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anti-Human Rhodopsin Antikörper:
anti-Mouse (Murine) Rhodopsin Antikörper:
anti-Rat (Rattus) Rhodopsin Antikörper:
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Human Monoclonal Rhodopsin Primary Antibody für IF, WB - ABIN968301
Brandt, Gimona, Hillmann, Haller, Mischak: Protein kinase C induces actin reorganization via a Src- and Rho-dependent pathway. in The Journal of biological chemistry 2002
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Human Monoclonal Rhodopsin Primary Antibody für IF, WB - ABIN968300
Madaule, Axel: A novel ras-related gene family. in Cell 1985
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Chemical Monoclonal Rhodopsin Primary Antibody für ICC, IF - ABIN4350422
Li, He, Li, Ni, Sun, Zhou: Proliferation and differentiation of direct co‑culture of bone marrow mesenchymal stem cells and pigmented cells from the ciliary margin. in Molecular medicine reports 2017
Chemical Monoclonal Rhodopsin Primary Antibody für ICC, IF - ABIN863083
Molday, Hicks, Molday: Peripherin. A rim-specific membrane protein of rod outer segment discs. in Investigative ophthalmology & visual science 1987
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Chemical Monoclonal Rhodopsin Primary Antibody für ICC, IF - ABIN863085
Iannaccone, Man, Waseem, Jennings, Ganapathiraju, Gallaher, Reese, Bhattacharya, Klein-Seetharaman: Retinitis pigmentosa associated with rhodopsin mutations: Correlation between phenotypic variability and molecular effects. in Vision research 2006
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Chemical Monoclonal Rhodopsin Primary Antibody für IF, IHC - ABIN267076
Cia, Cubizolle, Crauste, Jacquemot, Guillou, Vigor, Angebault, Hamel, Vercauteren, Brabet: Phloroglucinol protects retinal pigment epithelium and photoreceptor against all-trans-retinal-induced toxicity and inhibits A2E formation. in Journal of cellular and molecular medicine 2016
Organisms use multiple strategies to maximize visual capabilities in different light conditions. Many invertebrates show a daily cycle of shedding the photoreceptor's rhabdomeric membranes at dawn and rebuilding these during the following night. We show here that the Aedes aegypti mosquito possesses two distinct light-driven cellular signaling processes for modulating rhodopsin content during this cycle.
Fmr1 (zeige FMR1 Antikörper) protein associates with ninaE mRNA and represses its translation.
Data show that site-directed mutagenesis of conserved residues has only modest effects on Rhodopsin 1 absorption.
Data indicate that mutations in Golgi SNARE (zeige GOSR2 Antikörper) protein gos28 (zeige GOSR1 Antikörper) lead to defective rhodopsin (Rh1) trafficking.
Upon light stimulation, Crag is required for trafficking of Rh from the trans-Golgi network to rhabdomere membranes via a Rab11-dependent vesicular transport.
GPI (zeige GPI Antikörper) biosynthesis is essential for rhodopsin sorting at the trans-Golgi network in Drosophila photoreceptors
Our results indicate that fatp promotes photoreceptor survival by regulating Rh1 abundance
Light reception mediated by Rh5 and Rh6 must utilize either a different (nonretinal) phospholipase C-beta (zeige PLCb4 Antikörper) enzyme or alternative signaling mechanisms, at least in terms of clock-relevant photoreception
Dominant rhodopsin (ninaE) mutants showed progressive age-dependent and light-independent loss of the deep pseudopupil.
These data show that the Drosophila metallophosphoesterase-dephosphorylated alpha-Man-II (zeige MAN2A1 Antikörper) is required for the removal of the Rh1 oligosaccharide chain.
Wild-type opsin mainly formed oligomers. Only a minor population formed aggregates. The G188R opsin mutant mainly formed aggregates. When wild-type opsin and G188R opsin were coexpressed in cells, properly folded wild-type opsin did not aggregate with G188R opsin and was trafficked normally to the cell membrane. The autosomal dominant phenotype due to misfolded opsin mutants is not due to WT-mutant physical interaction.
