Catalog number: 544 - MBS566041-002mg
Product Category: Business & Industrial > Science & Laboratory
Size: 0.02mg
100-156
RANKL and RANK are members of the TNF superfamily of ligands and receptors that play an important role in the regulation of specific immunity and bone turnover. RANK (receptor) was originally identified as a dendritic cell-membrane protein, which, by interacting with RANKL, augments the ability of dendritic cells. These dendritic cells then stimulate naïve T-cell proliferation in a mixed lymphocyte reaction,promote the survival of RANK + T-cells, and regulate T-cell-dependent immune response. RANKL, which is expressed in a variety of cells,including osteoblasts, fibroblasts, activated T-cells and bone marrow stromal cells, is also capable of interacting with a decoy receptor called OPG. Binding of soluble OPG to sRANKL inhibits osteoclastogenesis by interrupting the signaling between stromal cells and osteoclastic progenitor cells, thereby leading to excess accumulation of bone and cartilage. Human RANKL is reactive on murine cells. Recombinant Human sRANK Ligand is a 22.1 kDa polypeptide comprised of the TNF-homologous region of RANKL and a N-terminal His-tag.
100-156S
RANKL and RANK are members of the TNF superfamily of ligands and receptors that play an important role in the regulation of specific immunity and bone turnover. RANK (receptor) was originally identified as a dendritic cell-membrane protein, which, by interacting with RANKL, augments the ability of dendritic cells. These dendritic cells then stimulate naïve T-cell proliferation in a mixed lymphocyte reaction,promote the survival of RANK + T-cells, and regulate T-cell-dependent immune response. RANKL, which is expressed in a variety of cells,including osteoblasts, fibroblasts, activated T-cells and bone marrow stromal cells, is also capable of interacting with a decoy receptor called OPG. Binding of soluble OPG to sRANKL inhibits osteoclastogenesis by interrupting the signaling between stromal cells and osteoclastic progenitor cells, thereby leading to excess accumulation of bone and cartilage. Human RANKL is reactive on murine cells. Recombinant Human sRANK Ligand is a 22.1 kDa polypeptide comprised of the TNF-homologous region of RANKL and a N-terminal His-tag.
100-276
RANKL and RANK are members of the TNF superfamily of ligands and receptors that play an important role in the regulation of specific immunity and bone turnover. RANK (receptor) was originally identified as a dendritic-cell-membrane protein, which by interacting with RANKL augments the ability of dendritic cells to stimulate naïve T-cell proliferation in a mixed lymphocyte reaction, to promote the survival of RANK + T cells, and to regulate T-cell-dependent immune response. RANKL, which is expressed in a variety of cells including osteoblasts, fibroblasts, activated T-cells and bone marrow stromal cells, is also capable of interacting with a decoy receptor called OPG. Binding of soluble OPG to sRANKL inhibits osteoclastogenesis by interrupting the signaling between stromal cells and osteoclastic progenitor cells, thereby leading to excess accumulation of bone and cartilage. Recombinant human sRANKL is a 20.0 kDa polypeptide comprising the TNF homologous region of RANKL (176 amino acid residues).
S01-041
CD27 Ligand, a type II transmembrane protein, is a member of the TNF superfamily. It is expressed on activated T and B lymphocytes as well as NK cells. CD27L and its receptor (CD27) regulate the immune response by promoting T-cell expansion and differentiation, as well as NK enhancement. CD27 signaling can act as a co-stimulatory effector to sustain the survival of CD8+ T cells, primarily by inducing increased expression of the IL-2 gene. Full length human CD27L is a 193 amino acid protein, consisting of a 17 amino acid cytoplasmic domain, a 21 amino acid transmembrane domain, and a 155 amino acid extracellular domain. Human soluble CD27L corresponds to the 155 amino acid extracellular domain of the full length CD27L protein. The provided human sCD27L protein contains the extracellular domain plus an N-terminal His-Tag.
S01-041S
CD27 Ligand, a type II transmembrane protein, is a member of the TNF superfamily. It is expressed on activated T and B lymphocytes as well as NK cells. CD27L and its receptor (CD27) regulate the immune response by promoting T-cell expansion and differentiation, as well as NK enhancement. CD27 signaling can act as a co-stimulatory effector to sustain the survival of CD8+ T cells, primarily by inducing increased expression of the IL-2 gene. Full length human CD27L is a 193 amino acid protein, consisting of a 17 amino acid cytoplasmic domain, a 21 amino acid transmembrane domain, and a 155 amino acid extracellular domain. Human soluble CD27L corresponds to the 155 amino acid extracellular domain of the full length CD27L protein. The provided human sCD27L protein contains the extracellular domain plus an N-terminal His-Tag.
S01-042
The type-II membrane-associated glycoprotein CD30 ligand (CD30L) is a protein belonging to the TNF superfamily. The CD30L gene encodes for a 234 amino acid type II transmembrane protein, which contains a 37 amino acid cytoplasmic sequence, a 25 amino acid transmembrane domain and a 172 amino acid extracellular domain. The protein is expressed primarily on certain B cells, T cells, and monocytes. CD30L binds specifically to CD30 (receptor), which is expressed on activated, but not resting, B and T cells, in lymphomas and various chronically inflamed tissues. CD30L/CD30 interactions initiate a signaling cascade that can ultimately lead to the activation of NF-KappaB. CD30L/CD30 signaling exerts pleiotropic effects on normal cells, including cell death, differentiation, or cell division. Certain diseases, including Hodgkins’s lymphoma, allergic inflammation, diabetes (in NOD mice), and mycobacterial infection can also be affected by CD30L/CD30 signaling. The provided recombinant human soluble CD30L (sCD30L) is a 188 amino acid polypeptide corresponding to the extracellular domain, and contains an 8 residue N-terminal His -Tag.