GFAP R416WT Antibody, Clone N206B/9

Glial fibrillary acidic protein (GFAP) is a 50 kDa type III intermediate filament protein that serves as a key structural component of astrocytes in the central nervous system. It plays a critical role in maintaining astrocyte architecture and function. GFAP polymerization is regulated through phosphorylation and interactions with calcium-binding proteins such as annexin II-p2 and S-100, enabling dynamic responses to physiological and pathological stimuli. One of the earliest and most prominent astrocytic responses to central nervous system injury is astrogliosis, characterized by astrocyte proliferation and hypertrophy. A hallmark of this process is the upregulation of GFAP expression, making it a widely used biomarker for reactive astrocytes and neuroinflammation. In the context of neurodegenerative diseases—including Alzheimer’s disease, Parkinson’s disease, and multiple sclerosis—elevated GFAP levels reflect ongoing glial activation and are associated with disease progression. Notably, autoantibodies against GFAP have been detected in individuals with dementia, suggesting a potential link between astrocytic dysfunction and neuroimmune mechanisms in neurodegeneration. Due to its specificity and responsiveness to neural injury, GFAP is extensively used in both experimental and clinical neuroscience as a diagnostic and prognostic marker. Its role in glial biology and neuroinflammation continues to make it a focal point in the development of therapeutic strategies targeting astrocyte-mediated pathology.

Synthetic peptide amino acids 411-422 (KTVEMRDGEVIK) of human GFAP; 100% identical in rat and mouse. >50% identity with other proteins (Vimentin, Desmin and Peripherin) .

1 µg/ml of SMC-442 was sufficient for detection of GFAP R416WT in 20 µg of rat brain lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.

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1. Velasco M.E., et al. (1980) Cancer. 45:484. 2. Bonnin J.M., et al. (1984) Acta Neuropathology. 62:185. 3. Lee VM-Y., et al. (1984) J. Neurochem. 42:25-32 (1984) . 4. Trojanowski JQ et al. (1986) J. Neurochem. 6 (3) : 650-660 (1986) . 5. Schmidt ML et al; Lab Invest 56:282-294 (1987) . 6. Kosik KS et al; Neuron 1:817-825 (1988) . 7. Schmidt ML et al; Lab Invest 59:460-466 (1988) . 8. Mokuna, K, et al: J Neurosci Res 23:396 (1989) . 9. Molenaar, et al; Exp Neurology 108:1-9 (1990) . 10. Tohyama T et al; Am J Pathol, 142:871-882 (1993) . 11. Tohyama T et al; Am J Pathol 142:883-892 (1993) . 12. Thilenius, A.R.B., et al; J. Immunol. 162 (2) : 643-650 (1999) .