CD40 Ligand Recombinant Protein (Animal Free)
621.71 €
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product details
Catalog number: 223 - 40-759
Product Category: Business & Industrial > Science & Laboratory
Gentaur
Size: 10 ug
40-758
sRank Ligand Recombinant Protein (Animal Free)
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 sRANKL is a 20.0 kDa polypeptide comprising the TNF-homologous region of RANKL (176 amino acid residues).
621.71 €
100-115-AF
Human CD40-Ligand (Animal Free) Recombinant Protein
CD40, a member of the TNF receptor superfamily, is a cell surface protein expressed on B cells, dendritic cells, monocytes, thymic epithelial cells and, at low levels, on T cells. Signaling though CD40 plays an important role in the proliferation and differentiation of B cells, and is critical for immunoglobulin (Ig) class switching. The membrane-anchored CD40 Ligand is expressed almost exclusively on activated CD4+ T lymphocytes. Failure to express CD40L leads to “immunodeficiency with hyper-IgM”, a disease characterized by failure to produce IgG, IgA and IgE. The human CD40L gene codes for a 261 amino acid type II transmembrane protein, which contains a 22 amino acid cytoplasmic domain, a 24 amino acid transmembrane domain, and a 215 amino acid extracellular domain. The soluble form of CD40L is an 18 kDa protein comprising the entire TNF homologous region of CD40L and is generated in vivo by an intracellular proteolytic processing of the full length CD40L. Recombinant Human soluble CD40 ligand is a 16.3 kDa protein containing 149 amino acid residues comprising the receptor binding TNF-like domain of CD40L.
499.87 €
100-115S-AF
Human CD40-Ligand (Animal Free) Recombinant Protein
CD40, a member of the TNF receptor superfamily, is a cell surface protein expressed on B cells, dendritic cells, monocytes, thymic epithelial cells and, at low levels, on T cells. Signaling though CD40 plays an important role in the proliferation and differentiation of B cells, and is critical for immunoglobulin (Ig) class switching. The membrane-anchored CD40 Ligand is expressed almost exclusively on activated CD4+ T lymphocytes. Failure to express CD40L leads to “immunodeficiency with hyper-IgM”, a disease characterized by failure to produce IgG, IgA and IgE. The human CD40L gene codes for a 261 amino acid type II transmembrane protein, which contains a 22 amino acid cytoplasmic domain, a 24 amino acid transmembrane domain, and a 215 amino acid extracellular domain. The soluble form of CD40L is an 18 kDa protein comprising the entire TNF homologous region of CD40L and is generated in vivo by an intracellular proteolytic processing of the full length CD40L. Recombinant Human soluble CD40 ligand is a 16.3 kDa protein containing 149 amino acid residues comprising the receptor binding TNF-like domain of CD40L.
355.12 €
100-128-AF
Human Artemin (Animal Free) Recombinant Protein
Artemin is a disulfide-linked homodimeric neurotrophic factor structurally related to GDNF, Artemin, Neurturin and Persephin. These proteins belong to the cysteine knot superfamily of growth factors that assume stable dimeric protein structures. Artemin, GDNF, Persephin and Neurturin all signal through a multicomponent receptor system, composed of RET (receptor tyrosine kinase) and one of the four GFRα (α1-α4) receptors. Artemin prefers the receptor GFRα3-RET, but will use other receptors as an alternative. Artemin supports the survival of all peripheral ganglia, such as sympathetic, neural crest and placodally-derived sensory neurons, and dopaminergic midbrain neurons. The functional human Artemin ligand is a disulfide-linked homodimer of two 12.0 kDa polypeptide monomers. Each monomer contains seven conserved cysteine residues, one of which is used for interchain disulfide bridging and the others are involved in intramolecular ring formation known as the cysteine-knot configuration.Recombinant Human Artemin is a 24.2 kDa, disulfide-linked homodimer formed by two identical 113 amino acid subunits.
499.87 €
100-128S-AF
Human Artemin (Animal Free) Recombinant Protein
Artemin is a disulfide-linked homodimeric neurotrophic factor structurally related to GDNF, Artemin, Neurturin and Persephin. These proteins belong to the cysteine knot superfamily of growth factors that assume stable dimeric protein structures. Artemin, GDNF, Persephin and Neurturin all signal through a multicomponent receptor system, composed of RET (receptor tyrosine kinase) and one of the four GFRα (α1-α4) receptors. Artemin prefers the receptor GFRα3-RET, but will use other receptors as an alternative. Artemin supports the survival of all peripheral ganglia, such as sympathetic, neural crest and placodally-derived sensory neurons, and dopaminergic midbrain neurons. The functional human Artemin ligand is a disulfide-linked homodimer of two 12.0 kDa polypeptide monomers. Each monomer contains seven conserved cysteine residues, one of which is used for interchain disulfide bridging and the others are involved in intramolecular ring formation known as the cysteine-knot configuration.Recombinant Human Artemin is a 24.2 kDa, disulfide-linked homodimer formed by two identical 113 amino acid subunits.
355.12 €
100-336-AF
Human Epiregulin (Animal Free) Recombinant Protein
Epiregulin is an EGF-related growth factor that binds specifically to EGFR (ErbB1) and ErbB4, but not ErbB2 or ErbB3. It is expressed mainly in the placenta and peripheral blood leukocytes, as well as in certain carcinomas of the bladder, lung, kidney and colon. Epiregulin stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts and vascular smooth muscle cells. It also inhibits the growth of several tumor-derived epithelial cell lines. Human Epiregulin is initially synthesized as a glycosylated 19.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a 6.0 kDa mature secreted sequence. Recombinant Human Epiregulin is a 5.6 kDa monomeric protein, containing 50 amino residues, which corresponds to the mature secreted Epiregulin sequence.