Data suggest that retinitis pigmentosa-associated mutation G51A behaves differently in human rhodopsin compared to bovine rhodopsin; human rhodopsin is more thermally stable than ancestral ancestrally reconstructed mammalian rhodopsin.
The metformin-rescued P23H rhodopsin was still intrinsically unstable and led to increased structural instability of the rod outer segments. These data suggest that improving the traffic of misfolding rhodopsin mutants is unlikely to be a practical therapy, but also highlights the potential of altering translation through AMPK (zeige PRKAA1 Antikörper) to improve protein function in other protein misfolding diseases
Study reports an X-ray free electron laser crystal structure of the rhodopsin-arrestin (zeige SAG Antikörper) complex, in which the phosphorylated C terminus of rhodopsin forms an extended intermolecular beta sheet with the N-terminal beta strands of arrestin (zeige SAG Antikörper). Phosphorylation was detected at rhodopsin C-terminal tail residues T336 and S338.
results suggest that nonsense-mediated mRNA decay modulates the severity of retinitis pigmentosa in patients with nonsense mutations in the rhodopsin gene
both the charged G90D(2.57) and the hydrophobic T94I(2.61) mutation alter the dark state by weakening the interaction between the Schiff base (SB) and its counterion E113(3.28) We propose that this interference with the tight regulation of the dim light photoreceptor rhodopsin increases background noise in the visual system and causes the loss of night vision characteristic for CSNB (zeige CSN2 Antikörper) patients.
a recurrent missense mutation (c.403C > T, p.R135W) in the rhodopsin (RHO) gene cosegregated with all retinitis pigmentosa affected individuals in the family.
Autosomal recessive retinitis pigmentosa with homozygous rhodopsin mutation E150K and non-coding cis-regulatory variants in CRX-binding regions of SAMD7.
Functional role of positively selected amino acid substitutions in mammalian rhodopsin evolution has been uncovered for a large number of mammalian species.
Our study shows that RHO mutations are a major cause of adRP (zeige PLIN2 Antikörper) in this cohort and are responsible for 28% of adRP (zeige PLIN2 Antikörper) families.
These findings revealed a total water flux between the bulk and the protein inside in the Meta II state, and suggested that these pathways provide water molecules to the crucial sites of the activated rhodopsin.
Data suggest that a hetero-multimer complex forms between light-activated rhodopsin and light-activated heterotrimeric transducin (zeige GNAT1 Antikörper) (T-alpha-1, Gnb1 (zeige GNB1 Antikörper), Gngt1 (zeige GNGT1 Antikörper)); the stoichiometry is 1:1 rhodopsin:transducin. The complex appears to form on native rod outer segment membranes upon light activation.
Study presents a comprehensive analysis of the kinetics and thermodynamics of the recombination reaction between opsin and 11-cis (zeige CISH Antikörper)-retinal (11CR) to form the mature visual pigment, Rho; and found that the lipid bilayer environment is important for ligand binding in Rho.
In response to light-induced isomerization of the retinal chromophore rhodopsin, hydrogen-bonding interactions involving these C=O groups are released, thus facilitating repacking of H5 and H7 onto the transmembrane core of the receptor.
rhodopsin can tolerate a second Lys (zeige LYZ Antikörper) in the retinal binding pocket and suggest that an evolutionary intermediate with two Lys (zeige LYZ Antikörper) could allow migration of the Schiff base Lys (zeige LYZ Antikörper) to a position other than the observed, highly conserved location in the seventh TM helix
multiconfigurational quantum chemistry is used to compare the isomerization mechanisms of the sensory rhodopsin from the cyanobacterium Anabaena PCC 7120 (ASR) and of the bovine rhodopsin (Rh).
show that although the basic activation pathways of human and bovine rhodopsin are similar, structural deviations exist in the inactive conformation and during receptor activation, even between closely related rhodopsins
DMPC/DHPC bicelles dramatically increase the thermal stability of the rhodopsin mutants G90V and N55K.
The molecular mechanism of the ultrafast reversible photoreaction of visual pigment rhodopsin may be used as a concept for the development of an ultrafast optical molecular switch.
