Cytokines & Chemokines

CD38 (also referred to as T10 antigen) is a nonlineage-restricted type II transmembrane glycoprotein that has emerged as an intracellular calcium ion mobilizing messenger. It can serve as an ectoenzyme that catalyzes the synthesis and hydrolysis of cyclic ADP-ribose. The enzymatic functions of CD38 probably contribute to an array of its immunoregulatory functions. It has been found on the surface of many immune cells (white blood cells), including CD4+, CD8+, B lymphocytes and natural killer cells. Soluble CD38 and the ability of membrane-bound CD38 to become internalized in response to appropriate stimuli suggest that extracellular and intracellular roles for this protein are equally plausible.

CD38 (also referred to as T10 antigen) is a nonlineage-restricted type II transmembrane glycoprotein that has emerged as an intracellular calcium ion mobilizing messenger. It can serve as an ectoenzyme that catalyzes the synthesis and hydrolysis of cyclic ADP-ribose. The enzymatic functions of CD38 probably contribute to an array of its immunoregulatory functions. It has been found on the surface of many immune cells (white blood cells), including CD4+, CD8+, B lymphocytes and natural killer cells. Soluble CD38 and the ability of membrane-bound CD38 to become internalized in response to appropriate stimuli suggest that extracellular and intracellular roles for this protein are equally plausible.

T7 Endonuclease I (T7E1) recognizes and cleaves non-perfectly matched DNA, cruciform DNA structures, Holliday structures or junctions, hetero duplex DNA and more slowly, nicked double-stranded DNA. The cleavage site is at the first, second or third phosphodiester bond that is 5´ to the mismatch. The protein is the product of T7 gene 3. GenCrispr T7 Endonuclease I is a fusion protein produced from <i>E.coli</i>.

T7 Endonuclease I (T7E1) recognizes and cleaves non-perfectly matched DNA, cruciform DNA structures, Holliday structures or junctions, hetero duplex DNA and more slowly, nicked double-stranded DNA. The cleavage site is at the first, second or third phosphodiester bond that is 5´ to the mismatch. The protein is the product of T7 gene 3. GenCrispr T7 Endonuclease I is a fusion protein produced from <i>E.coli</i>.

The IL-2 receptor system consists of three non-covalently linked subunits termed IL-2Rα, IL-2Rβ, and IL-2Rγ. The IL-2Rα is a type I transmembrane protein consisting of a 219 amino acid (a.a.) extracellular domain, a 19 a.a. transmembrane domain and a 13 a.a. intracellular domain, which is not involved in the transduction of IL-2 signal. Activated T cells, regulatory T cells (Tregs) and NK cells express high levels of CD25 and expression of the high-affinity IL-2Rα is mostly limited to these cell populations. Signaling via IL-2Rα mediates multiple biological processes in various cell populations, e.g. proliferation and differentiation of B cells and NK cells. A soluble form of IL-2Rα (IL-2Rα) appears in serum, concomitant with its increased expression on cells. The function of the soluble IL-2Rα is unclear. Increased levels of IL-2Rα in biological fluids reportedly correlate with increased T and B cell activation and immune system activation. Increased serum concentration of IL-2Rα has

The IL-2 receptor system consists of three non-covalently linked subunits termed IL-2Rα, IL-2Rβ, and IL-2Rγ. The IL-2Rα is a type I transmembrane protein consisting of a 219 amino acid (a.a.) extracellular domain, a 19 a.a. transmembrane domain and a 13 a.a. intracellular domain, which is not involved in the transduction of IL-2 signal. Activated T cells, regulatory T cells (Tregs) and NK cells express high levels of CD25 and expression of the high-affinity IL-2Rα is mostly limited to these cell populations. Signaling via IL-2Rα mediates multiple biological processes in various cell populations, e.g. proliferation and differentiation of B cells and NK cells. A soluble form of IL-2Rα (IL-2Rα) appears in serum, concomitant with its increased expression on cells. The function of the soluble IL-2Rα is unclear. Increased levels of IL-2Rα in biological fluids reportedly correlate with increased T and B cell activation and immune system activation. Increased serum concentration of IL-2Rα has

OX40 (TNFRSF4, CD134) is a member of the tumor necrosis factor (TNF) receptor superfamily that regulates T cell activity and immune responses. The OX40 protein contains four cysteine rich domains, a transmembrane domain, and a cytoplasmic tail containing a QEE motif. OX40 is primarily expressed on activated CD4+ and CD8+ T-cells, while the OX40 ligand (OX40L, TNFSF4, CD252) is predominantly expressed on activated antigen presenting cells. The engagement of OX40 with OX40L leads to the recruitment of TNF receptor-associated factors (TRAFs) and results in the formation of a TCR-independent signaling complex. One component of this complex, PKCθ, activates the NF-κB pathway. OX40 signaling through Akt can also enhance TCR signaling directly. Research studies indicate that the OX40L-OX40 pathway is associated with inflammation and autoimmune diseases. Additional research studies show that OX40 agonists augment anti-tumor immunity in several cancer types.

OX40 (TNFRSF4, CD134) is a member of the tumor necrosis factor (TNF) receptor superfamily that regulates T cell activity and immune responses. The OX40 protein contains four cysteine rich domains, a transmembrane domain, and a cytoplasmic tail containing a QEE motif. OX40 is primarily expressed on activated CD4+ and CD8+ T-cells, while the OX40 ligand (OX40L, TNFSF4, CD252) is predominantly expressed on activated antigen presenting cells. The engagement of OX40 with OX40L leads to the recruitment of TNF receptor-associated factors (TRAFs) and results in the formation of a TCR-independent signaling complex. One component of this complex, PKCθ, activates the NF-κB pathway. OX40 signaling through Akt can also enhance TCR signaling directly. Research studies indicate that the OX40L-OX40 pathway is associated with inflammation and autoimmune diseases. Additional research studies show that OX40 agonists augment anti-tumor immunity in several cancer types.

Interleukin-11 is a pleiotropic cytokine that was originally detected in the conditioned medium ofan IL-1α-stimulated primate bone marrow stromal cell line (PU-34) as a mitogen for the IL-6-responsive mouse plasmacytoma cell line T11. IL-11 has multiple effects on both hematopoietic and non-hematopoietic cells. Many of the biological effects described for IL-11 overlap with those for IL-6. In vitro, IL-11 can synergize with IL-3, IL-4 and SCF to shorten the G0 period of early hematopoietic progenitors. IL-11 alsoenhances the IL-3-dependent megakaryocyte colony formation. IL-11 has been found to stimulate the T cell-dependent development of specific immunoglobulin-secreting B cells.