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NGFR (192-IgG, p75) Mouse Monoclonal, Alexa488-labeled [AB-N43-FLA]

$504.00

SKU: AB-N43-FLA Categories: , Quantity: 50 ug | Antibody Type: Monoclonal | Host: mouse | Reactivity: rat | Conjugate: Alexa488 | Usage: flow cytometry, fluorescence applications |

192-IgG is the antibody to the p75 neurotrophin receptor (p75NTR). The p75NTR, also known as the low affinity nerve growth factor receptor, binds nerve growth factor, brain-derived neurotrophic factor, neurotrophin-3 and neurotrophin-4 with varying specificities. The p75NTR plays an important role in neurotrophic factor signaling and has been shown to modulate the susceptibility of selective cellular populations to programmed cell death.

This fluorescent conjugate recognizes p75 receptor-positive cells in rat. It was prepared using mouse monoclonal antibody 192-IgG conjugated to Alexa 488. This product is routinely tested by flow cytometry.

Applications include flow cytometry, fluorescence spectroscopy, fluorescence anisotropy, epifluorescence microscopy, qualitative probe of binding to membrane-bound IgG’s and the cytoskeleton.

keywords: P75NTR, NGFR, Alzheimer’s Disease, dementia, basal forebrain, animal model, neuronal loss, low affinity nerve growth factor, neurotrophin receptors, mesenchyme, Anti-NGFR, Anti-Nerve Growth Factor, 192-IgG, p75, fluorescent, Alexa488, brain, neuroscience

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Environment and mobility of a series of fluorescent reporters at the amino terminus of structurally related peptide agonists and antagonists bound to the cholecystokinin receptor.

Harikumar KG, Pinon DI, Wessels WS, Prendergast FG, Miller LJ (2002) Environment and mobility of a series of fluorescent reporters at the amino terminus of structurally related peptide agonists and antagonists bound to the cholecystokinin receptor. J Biol Chem 277(21):18552-18560. doi: 10.1074/jbc.M201164200 PMID: 11893747

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Analysis of fluorescently labeled substance P analogs: binding, imaging and receptor activation.

Bennett VJ, Simmons MA (2001) Analysis of fluorescently labeled substance P analogs: binding, imaging and receptor activation. BMC Chem Biol 1(1):1. doi: 10.1186/1472-6769-1-1 PMID: 11418083

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Characterization of immunoglobulin binding to isolated human erythrocyte membranes: evidence for selective, temperature-induced binding of naturally occurring autoantibodies to the cytoskeleton.

Salhany JM, Cordes KS, Sloan RL (2001) Characterization of immunoglobulin binding to isolated human erythrocyte membranes: evidence for selective, temperature-induced binding of naturally occurring autoantibodies to the cytoskeleton. Biochim Biophys Acta 1511(1):168-180. doi: 10.1016/s0005-2736(01)00280-2 PMID: 11248215

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