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α Fodrin monoclonal antibody (AA6)

 
BML-FG6090-0100 100 µl 283.00 USD
 
BML-FG6090-0500 500 µl 989.00 USD
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Product Details

Alternative Name:αII-spectrin
 
Clone:AA6
 
Host:Mouse
 
Isotype:IgG1
 
Immunogen:Chicken blood cell membranes following hypotonic lysis and mechanical enucleation.
 
UniProt ID:P07751
 
Species reactivity:Chicken, Mammalian
 
Applications:IHC, WB
 
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).
 
Shipping:Blue Ice
 
Long Term Storage:-20°C
 
Scientific Background: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.
 
Regulatory Status:RUO - Research Use Only
 
α Fodrin monoclonal antibody (AA6) Western blot
Rat primary septo-hippocampal co-cultures (astrocytes and neurons cultured from day E18 rat embyros) were challenged with the pro-apoptotic compound staurosporine or with vehicle (DMSO) for times indicated above. Protein (40 μg) was separated by SDS-PAGE, transferred to PVDF membrane and probed with FG6090. The caspase-3 cleaved 120-kDa fragment of alpha-II-spectrin was detected at a dilution of 1:4000. Western blot provided by courtesy of Dr Brian Pike, University of Florida.
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α Fodrin monoclonal antibody (AA6) Western blot

Product Literature References

Influence of traumatic brain injury on ipsilateral and contralateral cortical perfusion in mice: S. Meyer, et al.; Neurosci. Lett. 795, 137047 (2023), Abstract;
Neurobiochemical, Peptidomic, and Bioinformatic Approaches to Characterize Tauopathy Peptidome Biomarker Candidates in Experimental Mouse Model of Traumatic Brain Injury: H. Yadikar, et al.; Mol. Neurobiol. 60, 2295 (2023), Abstract;
Impairment of μ-calpain activation by rhTNFR:Fc reduces severe burn-induced membrane disruption in the heart: M.S. Cao, et al.; Cell Death Discov. 8, 10 (2022), Abstract;
The effect of clopidogrel and aspirin on the severity of traumatic brain injury in a rat model: F. Kobeissy, et al.; Neurochem. Int. 154, 105301 (2022), Abstract;
Acute liver injury following acetaminophen administration does not activate atrophic pathways in the mouse diaphragm: C.S. Bruells , et al.; Sci. Rep. 11, 6302 (2021), Abstract;
Inhibition of Calpain Alleviates Apoptosis in Coxsackievirus B3-induced Acute Virus Myocarditis Through Suppressing Endoplasmic Reticulum Stress: H. Shi, et al.; Int. Heart J. 62, 900 (2021), Abstract;
Activation of Cytosolic Calpain, Not Caspase, Is Underlying Mechanism for Hypoxic RGC Damage in Human Retinal Explants: M. Kobayashi-Otsugu, et al.; Invest. Ophthalmol. Vis. Sci. 61, 13 (2020), Abstract; Full Text
Calpain system is altered in survival motor neuron-reduced cells from in vitro and in vivo spinal muscular atrophy models: S. de la Fuente, et al.; Cell Death Dis. 11, 487 (2020), Abstract; Full Text
Buffering of cytosolic calcium plays a neuroprotective role by preserving the autophagy-lysosome pathway during MPP+-induced neuronal death: S. Jung, et al.; Cell Death Dis. 5, 130 (2019), Abstract; Full Text
Depletion of regulatory T cells increases T cell brain infiltration, reactive astrogliosis, and interferon-γ gene expression in acute experimental traumatic brain injury: T.J. Kramer, et al.; J. Neuroinflammation 16, 163 (2019), Abstract; Full Text
BrainPhys® increases neurofilament levels in CNS cultures, and facilitates investigation of axonal damage after a mechanical stretch-injury in vitro: T.C. Jackson, et al.; Exp Neurol. 300, 232 (2018), Abstract;
Calpain inhibition ameliorates scald burn-induced acute lung injury in rats: P. Du, et al.; Burns Trauma 6, 28 (2018), Abstract; Full Text
Cerebrospinal Fluid Biomarkers Are Associated With Glial Fibrillary Acidic Protein and αII-spectrin Breakdown Products in Brain Tissues Following Penetrating Ballistic-Like Brain Injury in Rats: K.E. DeDominicis, et al.; Front. Neurol. 9, 490 (2018), Abstract; Full Text
Exposure to mild blast forces induces neuropathological effects, neurophysiological deficits and biochemical changes: A. Hernandez, et al.; Mol. Brain 11, 64 (2018), Abstract; Full Text
Neuroprotective Effects of Psalmotoxin-1, an Acid-Sensing Ion Channel (ASIC) Inhibitor, in Ischemia Reperfusion in Mouse Eyes: A. Dibas, et al.; Curr. Eye Res. 43, 921 (2018), Abstract;
Chemosensitivity of U251 Cells to the Co-treatment of D-Penicillamine and Copper: Possible Implications on Wilson Disease Patients: M. Katerji, et al.; Front. Mol. Neurosci. 10, 10 (2017), Abstract; Full Text
Contribution of Calpain and Caspases to Cell Death in Cultured Monkey RPE Cells: E. Nakajima, et al.; Invest. Ophthalmol. Vis. Sci. 58, 5412 (2017), Abstract; Full Text
Mild fluid percussion injury induces diffuse axonal damage and reactive synaptic plasticity in the mouse olfactory bulb: M.A. Powell, et al.; Neuroscience 371, 106 (2017), Application(s): Western Blot, Abstract;
Sequestosome 1 Deficiency Delays, but Does Not Prevent Brain Damage Formation Following Acute Brain Injury in Adult Mice: A. Sebastiani, et al.; Front. Neurosci. 11, 678 (2017), Abstract; Full Text
Ammonium accumulation is a primary effect of 2-methylcitrate exposure in an in vitro model for brain damage in methylmalonic aciduria: H.P. Cudré-Cung, et al.; Mol. Genet. Metab. 119, 57 (2016), Application(s): Western blot analysis, Abstract;
Influence of weaning methods on the diaphragm after mechanical ventilation in a rat model: C.S. Bruells, et al.; BMC Pulm. Med. 16, 127 (2016), Application(s): Proteolysis, Calpain and caspase-3 activity measurement, Abstract; Full Text
miR-711 upregulation induces neuronal cell death after traumatic brain injury: B. Sabirzhanov, et al.; Cell Death Differ. 23, 654 (2016), Application(s): Western Blot, Abstract;
Tissue Plasminogen Activator Neurotoxicity is Neutralized by Recombinant ADAMTS 13: M. Fan, et al.; Sci. Rep. 6, 25971 (2016), Application(s): Western blot, Abstract; Full Text
Calpain-mediated cleavage of DARPP-32 in Alzheimer's disease: K. Cho, et al.; Aging Cell 14, 878 (2015), Application(s): Western Blot, Abstract; Full Text
The Blockade of Transmembrane Cl Flux Mitigates I/R-Induced Heart Injury via the Inhibition of Calpain Activity: J. Y. Zhang, et al.; Cell. Physiol. Biochem. 35, 2121 (2015), Application(s): Western Blot, Abstract; Full Text
The nuclear splicing factor RNA binding motif 5 promotes caspase activation in human neuronal cells, and increases after traumatic brain injury in mice: T.C. Jackson, et al.; J. Cereb. Blood Flow Metab. 35, 655 (2015), Application(s): Western Blotting, Abstract;

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