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|+1 404 474 4654|
|+1 888 205 9894 (TF)|
Glial Fibrillary Acidic Protein (GFAP) antibody
|Synonyms||GFAP, DKFZp459C0729, MGC139638, FLJ45472, AI836096, cb345, gfapl, MGC110485, wu:fb34h11, wu:fk42c12, zgc:110485, etID36982.3, xx:af506734|
Alternatives Immunohistochemistry (Paraffin-embedded Sections) (IHC (p)), ELISA
|10 references available|
|Quantity||0.25 mg (Variants)|
|Price||Product not available in this region.|
|Gene ID||2670, 14580, 24387|
|Immunogen||Native GFAP extracted from rat spinal cord .|
|Cross-Reactivity||Human, Mouse (Murine), Rat (Rattus)|
|Description||Glial fibrillary acidic protein (GFAP) is a member of the class III intermediate filamentprotein family. It is heavily, and specifically, expressed in astrocytes and certain otherastroglia in the central nervous system, in satellite cells in peripheral ganglia, and in nonmyelinating Schwann cells in peripheral nerves. In addition, neural stem cells frequentlystrongly express GFAP. Antibodies to GFAP are therefore very useful as markers ofastrocytic cells. In addition many types of brain tumor, presumably derived fromastrocytic cells, heavily express GFAP. GFAP is also found in the lens epithelium,Kupffer cells of the liver, in some cells in salivary tumors and has been reported inerythrocytes. Alternate Names: anti-Astrocyte antibody, anti-Glial Fibrillary Acidic Protein antibody, anti-FLJ45472antibody. Related Diseases: Developmental CNS|
|Specificity||Species Reactivity: Reacts with Human, Mouse, Rat and Cow.|
|Application Notes||Suggested working dilutions: Immunohistochemistry-Paraffin 1:500-1:1000|
|Buffer||Reconstitute in 250 ul of sterile water. Centrifuge to remove any insoluble material. Preservative: No Preservative.|
|Storage||Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.|
|Research Area||Stem Cells, Cytoskeleton, Glia marker, Cell/Tissue Markers, Neurology|
|Restrictions||For Research Use only|
Brenner, Lampel, Nakatani et al.: "Characterization of human cDNA and genomic clones for glial fibrillary acidic protein." in: Brain research. Molecular brain research, Vol. 7, Issue 4, pp. 277-86, 1990 (PubMed).
Reeves, Helman, Allison et al.: "Molecular cloning and primary structure of human glial fibrillary acidic protein." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 86, Issue 13, pp. 5178-82, 1989 (PubMed).
Brenner, Johnson, Boespflug-Tanguy et al.: "Mutations in GFAP, encoding glial fibrillary acidic protein, are associated with Alexander disease." in: Nature genetics, Vol. 27, Issue 1, pp. 117-20, 2001 (PubMed).
Aoki, Haginoya, Munakata et al.: "A novel mutation in glial fibrillary acidic protein gene in a patient with Alexander disease." in: Neuroscience letters, Vol. 312, Issue 2, pp. 71-4, 2001 (PubMed).
Sawaishi, Yano, Takaku et al.: "Juvenile Alexander disease with a novel mutation in glial fibrillary acidic protein gene." in: Neurology, Vol. 58, Issue 10, pp. 1541-3, 2002 (PubMed).
Nielsen, Holm, Johansen et al.: "A new splice variant of glial fibrillary acidic protein, GFAP epsilon, interacts with the presenilin proteins." in: The Journal of biological chemistry, Vol. 277, Issue 33, pp. 29983-91, 2002 (PubMed).
Singh, Nielsen, Johansen et al.: "Genetic polymorphism and sequence evolution of an alternatively spliced exon of the glial fibrillary acidic protein gene, GFAP." in: Genomics, Vol. 82, Issue 2, pp. 185-93, 2003 (PubMed).
Brockmann, Meins, Taubert et al.: "A novel GFAP mutation and disseminated white matter lesions: adult Alexander disease?" in: European neurology, Vol. 50, Issue 2, pp. 100-5, 2003 (PubMed).
Stumpf, Masson, Duquette et al.: "Adult Alexander disease with autosomal dominant transmission: a distinct entity caused by mutation in the glial fibrillary acid protein gene." in: Archives of neurology, Vol. 60, Issue 9, pp. 1307-12, 2003 (PubMed).
Ota, Suzuki, Nishikawa et al.: "Complete sequencing and characterization of 21,243 full-length human cDNAs." in: Nature genetics, Vol. 36, Issue 1, pp. 40-5, 2003 (PubMed).