AKAP7 monoclonal antibody (M13), clone 1F9
- Known as:
- AKAP7 mab (anti-) (M13), clonality 1F9
- Catalog number:
- H00009465-M13
- Product Quantity:
- 100 ug
- Category:
- -
- Supplier:
- Abno
- Gene target:
- AKAP7 monoclonal antibody (M13) clone 1F9
Related genes to: AKAP7 monoclonal antibody (M13), clone 1F9
- Gene:
- ADH5P4 NIH gene
- Name:
- ADH5 pseudogene 4
- Previous symbol:
- ADH5B
- Synonyms:
- bA707M13.2
- Chromosome:
- 6q12
- Locus Type:
- pseudogene
- Date approved:
- 2003-11-26
- Date modifiied:
- 2019-01-18
- Gene:
- AKAP5 NIH gene
- Name:
- A-kinase anchoring protein 5
- Previous symbol:
- -
- Synonyms:
- AKAP75, AKAP79
- Chromosome:
- 14q23.3
- Locus Type:
- gene with protein product
- Date approved:
- 1999-09-16
- Date modifiied:
- 2015-11-17
- Gene:
- AKAP7 NIH gene
- Name:
- A-kinase anchoring protein 7
- Previous symbol:
- -
- Synonyms:
- AKAP18, AKAP15
- Chromosome:
- 6q23.2
- Locus Type:
- gene with protein product
- Date approved:
- 1999-09-16
- Date modifiied:
- 2018-05-03
- Gene:
- ARHGAP42 NIH gene
- Name:
- Rho GTPase activating protein 42
- Previous symbol:
- TMEM133
- Synonyms:
- FLJ32810, GRAF3, AD031
- Chromosome:
- 11q22.1
- Locus Type:
- gene with protein product
- Date approved:
- 2010-04-28
- Date modifiied:
- 2017-11-20
- Gene:
- C1QTNF12 NIH gene
- Name:
- C1q and TNF related 12
- Previous symbol:
- C1QDC2, FAM132A
- Synonyms:
- MGC105127, CTRP12, ADIPOLIN
- Chromosome:
- 1p36.33
- Locus Type:
- gene with protein product
- Date approved:
- 2005-09-27
- Date modifiied:
- 2018-11-15
Related products to: AKAP7 monoclonal antibody (M13), clone 1F9
Related articles to: AKAP7 monoclonal antibody (M13), clone 1F9
- The cardiac I current stabilizes the resting membrane potential of cardiomyocytes. Protein kinase A (PKA) induces an inhibition of I current which strongly promotes focal arrhythmogenesis. The molecular mechanisms underlying this regulation have only partially been elucidated yet. Furthermore, the role of A-kinase anchoring proteins (AKAPs) in this regulation has not been examined to date. The objective of this project was to elucidate the molecular mechanisms underlying the inhibition of I by PKA and to identify novel molecular targets for antiarrhythmic therapy downstream β-adrenoreceptors. Patch clamp and voltage clamp experiments were used to record currents and co-immunoprecipitation, and co-localization experiments were performed to show spatial and functional coupling. Activation of PKA inhibited I current in rat cardiomyocytes. This regulation was markedly attenuated by disrupting PKA-binding to AKAPs with the peptide inhibitor AKAP-IS. We observed functional and spatial coupling of the plasma membrane-associated AKAP15 and AKAP79 to Kir2.1 and Kir2.2 channel subunits, but not to Kir2.3 channels. In contrast, AKAPyotiao had no functional effect on the PKA regulation of Kir channels. AKAP15 and AKAP79 co-immunoprecipitated with and co-localized to Kir2.1 and Kir2.2 channel subunits in ventricular cardiomyocytes. In this study, we provide evidence for coupling of cardiac Kir2.1 and Kir2.2 subunits with the plasma membrane-bound AKAPs 15 and 79. Cardiac membrane-associated AKAPs are a functionally essential part of the regulatory cascade determining I current function and may be novel molecular targets for antiarrhythmic therapy downstream from β-adrenoreceptors. - Source: PubMed
Publication date: 2017/03/22
Seyler ClaudiaScherer DanielKöpple ChristophKulzer MartinKorkmaz SevilXynogalos PanagiotisThomas DierkKaya ZiyaScholz EberhardBacks JohannesKarle ChristophKatus Hugo AZitron Edgar - PKA is retained within distinct subcellular environments by the association of its regulatory type II (RII) subunits with A-kinase anchoring proteins (AKAPs). Conventional reagents that universally disrupt PKA anchoring are patterned after a conserved AKAP motif. We introduce a phage selection procedure that exploits high-resolution structural information to engineer RII mutants that are selective for a particular AKAP. Selective RII (RSelect) sequences were obtained for eight AKAPs following competitive selection screening. Biochemical and cell-based experiments validated the efficacy of RSelect proteins for AKAP2 and AKAP18. These engineered proteins represent a new class of reagents that can be used to dissect the contributions of different AKAP-targeted pools of PKA. Molecular modeling and high-throughput sequencing analyses revealed the molecular basis of AKAP-selective interactions and shed new light on native RII-AKAP interactions. We propose that this structure-directed evolution strategy might be generally applicable for the investigation of other protein interaction surfaces. - Source: PubMed
