Death Receptor 6 Recombinant Protein
851.8 EUR
In Stock
quantity
Produktdetaljer
Katalognummer: 223 - 92-146
Produktkategori: Företag och industri > Vetenskap och laboratorium
Gentaur
Storlek: 0.05 mg
91-303
Death Receptor 6 Recombinant Protein
Tumor Necrosis Factor Receptor Superfamily Member 21 (TNFRSF21) is a type I transmembrane receptor that includes four extracellular cysteine-rich motifs and a cytoplasmic death domain. DR6 is highly expressed in heart, brain, placenta, pancreas, lymph node, thymus and prostate. DR6 may activate NF-kappa-B and JNK to promote apoptosis and T-cell differentiation. In addition, DR6 binds with N-APP, which is released by the deprivation of Trophic-factor. It triggers caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6). DR6 is also expressed on the tumor cell lines and can be induced by TNF- alpha.
738.4 €
91-950
Death Receptor 6 Recombinant Protein
Tumor necrosis factor receptor superfamily member 21(DR6) is a single-pass type I membrane protein and contains 1 death domain and 4 TNFR-Cys repeats. The protein may activate NF-kappa-B and promote apoptosis and it may activate JNK and be involved in T-cell differentiation.It is required for both normal cell body death and axonal pruning. Trophic-factor deprivation triggers the cleavage of surface APP by beta-secretase to release sAPP-beta which is further cleaved to release an N-terminal fragment of APP (N-APP). N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6).
1012.45 €
40-671
IL-6 Receptor Recombinant Protein
IL-6 mediates its biological effects through the type I IL-6 receptor system that consists of two chains, IL-6Rα and gp130. While the IL-6Rα chain is the binding component specific to IL-6, the gp130 chain only transmits signals of IL-6 when bound to IL-6Rα. The gp130 can also transmit signals from LIF, OSM, CNTF, IL-11 and CT-1 in conjunction with other receptor subunits. The low-affinity binding site for IL-6 is composed of IL-6Rα alone. IL-6Rα is expressed in a wide range of cells, including T cells, fibroblasts and macrophages. Soluble IL-6Rα, which consists of only the extracellular domain of the IL-6Rα chain, acts as an agonist of IL-6 activity at low concentrations. Recombinant Human sIL-6Rα is a 37.6 kDa protein consisting of the extracellular domain of the IL-6Rα chain (339 amino acid residues).
596.65 €