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anti-Mouse (Murine) SPTBN4 Antikörper:
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Human Polyclonal SPTBN4 Primary Antibody für IHC (p) - ABIN5554206
Stein, Thiart: TrackNTrace: A simple and extendable open-source framework for developing single-molecule localization and tracking algorithms. in Scientific reports 2018
bi-allelic pathogenic SPTBN4 variants (three homozygous and two compound heterozygous) that cause a severe neurological syndrome that includes congenital hypotonia, intellectual disability, and motor axonal and auditory neuropathy, are reported.
In embryonic mouse axons neither beta4-spectrin nor Neurofascin control the distal-to-proximal restriction of AnkG.
provide new insight into membrane targeting of TREK-1 in the heart and establish a broader role for beta(IV)-spectrin in organizing functional membrane domains critical for normal heart function
Data indicate that betaIV-Spectrin-targeted CaMKII directly phosphorylates the inwardly-rectifying potassium channel, Kir6.2.
These findings demonstrate that spectrin cytoskeleton finely regulates ion channel distribution and implicates KCNQ2/3 subunits in axonal excitability and in myokymia etiology.
identified a regulatory mechanism for Na(+) channels, via direct phosphorylation by beta(IV)-spectrin-targeted calcium/calmodulin-dependent kinase II
Beta]IV-spectrin regulates sodium channel clustering through ankyrin-G at axon initial segments and nodes of Ranvier
Distinct protein domains of BetaIV spectrin regulate membrane stability and the molecular organization of nodes of Ranvier.
BetaIVSigma1 spectrin, the only betaIV spectrin with an actin-binding domain, is an essential component of this coat. Specifically, betaIVSigma1 coexists with betaIVSigma6 at both axon initial segments and nodes of Ranvier.
truncated betaIV-spectrin isoform Sigma6 plays a specific role in clustering voltage-gated sodium channels, whereas it is dispensable for membrane stabilization at axon initial segments and nodes of Ranvier.
We identify a distinct protein domain in betaIV spectrin required for its localization to the AIS, and show that this domain mediates betaIV spectrin's interaction with ankG.
We confirmed their localization on the axonal initial segments of Beta-IV Spectrin on the large short-axon cells and periglomerular cellsof the main olfactory bulb.
we characterize dendritic segments which displayed some betaIV-spectrin postive clusters
our findings demonstrate that betaIV-spectrin is required for normal granule cell firing & for physiological levels of network excitability in the mouse dentate gyrus in vivo
Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. This gene is one member of a family of beta-spectrin genes. The encoded protein localizes to the nuclear matrix, PML nuclear bodies, and cytoplasmic vesicles. A highly similar gene in the mouse is required for localization of specific membrane proteins in polarized regions of neurons. Multiple transcript variants encoding different isoforms have been found for this gene.
spectrin beta 4
, beta-spectrin 4
, neuroaxonal dystrophy
, lumbosacral neuroaxonal dystrophy
, spectrin, beta, non-erythrocytic 4
, beta-IV spectrin
, spectrin beta chain, brain 3
, spectrin beta chain, non-erythrocytic 4
, spectrin, non-erythroid beta chain 3