€724.00 €615.40
Glial fibrillary acidic protein (GFAP) is a protein encoded by the GFAP gene in humans and a member of the class III intermediate filament (IF) protein family.{53009} It is composed of an N-terminal head domain, a highly conserved ?-helical rod domain, and a C-terminal tail domain that mediate GFAP self-assembly, dimerization, and oligomerization, respectively.{53010,53011} GFAP is expressed in, and has commonly been used as a pan marker for, mature astrocytes.{53009} GFAP IFs form a dynamic network of cytosolic filament proteins that collectively provide structure and strength to the cytoskeleton of astrocytes, thus supporting their morphology and function.{53009} Isolated astrocytes from neonatal Gfap-/- mouse brain have reduced numbers of IFs and IF bundles, increased proliferation, and loss of contact-inhibited growth.{53015,53016} Gfap-/- mice develop more diffuse and infiltrative brain lesions compared to wild-type littermates in a mouse model of experimental autoimmune encephalomyelitis (EAE).{53019} Mutations in the rod and tail domains of GFAP have been associated with Rosenthal fiber formation, a hallmark of Alexander disease.{53013} Transgenic overexpression of Gfap in mice increases the expression of certain cytokines and antioxidative enzymes in the olfactory bulb and has been used as a mouse model of Alexander disease.{53017} GFAP can be citrullinated on the arginine residue at position 270 (R270) and at R416 by protein arginine deiminase 1 (PAD1; Item No. 10784) and PAD2 (Item No. 10785).{53021} Citrullinated GFAP has been found in rat cerebral cortex in a model of traumatic brain injury, as well as in postmortem hippocampus from patients with Alzheimer’s disease.{53021,53020}
Territorial Availability: Available through Bertin Technologies only in France
| Size | 100 µg |
|---|---|
| Shipping | dry ice |
| Molecular weight | 0 |
| Formulation | 10 mM Tris, pH 8.0 |
| Purity | ≥65% estimated by SDS-PAGE |
| Custom code | 3504.00 |
| UNSPSC code | 12352204 |
Cayman Chemical’s mission is to help make research possible by supplying scientists worldwide with the basic research tools necessary for advancing human and animal health. Our utmost commitment to healthcare researchers is to offer the highest quality products with an affordable pricing policy.
Our scientists are experts in the synthesis, purification, and characterization of biochemicals ranging from small drug-like heterocycles to complex biolipids, fatty acids, and many others. We are also highly skilled in all aspects of assay and antibody development, protein expression, crystallization, and structure determination.
Over the past thirty years, Cayman developed a deep knowledge base in lipid biochemistry, including research involving the arachidonic acid cascade, inositol phosphates, and cannabinoids. This knowledge enabled the production of reagents of exceptional quality for cancer, oxidative injury, epigenetics, neuroscience, inflammation, metabolism, and many additional lines of research.
Our organic and analytical chemists specialize in the rapid development of manufacturing processes and analytical methods to carry out clinical and commercial GMP-API production. Pre-clinical drug discovery efforts are currently underway in the areas of bone restoration and repair, muscular dystrophy, oncology, and inflammation. A separate group of Ph.D.-level scientists are dedicated to offering Hit-to-Lead Discovery and Profiling Services for epigenetic targets. Our knowledgeable chemists can be contracted to perform complete sample analysis for analytes measured by the majority of our assays. We also offer a wide range of analytical services using LC-MS/MS, HPLC, GC, and many other techniques.
Accreditations
ISO/IEC 17025:2005
ISO Guide 34:2009
Cayman is a leader in the field of emerging drugs of abuse, providing high-purity Schedule I-V Controlled Substances to federally-licensed laboratories and qualified academic research institutions for forensic analyses. We are certified by ACLASS Accreditation Services with dual accreditation to ISO/IEC 17025:2005 and ISO Guide 34:2009.
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