Publication date: 2013/04/26
Gold Matthew GFowler Douglas MMeans Christopher KPawson Catherine TStephany Jason JLangeberg Lorene KFields StanleyScott John D - - Source: PubMed
Scott John DSantana Luis F - Protein kinase A anchoring proteins or AKAPs regulate the activity of many ion channels. Protein kinase A (PKA) is a well-recognized target of AKAPs, with other kinases now emerging as additional targets. We examined the roles of epithelial-expressed AKAPs in regulating the epithelial Na+ channel (ENaC). Experiments used heterologous expression with AKAP15, AKAP-KL, and AKAP79 in Xenopus oocytes. Experiments were carried out under high and low Na+ conditions, as Na+ loading is known to affect the baseline activity of ENaC in a PKC-dependent mechanism. ENaC activity was unaffected by AKAP79 and AKAP-KL expression. However, oocytes coexpressing AKAP15 exhibited an 80% and 91% reduction in the amiloride-sensitive, whole-cell conductance in high and low Na+ conditions, respectively. The reduced channel activity was unaffected by PKA activation or inhibition, indicating a PKA-independent mechanism. Expression with a membrane-targeting domain, mutant form of AKAP15 (AKAP15m) prevented the decrease of ENaC activity, but only under low Na+ conditions. In high sodium conditions, coexpression with AKAP15m led to an increase of ENaC activity to levels similar to those observed under low Na+. These results indicate that membrane-associated AKAP15 reduces ENaC activity whereas the cytoplasmically associated one may participate in the channel's feedback inhibition by intracellular Na+, a process known to involve PKC. This hypothesis was further confirmed in coexpression experiments, which demonstrated functional and physical interaction between AKAP15 and PKCalpha. We propose that AKAP15 regulates ENaC via a novel PKA-independent pathway. - Source: PubMed
Publication date: 2007/01/23
Bengrine AbderrahmaneLi JinqingAwayda Mouhamed S - In cardiac myocytes, the slow component of the delayed rectifier K(+) current (I(Ks)) is regulated by cAMP. Elevated cAMP increases I(Ks) amplitude, slows its deactivation kinetics, and shifts its activation curve. At the molecular level, I(Ks) channels are composed of KvLQT1/IsK complexes. In a variety of mammalian heterologous expression systems maintained at physiological temperature, we explored cAMP regulation of recombinant KvLQT1/IsK complexes. In these systems, KvLQT1/IsK complexes were totally insensitive to cAMP regulation. cAMP regulation was not restored by coexpression with the dominant negative isoform of KvLQT1 or with the cystic fibrosis transmembrane regulator. In contrast, coexpression of the neuronal A kinase anchoring protein (AKAP)79, a fragment of a cardiac AKAP (mAKAP), or cardiac AKAP15/18 restored cAMP regulation of KvLQT1/IsK complexes inasmuch as cAMP stimulation increased the I(Ks) amplitude, increased its deactivation time constant, and negatively shifted its activation curve. However, in cells expressing an AKAP, the effects of cAMP stimulation on the I(Ks) amplitude remained modest compared with those previously reported in cardiac myocytes. The effects of cAMP stimulation were fully prevented by including the Ht31 peptide (a global disruptor of protein kinase A anchoring) in the intracellular medium. We concluded that cAMP regulation of I(Ks) requires protein kinase A anchoring by AKAPs, which therefore participate with the channel protein complex underlying I(Ks). - Source: PubMed
Potet FScott J DMohammad-Panah REscande DBaró I