Recombinant Rat Sodium channel protein type 2 subunit alpha (Scn2a), partial

1. The Nav1.2 are highly expressed in axon terminals in central hilus compared to stratum radiatum and in dendrites and spines in stratum radiatum compared to central hilus . PMID: 28758202
2. Knockdown of Nav1.2 channels in pre-oligodendrocyte alters their morphology, reduces axon-oligodendrocyte interactions and impairs myelination. PMID: 28916793
3. Here, the authors show that hypoxia activates the Small Ubiquitin-like Modifier (SUMO) pathway in rat cerebellar granule neurons (CGN) and that SUMOylation of NaV1.2 channels increases sodium current. PMID: 28029095
4. The polarity of (Ca(2+))2-CaMC relative to the IQ motif of NaV1.2 was opposite to that seen in apo CaMC-Nav1.2IQp (2KXW), revealing that CaMC recognizes nested, anti-parallel sites in Nav1.2IQp. (CaMC is C-domain residues of CaM, calmodulin). PMID: 28343066
5. miR-9 suppressed the trafficking of Nav1.1/Nav1.2 from cytoplasm to cell membrane. miR-9 overexpression inhibited Navbeta2 expression by targeting its coding sequence domain. PMID: 26259688
6. Fibroblast growth factor 12 is a component of the voltage-gated sodium channel 1.2 (nav1.2) macromolecular complex in the rat brain. PMID: 25724910
7. In NaV1.2, Cys910 is disulfide-bonded to Cys918 and Cys912. PMID: 26039939
8. Reciprocal regulation of phosphorylation and MeArg of Nav1.2 may underlie changes in neuronal Nav channel function in response to seizures and also contribute to physiological modulation of neuronal excitability. PMID: 24737319
9. In the dorsal horn of the developing rat, Na(v) isoforms are developmentally regulated at the mRNA level in a subtype-specific manner, as Na(v)1.2 and Na(v)1.3 decreased significantly from P3 to adulthood, while Na(v)1.1 was upregulated during this period PMID: 23219908
10. NaV1.2 channels are expressed in vascular smooth muscle cells where they are involved in muscle contraction. PMID: 23364266
11. Lipid modifications are capable of altering the gating and pharmacological properties of rNav1.2a. PMID: 22123950
12. Data demonstrate that the two N-terminal alternatively spliced FGF14 variants, FGF14-1a and FGF14-1b, differentially regulate currents produced by Nav1.2 and Nav1.6 channels. PMID: 19465131
13. The wedge-shaped CssIV inserts between the IIS1-S2 and IIS3-S4 loops of rat brain sodium channels, placing key amino acid residues in position to interact with binding partners in these extracellular loops. PMID: 21795675
14. The ability to manipulate mu-conopeptide KIIIA's affinity and efficacy, as well as its capacity to interfere with subsequent tetrodotoxin binding, greatly expands its scope as a reagent for probing sodium channel structure and function. PMID: 20459109
15. the TTX-sensitive Na(v)1.2 isoform, together with the Na(+)/Ca(2+) exchanger, contributes to the contractile response of aortic myocytes at physiological range of membrane depolarizatio PMID: 19809503
16. Helix-stabilizing effects of the pentapeptide KIFMK and its related peptides on the sodium channel inactivation gate peptides PMID: 11892850
17. Interaction of the Nav1.2a subunit of the voltage-dependent sodium channel with nodal ankyrinG PMID: 12036953
18. expression of a soluble Nav1.2II-III linker protein led to the disorganization of endogenous sodium channels; results indicate this motif may play a fundamental role in controlling electrical excitability during development and plasticity [Nav1.2] PMID: 12829783
19. Oscillatory properties of the voltage-gated sodium channel may contribute to the sub-threshold membrane-potential oscillation and epileptic discharges in a single neuron. PMID: 16596442
20. NaV1.2 channels were predominately localized in unmyelinated fibers in the cortex, hippocampus, spinal cord and hypothalamus. PMID: 16815341
21. The pathogenic mechanism of benign familial neonatal-infantile seizures (BFNIS) mutations is neuronal hyperexcitability caused by increased Na(v)1.2 Na+ current, as shown in functional studies of rat pups. PMID: 17021166
22. AKAP15 directly interacts with Na(v)1.2a channels via the intracellular loop between domains I and II. PMID: 17360357
23. Synergistic and antagonistic interactions between tetrodotoxin and mu-conotoxin in blocking voltage-gated sodium channels. PMID: 19221510
24. Proteolysis results in loss of full-length alpha-subunits and the creation of fragments comprising all domains of the channel that retain interaction even after proteolysis. PMID: 19692609

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KEGG: rno:24766

STRING: 10116.ENSRNOP00000007069

UniGene: Rn.89192