Cayman Gfap (Human, Recombinant); Purity- Greater Than Or Equal T

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. It is composed of an N-terminal head domain, a highly conserved α-helical rod domain, and a C-terminal tail domain that mediate GFAP self-assembly, dimerization, and oligomerization, respectively.^, GFAP is expressed in, and has commonly been used as a pan marker for, mature astrocytes. 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. Isolated astrocytes from neonatal Gfap^-/- mouse brain have reduced numbers of IFs and IF bundles, increased proliferation, and loss of contact-inhibited growth.^, Gfap^-/- mice develop more diffuse and infiltrative brain lesions compared to wild-type littermates in a mouse model of experimental autoimmune encephalomyelitis (EAE). Mutations in the rod and tail domains of GFAP have been associated with Rosenthal fiber formation, a hallmark of Alexander disease. 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. GFAP can be citrullinated on the arginine residue at position 270 (R270) and at R416 by protein arginine deiminase 1 (PAD1; Item No. ) and PAD2 (Item No. ). 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 Alzheimers disease.^,

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