Human/Mouse/Rat NGF R/TNFRSF16 ELISA Standard Curve.
Recombinant Human/Mouse/Rat NGF R/TNFRSF16 (Catalog # 367-NR) was serially diluted 2-fold and captured by Goat Anti-Human/Mouse/Rat NGF R/TNFRSF16 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF367) coated on a Clear Polystyrene Microplate (Catalog # DY990). Goat Anti-Human/Mouse NGF R/TNFRSF16 Biotinylated Antigen Affinity-purified Polyclonal Antibody (Catalog # BAF367) was incubated with the protein captured on the plate. Detection of the standard curve was achieved by incubating Streptavidin-HRP (Catalog # DY998) followed by Substrate Solution (Catalog # DY999) and stopping the enzymatic reaction with Stop Solution (Catalog # DY994).
Preparation and Storage
Reconstitute at 0.2 mg/mL in sterile PBS.
Reconstitution Buffer Available
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: NGF R/TNFRSF16
p75 neurotrophin receptor, also named low affinity NGF receptor (NGF R), is a type I transmembrane protein that belongs to the tumor necrosis factor receptor family. NGF R cDNA encodes a 427 amino acid (aa) residue precursor protein with a 28 aa residue signal peptide, a 222 aa residue extracellular domain, a 22 aa residue transmembrane domain and a 155 aa residue intracellular domain. The extracellular region contains four cysteine-rich domains and binds NGF, BDNF, NT-3, and NT-4 approximately equally with low affinity. The cytoplasmic region contains a subtype 2 death domain.
NGF R expression has been shown to occur widely during development and in the adult. Expression has been detected in both neuronal and non-neuronal cells. NGF R was originally reported to function as a positive regulator of TrkA activity. NGF R has also been shown to signal by itself. Depending on its cellular environment, NGF R has now been shown to regulate cell migration, gene expression and to mediate apoptosis. Recombinant NGF R Fc chimera binds NGF with high affinity and is a potent NGF antagonist. Naturally occurring truncated NGF R containing the extracellular domain and lacking the transmembrane or intracellular domain has been detected in vivo in urine, plasma and in amniotic fluid of humans and rats.
Barker, P.A. and R.A. Murphy (1992) Molecular and Cellular Biochemistry 110:1.
Bamji, A.X. et al. (1998) J. Cell Biol. 140:911.
Feinstein, E. et al. (1995) Trends Biochem. Sci. 20:342.
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