GFAP Antibody, Clone N206A/8: Biotin

Glial fibrillary acidic protein (GFAP) is a 50 kDa type III intermediate filament protein that serves as a major structural component of astrocytes in the central nervous system. GFAP plays a critical role in maintaining astrocyte integrity and function, particularly during responses to neural injury and disease. Its polymerization is tightly regulated through phosphorylation and interactions with calcium-binding proteins such as annexin II-p2 and S-100. One of the earliest cellular responses to brain injury is astrogliosis, a process marked by astrocyte proliferation and increased GFAP expression. Elevated GFAP levels are a hallmark of reactive astrocytes and are commonly observed in neurodegenerative conditions including Alzheimer’s disease, Parkinson’s disease, and multiple sclerosis. Notably, GFAP upregulation reflects both structural remodeling and inflammatory signaling within the diseased brain. Emerging evidence also suggests that autoantibodies targeting GFAP may be present in individuals with dementia and other neurodegenerative disorders, indicating a potential role in neuroimmune interactions and disease progression. Due to its specificity and dynamic expression, GFAP is widely used as a biomarker for astrocyte activation and neuroinflammation. Its involvement in glial responses makes it a valuable target for understanding the cellular mechanisms underlying neurodegeneration and for developing diagnostic and therapeutic strategies aimed at modulating glial function.

1 µg/ml of SMC-441 was sufficient for detection of GFAP in 20 µg of rat brain lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.

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).

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) .