KCNIP2 Antibody

1. although there is a baseline presence of KChIP2 in the nucleus both in vivo and in vitro, KChIP2 does not directly regulate transcriptional activity. Moreover, the nuclear transport of KChIP2 is not dependent on Ca(2+). Thus, KChIP2 does not function as a conventional transcription factor in the heart. PMID:27349185
2. Our results do not support the notion that accessory KChIP2 binding is a prerequisite for dendritic trafficking and functional surface expression of Kv4.2 channels, however, accessory KChIP2 binding may play a potential role in Kv4.2 modulation during intrinsic plasticity processes. PMID:29385176
3. Results identify the KChIP2/miR-34 axis as a central regulator in developing cardiac electrical dysfunction. PMID:28263709
4. A novel KCNQ1-G229D mutation identified in a juvenile-onset AF patient altered the IKs activity and kinetics, thereby increasing the arrhythmogenicity to AF. PMID:24096004
5. mutations cause a gainoffunction of KV4.3/KChIP2encoded channels by increasing membrane protein expression and slowing channel inactivation. PMID:26016905
6. The "structurally minimal" isoform KChIP2d modulates recovery of K(v)4.3 N-terminal deletion mutant Delta2-39. PMID:21422811
7. KChIP2 differentially regulates total and cell surface Kv4.2 protein expression and Kv4 current densities. PMID:20709747
8. The I(to) activator NS5806 modified Kv4.3/KChIP2 gating in several ways that inhibit current. PMID:20649599
9. The cytoplasmic accessory subunit KChIP2 also assembles with Kv4.2 to increase peak current, shift V1/2 ~5mV, slow time to peak ~10%, slow inactivation ~100%, and speed recovery from inactivation ~250% without overshoot. PMID:20498229
10. N-linked glycosylation of DPP10 plays an important role in modulating Kv4.3 channel/KCHIP2 complex activities. PMID:20354865
11. Down-regulated atrial KChIP2 and Kv4.3 mRNA expressions in rheumatic heart disease patients with chronic atrial fibrillation might be one of the molecular bases responsible for the down-regulation of the I(to) current density of AF. PMID:19927631
12. Regulation of Kv4.3 current by KChIP2 splice variants PMID:12135940
13. Kv4.2 and K+ channel-interacting protein 2 make up a complex of Ito channels PMID:14623880
14. Data show that KChIP1, KChIP2.1, and KChIP2.2 could form homo- as well as hetero-oligomers, and that this oligomerization did not perturb their interaction with Kv4.2 potassium channel. PMID:15358149
15. Both Kv4.3 and KChIP2 may contribute to epicardial-endocardial gradients in the transient outward current in normal and failing hearts. PMID:15498806
16. Co-expression of SGK1, but not of SGK2 or SGK3, increased Kv 4.3/KChIP2b channel currents. [KChIP2b; AH010566] PMID:15578212
17. KChIP-2 is a Ca2+-dependent repressor of the immune response. PMID:16177826
18. the C-terminal domain of Kv4.2 plays a critical role in voltage-dependent activation and functional expression that is mediated by direct interaction between the Kv4.2 C terminus and KChIP2 PMID:16820361
19. The conformational change with metal-bound KChIP4.1 is crucial for its interaction with Kv channel but not for KChIP2.2, and that the Mg2+- and Ca2+-binding properties of KChIP2.2 and KChIP4.1 have different effects on their molecular structure. PMID:16951992

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HGNC: 15522

UNIGENE: Hs.97044

KEGG: hsa:30819

OMIM: 604661