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Product Specification
Alternative Name:αII-spectrin
Clone:AA6
Host:Mouse
Isotype:IgG1
Immunogen:Chicken blood cell membranes following hypotonic lysis and mechanical enucleation.
UniProt ID:P07751
Application:Immunohistochemistry
Western Blot
Specificity:Recognizes mammalian and chicken α-fodrin
Purity Detail:Partially purified.
Formulation:Liquid. In PBS containing 1.0% BSA and 0.09% sodium azide.
Use/Stability:Store unopened vial at -20°C until required for use. AVOID REPEATED FREEZE-THAW CYCLES. Aliquot undiluted antibody into smaller volumes (not less than 10μL) prior to freezing if appropriate. The use of high quality ‘antiserum-grade’ plastic or glass vials is recommended. Store diluted antibody at 2-4°C (do not freeze) and use within 1 month. Dilute to working strength with 50mM Tris-HCl buffer (pH 7.6) containing 1.5% sodium chloride and 1% normal goat serum (if a goat anti-mouse IgG linker antibody is to be used).
Long Term Storage:-20°C
Miscellaneous/General:Fodrin, also referred to as non-erythroid (αII-; brain) spectrin, is a tetrameric (αγ)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 α-subunits of fodrins and spectrin are highly conserved phylogenetically, with the exception of human α-fodrin, which shares only 55-59% homology with erythroid-specific α-spectrins. The β-subunits of spectrin (and γ-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 150kDa fragment, proximal to CPP32 in Fas-induced and C2-ceramide mediated apoptosis. A cleavage product of α-fodrin has been proposed as a candidate autoantigen in primary Sjögren’s syndrome and α-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. |