Ask about this productRelated genes to: RGS9 Blocking Peptide
- Gene:
- RGS9 NIH gene
- Name:
- regulator of G protein signaling 9
- Previous symbol:
- -
- Synonyms:
- PERRS, RGS9L, MGC26458, MGC111763
- Chromosome:
- 17q24.1
- Locus Type:
- gene with protein product
- Date approved:
- 1998-12-15
- Date modifiied:
- 2017-04-13
- Gene:
- RGS9BP NIH gene
- Name:
- regulator of G protein signaling 9 binding protein
- Previous symbol:
- -
- Synonyms:
- FLJ45744, PERRS, R9AP, RGS9
- Chromosome:
- 19q13.11
- Locus Type:
- gene with protein product
- Date approved:
- 2006-10-05
- Date modifiied:
- 2017-04-13
Related products to: RGS9 Blocking Peptide
Related articles to: RGS9 Blocking Peptide
- Phototransduction, the process by which captured photons elicit electrical changes in retinal rod and cone cells, represents the first neuronal step in vision and involves interactions between several highly specialised proteins. Pathogenic variants in genes encoding many of these proteins can give rise to significant vision impairment, accounting for a substantial portion of inherited retinal disease. Such genes include RHO, OPN1LW, OPN1MW, GNAT1, GNAT2, GNB3, PDE6A, PDE6B, PDE6G, PDE6C, PDE6H, CNGA1, CNGB1, CNGA3, CNGB3, GRK1, SAG, ARR3, RGS9, RGS9BP, GUCY2D, GUCA1A and SLC24A1. Many of these conditions have distinct mechanisms and clinical features. They follow several modes of inheritance (including in one case digenic, or tri-allelic, inheritance). Some conditions also entail myopia. Rod and cone phototransduction will be outlined, followed by the discussion of diseases associated with these genes. Some phenotypic features will be highlighted as well as their prevalence in a large genotyped inherited retinal disease cohort. - Source: PubMed
Publication date: 2025/02/27
Wong Wendy MMahroo Omar A - Purification of recombinant proteins is often achieved using a purification tag which can be located either at the N- or C-terminus of a passenger protein of interest. Many purification tags exist and their advantages and limitations are well documented. However, designing fusion proteins can be a challenging task to get a fully expressed, soluble and highly purified passenger protein. Besides, there is a lack of systematic studies on the use of a single tag versus combined tags and on the effect of the position of the tags in the construct. In the present study, 9 different fusion proteins were expressed in Escherichia coli using some of the most commonly used purification tags: maltose-binding protein (MBP), glutathione S-transferase (GST) and polyHis tag. The expression and purification of N-terminus single-tagged fusion proteins (MBP, GST and polyHis) and fusion proteins with combined tags at different positions have been tested. Both the identity of the tag(s) and its position were found to have a strong effect on the expression, solubility and purification yields of the fusion proteins. Consequently, the different fusion proteins assayed have shown varying expression, solubility and purification yields, which were also dependent on the passenger protein. Therefore, there is a compelling need to design various fusion proteins with different single or combined tags to identify optimized constructions allowing to achieve high levels of expression, solubility and purification of the passenger protein. - Source: PubMed
Publication date: 2018/07/20
Bernier Sarah CCantin LineSalesse Christian - Novel diagnostic predictors and drug targets are needed for LUAD (lung adenocarcinoma). We aimed to build a specific SVM (support vector machine) classifier for diagnosis of LUAD and identify molecular markers with prognostic value for LUAD. - Source: PubMed
Publication date: 2018/05/25
Zhao JingmingCheng WeiHe XigangLiu YanliLi JiSun JiaxingLi JinfengWang FangfangGao Yufang - To characterize photoreceptor structure and mosaic integrity in subjects with RGS9- and R9AP-associated retinal dysfunction (bradyopsia) and compare to previous observations in other cone dysfunction disorders such as oligocone trichromacy. - Source: PubMed
Publication date: 2015/09/03
Strauss Rupert WDubis Adam MCooper Robert FBa-Abbad RolaMoore Anthony TWebster Andrew RDubra AlfredoCarroll JosephMichaelides Michel - Phototransduction cascade takes place in disc membranes of photoreceptor cells. Following its activation by light, rhodopsin activates the G-protein transducin causing the dissociation of its GTP-bound α-subunit, which in turn activates phosphodiesterase 6 (PDE6) leading to the hyperpolarization of photoreceptor cells. PDE6 must then be inactivated to return to the dark state. This is achieved by a protein complex which is presumably anchored to photoreceptor disc membranes by means of the transmembrane C-terminal segment of RGS9-1-Anchor Protein (R9AP). Information on the secondary structure and membrane binding properties of the C-terminal segment of R9AP is not yet available to further support its role in the membrane anchoring of this protein. In the present study, circular dichroism and infrared spectroscopy measurements have allowed us to determine that the C-terminal segment of human and bovine R9AP adopts an α-helical structure in solution. Moreover, this C-terminal segment has shown affinity for most of the phospholipids typical of photoreceptor membranes. In fact, the physical state and the type of phospholipid as well as electrostatic interactions influence the binding of the human and bovine peptides to phospholipid monolayers. In addition, these measurements revealed that the human peptide has a high affinity for saturated phosphocholine, which may suggest a possible localization of R9AP in photoreceptor microdomains. Accordingly, infrared spectroscopy measurements have allowed determining that the C-terminal segment of R9AP adopts an ordered α-helical structure in the presence of saturated phospholipid monolayers. Altogether, these data are consistent with the typical α-helical secondary structure and behavior observed for transmembrane segments and with the proposed role of membrane anchoring of the C-terminal segment of human and bovine R9AP. - Source: PubMed
Publication date: 2015/02/05
Bernier Sarah CHorchani HabibSalesse Christian