Overview
- Peptide (C)RHLGTIPRLSLSR, corresponding to amino acid residues 27-39 of rat Glial fibrillary acidic protein (Accession P47819). Intracellular, cytoplasm.
Western blot analysis of rat brain synaptosome lysates (lanes 1 and 3) and mouse brain lysates (lanes 2 and 4):1-2. Guinea Pig Anti-GFAP Antibody (#AFP-001-GP), (1:500).
3-4. Guinea Pig Anti-GFAP Antibody, preincubated with GFAP Blocking Peptide (BLP-FP001).
Expression of GFAP in rat parietal cortex.Immunohistochemical staining of perfusion-fixed frozen rat brain sections with Guinea Pig Anti-GFAP Antibody (AFP-001-GP). Sections were incubated with guinea pig anti GFAP (#AFP-001-GP), (1:1200), followed by goat anti guinea pig conjugated with Alexa 594 (red). A, GFAP immunoreactivity appears in cortical astrocytes in layers 1-2 (arrows). B, Pre-incubation of the antibody with GFAP blocking peptide (BLP-FP001), suppressed staining. Cell nuclei are stained with DAPI (blue).
Multiplex staining of CLEC7A and GFAP in rat hippocampal CA1 regionImmunohistochemical staining of perfusion-fixed frozen rat brain sections with Anti-CLEC7A/Dectin-1 (extracellular) Antibody (#ALR-062), (1:600), followed by goat anti-rabbit-AlexaFluor-488 and Guinea Pig Anti-GFAP Antibody (#AFP-001-GP), (1:600), followed by goat anti-guinea pig-AlexaFluor-594. A. CLEC7A immunoreactivity (green) appears in astrocyte profiles. B. GFAP immunoreactivity (red) appears in astrocyte profiles. C. Merge of the two images demonstrates extensive co-localization. Cell nuclei are stained with DAPI (blue). P = pyramidal layer.
- Eng, L.F. et al. (2000) Neurochem. Res. 25, 1439.
- Herrmann H and Aebi, U. (1998) Curr. Opin. Struct. Biol. 8, 177.
- Yang, Z. et al. (2015) Trends Neurosci. 38, 364.
- Prust, M. et al. (2011) Neurology 77, 1287.
- Kamphuis, W. et al. (2014) Neurobiol. Aging 35, 492.
Glial fibrillary acidic protein (GFAP) is a key intermediate filament (IF) III protein responsible for maintaining the mechanical strength of glia cells by supporting their cytoskeleton structure. GFAP is expressed in astrocytes in the CNS, non-myelinating Schwann cells in the PNS, and enteric glial cells1.
GFAP has a structural organization that is typical to class III IF proteins: it has a head, rod, and tail domains. The N-terminal head domain is important for filament formation and the C-terminal domain is important for oligomerization2.
GFAP is encoded by a single gene mapped to human chromosome 17q21. To date, 10 isoforms/splice variants have been identified. GFAP is tightly regulated: both at mRNA transcription level and by phosphorylation and other post-translational modifications. A number of growth factors such as CNTF, FGF and TGF-β can induce GFAP gene transcription activation leading to increased GFAP protein levels3.
Single nucleotide polymorphism (SNP) in GFAP results in the formation of Rosenthal fibers that cause Alexander Disease, hence, GFAP is a potential drug target for the treatment of this disease. A number of GFAP mutations were found in the coding and in the promoter regions of Alexander disease patients4.
GFAP gene activation and protein induction appear to play a critical role in astroglia cell activation (astrogliosis) following CNS injuries and neurodegeneration. GFAP protein and its breakdown products are rapidly released into biofluids following traumatic brain and spinal cord injuries and stroke, making them strong candidate biomarkers for such neurological disorders5.
Guinea Pig Anti-GFAP Antibody (#AFP-001-GP) is a highly specific antibody directed against an epitope of the rat Glial fibrillary acidic protein. The antibody can be used in western blot and immunohistochemistry applications. It has been designed to recognize GFAP from rat and mouse samples. The antibody will not recognize GFAP from human samples.
The antigen used to immunize guinea pigs is the same as Anti-GFAP Antibody (#AFP-001) raised in rabbit. Our line of guinea pig antibodies enables more flexibility with our products such as multiplex staining studies, immunoprecipitation and more.
Powered by Bioz
