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Merck

G6171

Sigma-Aldrich

Anti-Glial Fibrillary Acidic Protein antibody, Mouse monoclonal

clone G-A-5, purified from hybridoma cell culture

Sinónimos:

Anti-GFAP

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

Quality Level

conjugate

unconjugated

antibody form

purified from hybridoma cell culture
purified immunoglobulin

antibody product type

primary antibodies

clone

G-A-5, monoclonal

form

buffered aqueous solution

mol wt

antigen ~50 kDa

species reactivity

rat, human, pig

concentration

~1.0 mg/mL

technique(s)

immunocytochemistry: suitable
immunohistochemistry: suitable
indirect immunofluorescence: 2.5-5 μg/mL using alcohol-fixed sections of rat brain/cerebellum.
western blot: suitable

isotype

IgG1

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... GFAP(2670)
mouse ... Gfap(14580)
pig ... GFAP(396562)
rat ... Gfap(24387)

General description

Glial fibrillary acidic protein (GFAP) is intermediary filament present in astrocyte cells and is expressed in 10 different isoforms. It comprises of N-terminal head, central rod and C-terminal tail domains. GFAP is mapped to human chromosome 17q21.31.

Immunogen

purified GFAP from pig spinal cord.

Application

Anti-Glial Fibrillary Acidic Protein antibody, Mouse monoclonal has been used in immunocytochemistry and in immunofluorescence.
Monoclonal Anti-Glial Fibrillary Acidic Protein antibody is suitable for use in western blot and indirect immunofluorescence 2.5-5 μg/mL using alcohol-fixed sections of rat brain/cerebellum). The antibody can also be used for immunoblot (approx. 50 kDa), immunohistochemistry (in paraformaldehyde-fixed, frozen rabbit brain sections) and immunocytochemistry.

Biochem/physiol Actions

Glial fibrillary acidic protein or GFAP assembly has been implicated in mitotic remodeling of glial structures. Genetic mutations in GFAP have been associated with Alexander disease.
Microdeletion in glial fibrillary acidic protein (GFAP) gene locus is implicated in intellectual disability and facial dysmorphism in children. High levels of GFAP is associated with acute intracerebral haemorrhage.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class

10 - Combustible liquids

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Visite la Librería de documentos

Govindaiah Vinukonda et al.
Journal of neuroscience research, 90(11), 2173-2182 (2012-07-19)
Mechanisms of brain injury in intraventricular hemorrhage (IVH) of premature infants are elusive, and no therapeutic strategy exists to prevent brain damage in these infants. Therefore, we developed an in vitro organotypic forebrain slice culture model to advance mechanistic studies
M Inagaki et al.
Brain pathology (Zurich, Switzerland), 4(3), 239-243 (1994-07-01)
Glial fibrillary acidic protein (GFAP) is an intermediate filament (IF) protein of astroglia, and belongs to the type III subclass of IF proteins. IF proteins are composed of an amino-terminal HEAD domain, a central ROD domain and a carboxyterminal TAIL
Identification of genes associated with the astrocyte-specific gene Gfap during astrocyte differentiation
Ito K, et al.
Scientific Reports, 6, 23903-23903 (2016)
Plasma glial fibrillary acidic protein in the differential diagnosis of intracerebral hemorrhage
Katsanos AH, et al.
Stroke, 48(9), 2586 -22588 (2017)
Lipopolysaccharide differentially modulates expression of cytokines and cyclooxygenases in dorsal root ganglion cells via Toll-like receptor-4 dependent pathways
Tse KH, et al.
Neuroscience, 267, 241 -2251 (2014)

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