Though expressed primarily in dendritic cells, PD-L2 expression can be induced on a wide variety of immune and non-immune cells depending on the microenvironment. PD-L2 expression is particularly upregulated in the presence of Th2 cytokine, IL-4, as well as Th1 cytokines, TNF-alpha and IFN-gamma to a lesser degree. While generally expressed at lower levels compared to PD-L1, PD-L2 demonstrates a 2 to 6 times higher relative affinity to PD-1 than PD-L1. PD-1 and its ligands are referred to as inhibitory immune checkpoint molecules in that they provide useful negative feedback during physiological homeostasis. Ligation of PD-L2 or PD-L1 inhibits activation, proliferation, and cytokine secretion (e.g.

Recombinant Human PD-L2 Fc (Legacy Tebubio ref. 167310-38). Programmed death-ligand 2 (PD-L2), or B7-DC, is a member of the B7 ligand family within the immunoglobulin superfamily that, along with programmed death-ligand 1 (PD-L1), acts as a ligand for programmed cell death protein 1 (PD-1). Though expressed primarily in dendritic cells, PD-L2 expression can be induced on a wide variety of immune and non-immune cells depending on the microenvironment. PD-L2 expression is particularly upregulated in the presence of Th2 cytokine, IL-4, as well as Th1 cytokines, TNF-alpha and IFN-gamma to a lesser degree. While generally expressed at lower levels compared to PD-L1, PD-L2 demonstrates a 2 to 6 times higher relative affinity to PD-1 than PD-L1. PD-1 and its ligands are referred to as inhibitory immune checkpoint molecules in that they provide useful negative feedback during physiological homeostasis. Ligation of PD-L2 or PD-L1 inhibits activation, proliferation, and cytokine secretion (e.g.