83-5961-43　Alpha Fodrin 100ul　589942

特徴

• Fodrin, also referred to as non-erythroid (alphaII-; brain) spectrin, is a tetrameric (alpha gamma)2 actin-binding, fibrous protein, widely distributed in vertebrates, which forms part of the sub-membranous cytoskeleton within many cell types including neurons, and is particularly abundant with axons.
• The alpha-subunits of fodrins and spectrin are highly conserved phylogenetically, with the exception of human alpha-fodrin, which shares only 55-59% homology with erythroid-specific alpha-spectrins.
• The beta-subunits of spectrin (and gamma-subunits of fodrins) are species specific.
• The interleukin-1 converting enzyme (ICE) family of proteases has been implicated as important effectors of the apoptotic pathway, perhaps acting hierarchically in a protease cascade.
• Neuronal fodrin is known to be cleaved by calpain following ischaemic insult and it has been proposed that calpain and an unidentified protease play a role in the onset of neuronal death following transient forebrain ischaemia.
• Recently, an ICE-like protease has been implicated in the early cleavage of fodrin, producing a 150kD fragment, proximal to CPP32 in Fas-induced and C2-ceramide mediated apoptosis.
• A cleavage product of alpha-fodrin has been proposed as a candidate autoantigen in primary Sjögren’s syndrome and alpha-fodrin has been shown to be the source of a so-called ‘inhibitory protein factor’ family, members of which have been shown to inhibit both GABA and ATP-dependent glutamate uptake into purified synaptic vesicles.
• Applications:Suitable for use in Western Blot and immunohistochemistry.
• Other applications not tested.
• Recommended Dilutions:Optimal dilutions to be determined by the researcher.
• Storage and Stability:May be stored at 4℃ for short-term only.
• Aliquot to avoid repeated freezing and thawing.
• Store at -20℃.
• Aliquots are stable for 12 months after receipt.
• For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.