Glial fibrillary acidic protein Recombinant Protein | GFAP recombinant protein

Recombinant Human Glial fibrillary acidic protein

Cat. Num. AAA954882

• Gene Names: GFAP; ALXDRD
• Applications: Calibrator or standard
• Purity: 85% ± 5% by SDS-PAGE
• Synonyms: Glial fibrillary acidic protein; Recombinant Human Glial fibrillary acidic protein; GFAP recombinant protein

• Host: E.coli
• Purity/Purification: 85% ± 5% by SDS-PAGE
• Form/Format: Liquid, dissolved in 20mM Tris-HCl, 500mM NaCl, pH 8.0, 50%glycerol
• Sequence Positions: 292-432
• Sequence: LTCDLESLRGTNESLERQMREQEERHVREAASYQEALARLEEEGQSLKDEMARHLQEYQDLLNVKLALDIEIATYRKLLEGEENRITIPVQTFSNLQIRETSLDTKSVSEGHLKRNIVVKTVEMRDGEVIKESKQEHKDVM

• Applicable Applications for GFAP recombinant protein: Calibrator or standard
• Tag Information: his-tag
• Valid Period: -20 degree C for one year
• Product Note: Applications are user defined. Product is developed and quality control tested in house, data or additional information may be provided upon request. The researcher needs to establish and confirm the suitability of the product for their application.
• Preparation and Storage: Aliquot and store at < -20°C. Avoid repeated freeze / thaw cycles

Product Categories/Family for GFAP recombinant protein

Neuroscience; Raw Materials Assay Development

References

Molecular cloning and primary structure of human glial fibrillary acidic protein.Reeves S.A., Helman L.J., Allison A., Israel M.A.Proc. Natl. Acad. Sci. U.S.A. 86:5178-5182(1989) Characterization of human cDNA and genomic clones for glial fibrillary acidic protein.Brenner M., Lampel K., Nakatani Y., Mill J., Banner C., Mearow K., Dohadwala M., Lipsky R., Freese E.Brain Res. Mol. Brain Res. 7:277-286(1990) Human glial fibrillary acidic protein complementary DNA cloning, chromosome localization, and messenger RNA expression in human glioma cell lines of various phenotypes.Bongcam-Rudloff E., Nister M., Betsholtz C., Wang J.-L., Stenman G., Huebner K., Croce C.M., Westermark B.Cancer Res. 51:1553-1560(1991) Human glial fibrillary acidic protein (GFAP) molecular cloning of the complete cDNA sequence and chromosomal localization (chromosome 17) of the GFAP gene.Kumanishi T., Usui H., Ichikawa T., Nishiyama A., Katagiri T., Abe S., Yoshida Y., Washiyama K., Kuwano R., Sakimura K.Acta Neuropathol. 83:569-578(1992) Determination of the gene structure of human GFAP and absence of coding region mutations associated with frontotemporal dementia with parkinsonism linked to chromosome 17.Isaacs A., Baker M., Wavrant-De Vrieze F., Hutton M.Genomics 51:152-154(1998) Han C., Zhang B., Zhou Y., Peng X., Yuan J., Qiang B.Complete sequencing and characterization of 21,243 full-length human cDNAs.Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.Nat. Genet. 36:40-45(2004) Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. The full-ORF clone resource of the German cDNA consortium.Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.BMC Genomics 8:399-399(2007) DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage.Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.Nature 440:1045-1049(2006)

NCBI and Uniprot Product Information

• NCBI GI #: 196115290
• NCBI GeneID: 2670
• NCBI Accession #: NP_001124491.1
• NCBI GenBank Nucleotide #: NM_001131019.2
• UniProt Accession #: P14136; Q53H98; Q5D055; Q6ZQS3; Q7Z5J6; Q7Z5J7; Q96KS4; Q96P18; Q9UFD0; B2RD44; D3DX59; E9PAX3
• NCBI Official Full Name: glial fibrillary acidic protein isoform 2
• NCBI Official Synonym Full Names: glial fibrillary acidic protein
• NCBI Official Symbol: GFAP
• NCBI Official Synonym Symbols: ALXDRD
• NCBI Protein Information: glial fibrillary acidic protein
• UniProt Protein Name: Glial fibrillary acidic protein
• Protein Family: Glial fibrillary acidic protein
• UniProt Gene Name: GFAP
• UniProt Synonym Gene Names: GFAP
• UniProt Entry Name: GFAP_HUMAN

NCBI Description

This gene encodes one of the major intermediate filament proteins of mature astrocytes. It is used as a marker to distinguish astrocytes from other glial cells during development. Mutations in this gene cause Alexander disease, a rare disorder of astrocytes in the central nervous system. Alternative splicing results in multiple transcript variants encoding distinct isoforms. [provided by RefSeq, Oct 2008]

Uniprot Description

GFAP: a class-III intermediate filament protein. A cell-specific marker that, during the development of the central nervous system, distinguishes astrocytes from other glial cells. Mutations in this gene cause Alexander disease, a rare disorder of astrocytes in the central nervous system. An additional transcript variant isoform has been described, but its full length sequence has not been determined.

Protein type: Cytoskeletal

Chromosomal Location of Human Ortholog: 17q21

Cellular Component: cytoplasm; cytosol; intermediate filament; intermediate filament cytoskeleton; lysosome; membrane; myelin sheath

Molecular Function: integrin binding; kinase binding; protein binding; structural constituent of cytoskeleton

Biological Process: astrocyte development; Bergmann glial cell differentiation; extracellular matrix organization and biogenesis; intermediate filament organization; neurite regeneration; regulation of neurotransmitter uptake; regulation of protein complex assembly; response to wounding

Disease: Alexander Disease