Mouse Anti-Rat p75 NGF Receptor (extracellular) Antibody

p75NTR, NGFR p75, TNFR superfamily member 16, TNFRSF16, CD271
    Cat #: AN-170
  • Lyophilized Powder
  • Shipped at Room Temp.
  • Type: Monoclonal
    Source: Mouse
    Reactivity: r
    Immunogen
    Solubilized proteins from PC12 membranes.
    Peptide confirmation Confirmed by amino acid analysis and mass spectrometry.
    Purity Purified from cultured hybridoma medium on immobilized rProtein G.
    Formulation Lyophilized powder. Reconstituted antibody contains phosphate buffered saline (PBS), pH 7.4, 1% BSA, 0.05% NaN3.
    Isotype IgG1.
    Specificity 192-IgG reacts with rat p75NTR. It does not cross-react with p75NTR of human or mouse origin.
    Clone 192-IgG.
    Storage before reconstitution The antibody ships as a lyophilized powder at room temperature. Upon arrival, it should be stored at -20°C.
    Reconstitution 10 μl, 50 μl, 100 μl or 250 μl double distilled water (DDW), depending on the sample size.
    Antibody concentration after reconstitution 1 mg/ml.
    Storage after reconstitution The reconstituted solution can be stored at 4°C for up to 1 week. For longer periods, small aliquots should be stored at -20°C. Avoid multiple freezing and thawing. Centrifuge all antibody preparations before use (10000 x g 5 min).
    Control antigen storage before reconstitution Lyophilized powder can be stored intact at room temperature for 2 weeks. For longer periods, it should be stored at -20°C.
    Control antigen reconstitution 100 µl double distilled water (DDW).
    Control antigen storage after reconstitution -20°C.
    Standard quality control of each lot Western blot analysis.
    Applications: ifc, ih, wb
    May also work in: ic, ip
    Western blot
    Western blot analysis of PC12 cell lysate (non-reduced):
    1. Mouse Anti-Rat p75 NGF Receptor (extracellular) Antibody (#AN-170), (1:2500).
    2. Mouse Anti-Rat p75 NGF Receptor (extracellular) Antibody (1:1500).
    3. Mouse Anti-Rat p75 NGF Receptor (extracellular) Antibody (1:150).
    Immunohistochemistry
    Immuno-colocalization of Plexin-A2 and p75NTR in rat brain
    Immunohistochemical staining of perfusion-fixed frozen rat brain sections using Anti-Plexin-A2 (extracellular) Antibody (#APR-082), (1:400) and Mouse Anti-Rat p75 NGF Receptor (extracellular) Antibody (#AN-170), (1:300). A. Sections of rat horizontal diagonal band (HDB) were stained for Plexin-A2 (green). B. Same sections were stained for p75NTR (red). C. Merge of the two images reveals cells expressing both Plexin-A2 and p75NTR (horizontal arrows), cells expressing only Plexin-A2 (upwards pointing arrows) or cells expressing only p75NTR (downwards pointing arrows) can also be observed. Cell nuclei are stained with DAPI (blue).
    Indirect flow cytometry
    PC12 cells.
    References
    1. Dechant, G. et al. (1997) Curr. Opin. Neurobiol. 7, 413.
    2. Cosgaya, J.M. et al. (2002) J. Science 298, 1245.
    3. Yamashita, T. et al. (2003) Nature Neurosci. 6, 461.
    4. Bentley, C.A. et al. (2000) J. Neurosci. 20, 7706.
    5. Lee, R. et al. (2001) Science 294, 1945.
    6. Bibel, M. et al. (2000) Genes Dev. 14, 2919.
    7. Salehi, A.H. et al. (2002) J. Biol. Chem. 277, 48043.
    8. Casademunt, E. et al. (1999) EMBO J. 18, 6050.
    9. Yaar, M. et al. (1997) J. Clin. Invest. 100, 2333.
    Scientific background

    p75NTR known as a cell surface receptor for NGF, BDNF, NT-3 and NT-4, is also a receptor for b-amyloid, and for the myelin axon repellant protein MAG.1,2,4,6 Binding of neurotrophins induces receptor dimerization followed by phosphorylation of receptor kinase residues and recruitment of intracellular proteins involved in signal transduction.

    p75NTR functions alone, or in functional complexes with the neurotrophin receptors trkA, trkB and trkC. p75NTR signals via interaction with different transducers such as TRAF6, IRAK, and RIP-2, activating NF-κB, JNK and p38, and inactivating rhoA.1,3,6 

    Receptor degradation is mediated by a metalloproteinase-dependent shedding of the extracellular domain. p75NTR binds all neurotrophins with similar nM affinity, but binds pro-neurotrophins with greater affinity, and is more potently activated by pro-neurotrophins.5

    Overexpression of the intracellular domain in developing neurons induces apoptosis. NGF-dependent association of NRIF with p75NTR contributes to pro-apoptotic signaling.7,8 

    Beta-amyloid peptide binds p75NTR and stimulates pro apoptotic signaling by p75NTR, suggesting that the receptor may be relevant for Alzheimer's disease.9

    Application key:

    CBE- Cell-based ELISA, FC- Flow cytometry, ICC- Immunocytochemistry, IE- Indirect ELISA, IFC- Indirect flow cytometry, IHC- Immunohistochemistry, IP- Immunoprecipitation, LCI- Live cell imaging, N- Neutralization, WB- Western blot

    Species reactivity key:

    H- Human, M- Mouse, R- Rat
    Image & Title:

    Mouse Anti-Rat p75 NGF Receptor (extracellular) AntibodyImmuno-colocalization of Vesicular Acetylcholine Transporter and p75NTR in rat medial septum.Immunohistochemical staining of immersion-fixed, free floating rat brain frozen sections using rabbit Anti-Vesicular Acetylcholine Transporter (VAChT) Antibody (#ACT-003), (1:200) and Mouse Anti-Rat p75 NGF Receptor (extracellular) Antibody (#AN-170), (1:200). A. VAChT staining (green) appears in several neuronal cells. B. p75NTR (red) also stains neuronal cells. C. Merge of the two images shows colocalization of VAChT and p75NTR in some cells (horizontal arrows), while other cells express only VAChT (vertical arrows). Cell nuclei are stained with DAPI (blue).

    Last update: 27/11/2018

    Mouse Anti-Rat p75 NGF Receptor (extracellular) Antibody (#AN-170) is a highly specific monoclonal antibody directed against p75NTR. The antibody can be used in western blot, immunohistochemistry, and indirect flow cytometry applications. It has been designed to recognize p75NTR from rat samples only.

    For research purposes only, not for human use
    Citations
    More product citations
    1. Urra, S. et al. (2007) J. Biol. Chem. 282, 7606.
    2. Tan, J. et al. (2006) Am. J. Pathol. 169, 528.
    3. Kuwako, K. et al. (2005) J. Neurosci. 25, 7090.
    4. Tcherpakov, M. et al. (2002) J. Biol. Chem. 277, 49101.
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