Receptor for TNFSF5/CD40LG. Transduces TRAF6- and MAP3K8-mediated signals that activate ERK in macrophages and B cells, leading to induction of immunoglobulin secretion.
Host
Rabbit
Immunogen
Peptide sequence around phosphorylation site of threonine 254 (Q-E-T(p)-L-H) derived from Human TNFRSF5.
Involvement In Disease
Immunodeficiency with hyper-IgM 3 (HIGM3)
Raised In
Rabbit
Reactivity
Human, Mouse
Regulatory
RUO
Relevance
Receptor for TNFSF5/CD40LG. Transduces TRAF6- and MAP3K8-mediated signals that activate ERK in macrophages and B cells, leading to induction of immunoglobulin secretion.
Species
Homo Sapiens (Human)
Specificity
The antibody detects endogenous levels of TNFRSF5 only when phosphorylated at threonine 254.
Subcellular Location
Isoform I: Cell membrane, Single-pass type I membrane protein, SUBCELLULAR LOCATION: Isoform II: Secreted
Receptor for TNFSF5/CD40LG. Transduces TRAF6- and MAP3K8-mediated signals that activate ERK in macrophages and B cells, leading to induction of immunoglobulin secretion.
Pathway
NF-kappa B signaling pathway Toll-like receptor signaling pathway
Tissue Specificity
B-cells and in primary carcinomas.
Buffer
Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
Form
Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
Format
liquid
Purification
Antibodies were produced by immunizing rabbits with synthetic phosphopeptide and KLH conjugates. Antibodies were purified by affinity-chromatography using epitope-specific phosphopeptide. Non-phospho specific antibodies were removed by chromatogramphy usi
Purity
Antibodies were produced by immunizing rabbits with synthetic phosphopeptide and KLH conjugates. Antibodies were purified by affinity-chromatography using epitope-specific phosphopeptide. Non-phospho specific antibodies were removed by chromatogramphy using non-phosphopeptide.
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.