Our Anti-Beta4-spectrin mouse monoclonal primary antibody from NeuroMab is produced in-house from hybridoma clone N393/76. It detects human, mouse, and rat Beta4-spectrin, and is purified by Protein A chromatography. It is great for use in IHC, ICC, WB.
Spectrin beta chain, non-erythrocytic 4, or ß4 spectrin, is a member of the spectrin family of cytoskeletal proteins. It is found in the cytoskeleton and cell cortex of cells in the brain and pancreatic islets. It is also expressed in skeletal muscule. ß4 spectrin functions as a scaffold protein that links the actin cytoskeleton to the plasma membrane. It is involved in cell shape and organization. Mutations in the ß4 spectrin gene are associated with congenital myopathy, and neurodevelopmental disorder with hypotonia, neuropathy and deafness (NEDHND).
Purified by Protein A chromatography
1 mg/mL
Monoclonal
N393/76
IgG2b
ICC, IHC, WB
Mouse
SPTBN4 KIAA1642 SPTBN3
>200 kDa
Fusion protein amino acids 1621-1832 (C-terminal repeats 14 to 15) of human Beta4-spectrin (accession number Q9H254) produced recombinantly in E. Coli
Human, Mouse, Rat
AB_2315818
Aliquot and store at ≤ -20°C for long term storage. For short term storage, store at 2-8°C. For maximum recovery of product, centrifuge the vial prior to removing the cap.
Liquid
Produced by in vitro bioreactor culture of hybridoma line followed by Protein A affinity chromatography. Purified mAbs are >90% specific antibody.
10 mM Tris, 50 mM Sodium Chloride, 0.065% Sodium Azide pH 7.125
WB: 1:1000
IHC: 1:250
ICC: 1:500
Unconjugated
Does not cross-react with other Beta-spectrins
Each new lot of antibody is quality control tested by IHC on either rat or mouse brain and confirmed to give the expected staining pattern.
These antibodies are to be used as research laboratory reagents and are not for use as diagnostic or therapeutic reagents in humans.
Konietzny, A, et al. 2024. Efficient axonal transport of endolysosomes relies on the balanced ratio of microtubule tyrosination and detyrosination. Journal of Cell Science, .
Smalley, J.L., et al. 2023. Spectrin-beta 2 Facilitates the Selective Accumulation of GABAA Receptors at Somatodendritic Synapses. Communications Biology, 11.
Wang, Y., et al. 2022. Glucose Increases the Length and Spacing of the Lattice Structure of the Axon Initial Segment. Microscopy Research and Technique, 2679-2691.
Wang, Y., et al. 2021. The largest isoform of Ankyrin-G is required for lattice structure of the axon initial segment. Biochemical and biophysical research communications, 28-34.
Jarjour, A.A., et al. 2020. The formation of paranodal spirals at the ends of CNS myelin sheaths requires the planar polarity protein Vangl2. Glia, 1840-1858.
Sozmen, E.G., et al. 2019. White matter stroke induces a unique oligo-astrocyte niche that inhibits recovery. Journal of Neuroscience, 39(47), pp.9343-9359.. Journal of Neuroscience, 9343-9359.
Werginz, P., et al. 2020. The relationship between morphological properties and thresholds to extracellular electric stimulation in α RGCs. Journal of Neural Engineering, 45015.
Smalley, J.L., et al. 2023. Spectrin-beta 2 Facilitates the Selective Accumulation of GABAA Receptors at Somatodendritic Synapses. Communications Biology, 11.
Lee, M., et al. 2020. Ecm29-mediated proteasomal distribution modulates excitatory GABA responses in the developing brain. Journal of Cell Biology, e201903033.
Kneynsberg, A., et al. 2017. Aging Does Not Affect Axon Initial Segment Structure and Somatic Localization of Tau Protein in Hippocampal Neurons of Fischer 344 Rats. eNeuro, .
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