Detection of Mouse NGF R/TNFRSF16 by Western Blot.
Western blot shows lysates of mouse uterus tissue. PVDF membrane was probed with 2 µg/mL of Goat Anti-Mouse NGF R/TNFRSF16 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF1157) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF017). Specific bands were detected for NGF R/TNFRSF16 at approximately 60-75 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
NGF R/TNFRSF16 in Mouse Brain.
NGF R/TNFRSF16 was detected in perfusion fixed frozen sections of mouse brain (cortex) using 7 µg/mL Goat Anti-Mouse NGF R/TNFRSF16 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF1157) overnight at 4 °C. Tissue was stained (red) and counterstained (green). View our protocol for Fluorescent IHC Staining of Frozen Tissue Sections.
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
The low affinity nerve growth factor receptor (NGF R), also named p75 neurotrophin receptor, is a type I transmembrane protein that belongs to the tumor necrosis factor receptor family and has been designated TNFRSF16. 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 of the receptor 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 the amniotic fluid of humans and rats (1-3).
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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We have 4 reviews tested in 2 species: Mouse, Rat,Mouse.
We have 4 review tested in 1 application: Immunohistochemistry.