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SAB2500462

Sigma-Aldrich

Anti-GFAP antibody produced in goat

affinity isolated antibody, buffered aqueous solution

Synonym(s):

Anti-FLJ45472, Anti-Glial fibrillary acidic protein

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About This Item

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

biological source

goat

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

species reactivity

rat

technique(s)

indirect ELISA: suitable
western blot: suitable

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... GFAP(2670)

Related Categories

General description

Goat polyclonal anti-GFAP antibody reacts with rat, canine, human, and mouse glial fibrillary acidic proteins.
Intermediate filaments (IFs) with characteristic 10 nm diameter are a distinct class of molecularly heterogenous cytoskeletal filaments defined by ultrastructural, immunological, and biochemical criteria. Intermediate filaments differ significantly from the other cytoskeletal elements of the cell, namely microtubules and microfilaments, and are components of most eukaryotic cells. Glial Fibrillary Acidic Protein (GFAP) (molecular weight of 50 kDa) is found in astrocytes and ependymal cells of the central nervous system. It is found in various other cell types including stellate cells, chondrocytes, osteocytes, keratinocytes, Leydig cells and fibroblasts. GFAP is involved in mitosis, and cell:cell interactions and communications.

Immunogen

Peptide with sequence C-DGEVIKESKQEHKD from the C Terminus of the protein sequence according to NP_002046.1.

Application

Goat polyclonal anti-GFAP antibody is used to tag glial fibrillary acidic protein for detection and quantitation by Western blotting and immunohistochemical (IHC) techniques. It is used as a probe to determine the roles of glial fibrillary acidic protein in cell:cell communications, mitosis and cell structure. Anti-GFAP has proven a valuable tool for use in immunocytochemical localization of GFAP in normal central nervous system tissue, certain tumors and metastases of the glial antigen, as well as for immunofluorescent labeling of cultured mammalian cells.

Biochem/physiol Actions

Glial fibrillary acidic protein (GFAP) is associated with tumor progression of brain neoplasms and increase expression of this gene is observed in brain tumor. Gfap maintains cell stability and shape. Damage to the central nervous system (CNS) increases the levels of circulation Gfap. Gfap mediates cell migration, development, mitosis and signaling in astrocytes and a some glial cells. Mutation in GFAP gene is involved in neural dysfunction disease and Alexander disease characterized by the accumulation of Rosenthal fibers.

Features and Benefits

Evaluate our antibodies with complete peace of mind. If the antibody does not perform in your application, we will issue a full credit or replacement antibody. Learn more.

Physical form

Supplied at 0.5 mg/mL in Tris saline with 0.02% sodium azide and 0.5% bovine serum albumin.

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 Code

10 - Combustible liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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A novel functional polymorphism of GFAP decrease glioblastoma susceptibility through inhibiting the binding of miR-139
Wang J, et al.
Aging, 10(5), 988-988 (2018)
Post-mortem serum concentrations of GFAP correlate with agony time but do not indicate a primary cerebral cause of death
Breitling B, et al.
Testing, 13(10), e0205323-e0205323 (2018)
Crystal structure of the human glial fibrillary acidic protein 1B domain
Kim B, et al.
Biochemical and biophysical research communications, 503(4), 2899-2905 (2018)
Emerson Krock et al.
Osteoarthritis and cartilage, 26(9), 1236-1246 (2018-06-18)
Intervertebral disc degeneration is a leading cause of chronic low back pain (LBP) but current treatment is limited. Toll-like receptors (TLRs) on disc cells are activated by endogenous extracellular matrix (ECM) fragments and modulate degeneration in vitro. This study investigated whether
Corinne Orlemann et al.
Advanced healthcare materials, 13(15), e2304169-e2304169 (2024-02-07)
Brain interfaces that can stimulate neurons, cause minimal damage, and work for a long time will be central for future neuroprosthetics. Here, the long-term performance of highly flexible, thin polyimide shanks with several small (<15 µm) electrodes during electrical microstimulation of

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