Analytical Data
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Gene name
Glial fibrillary acidic
- Application
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Alternative Names
gfapGlial fibrillary acidic protein; GFAP
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Species
Zebrafish
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Source
E. coli
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Tag
N- His-SUMO & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q58EE9
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Expression Region
1-444aa
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Molecular Weight
71.2 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
Glial fibrillary acidic protein (GFAP) is a key intermediate filament protein primarily expressed in astrocytes, a type of glial cell in the central nervous system. GFAP plays a crucial role in maintaining the structural integrity of glial cells and is involved in various physiological processes, including neuroinflammation, neuroprotection, and the response to injury. Research into GFAP has gained momentum due to its significance as a biomarker for various neurological disorders, such as multiple sclerosis, Alzheimer's disease, and traumatic brain injury. Elevated levels of GFAP in the cerebrospinal fluid (CSF) or serum have been associated with glial activation and can indicate the severity of neurodegeneration or injury. Moreover, GFAP is involved in the formation of astrocytic scars, which can influence neuronal regeneration and recovery following CNS damage. Recombinant forms of GFAP have been developed to better understand its structure-function relationships and to explore its potential therapeutic applications. Studies using recombinant GFAP have provided insights into its role in cell signaling, its impact on astrocyte behavior, and its interactions with other proteins in the CNS. As research progresses, GFAP continues to be a focal point in understanding glial biology and its implications for treating and diagnosing neurological diseases, making it a promising target for future therapeutic interventions.