Rab8a (zeige RAB8A Antikörper) and Rab11a (zeige RAB11A Antikörper) Are Dispensable for Rhodopsin Transport in Mouse Photoreceptors
This study demonstrated that Rhodopsin Phosphorylation on Dark Adaptation in Mouse Rods.
Findings indicate that Rho and ROCK knockout may improve the behavior of mice and prevent MPTP (zeige PTPN2 Antikörper)-induced dopaminergic neurons damage by regulating Sema3A (zeige SEMA3A Antikörper), PlexinA and NRP-1 (zeige NRP1 Antikörper) in a mouse model of Parkinson's disease.
The authors elucidated this dependency by showing that guanylate cyclase-1 is a novel rhodopsin-binding protein.
Eliminating Cngb1 (zeige CNGB1 Antikörper) and reducing RDS (zeige PRPH2 Antikörper) leads to additive defects in RDS (zeige PRPH2 Antikörper) expression levels and rod electroretinogram (ERG (zeige ERG Antikörper)) function, (e.g., Cngb1 (zeige CNGB1 Antikörper)-/-/rds (zeige PRPH2 Antikörper)+/- versus rds (zeige PRPH2 Antikörper)+/- or Cngb1 (zeige CNGB1 Antikörper)-/-) but not to additive defects in rod ultrastructure.
These findings reveal that an early and significant pathophysiologic effect of endoplasmic reticulum stress in photoreceptors is the highly efficient elimination of misfolded rhodopsin protein.
Data show that G90D1 ribozyme efficiently and specifically cleaved the mutant transcript of the G90D mutation in the rhodopsin gene while G90D2 ribozyme cleaved both WT and mutant transcript.
Data show that misfolded opsin mutants form aggregates in the endoplasmic reticulum.
Data show that the step-like responses of serine-only rhodopsin reflect slow and stochastic arrestin (zeige SAG Antikörper) binding.
The form-deprived experimental myopia groups showed an increased expression of rhodopsin and its mRNA compared to the controls.
overexpression of full-length rhodopsin or its cytoplasmic tail domain, but not of rhodopsin lacking the cytoplasmic tail, exacerbated rod degeneration in kif3a (zeige KIF3A Antikörper) mutants, implying an important role of the cytoplasmic tail in rod degeneration.
expression as well as the protein localization of rhodopsin in the zebrafish from larval to adult stage were demonstrated; results demonstrated the involvement of rhodopsin in the zebrafish pineal gland physiology particularly in light capture during the zebrafish lifespan
Mitogen-associated protein kinase (zeige TGFB3 Antikörper) and protein kinase A regulate rhodopsin transcription through parallel signal transduction pathways
the rhodopsin is densely packed in the retina and the rhodopsin molecules are not aligned well.
Phototransduction, even when initiated by wild type rhodopsin, is altered in a way progressive with level of retinal degeneration. A model introduces idea of binding site for carboxy terminus of rhodopsin on rhodopsin kinase (zeige GRK1 Antikörper).
Retinal degeneration in the P23H (proline-to-histidine) rhodopsin mutation is partially reversed, with regeneration of rod photoreceptors recovering normal morphology in a retinitis pigmentosa model.
the Xenopus rhodopsin gene has conserved transcriptional activators
The newly identified ciliary targeting VxPx motif present in rhodopsin binds the small GTPase (zeige RACGAP1 Antikörper) Arf4 (zeige ARF4 Antikörper) and regulates its association with the trans-Golgi network.
Retinitis pigmentosa is an inherited progressive disease which is a major cause of blindness in western communities. It can be inherited as an autosomal dominant, autosomal recessive, or X-linked recessive disorder. In the autosomal dominant form,which comprises about 25% of total cases, approximately 30% of families have mutations in the gene encoding the rod photoreceptor-specific protein rhodopsin. This is the transmembrane protein which, when photoexcited, initiates the visual transduction cascade. Defects in this gene are also one of the causes of congenital stationary night blindness.
, rhodopsin 4
, R8 rhodopsin
, rhodopsin 6
, rhodopsin 1
, rhodopsin 3
, rhodopsin (opsin 2, rod pigment) (retinitis pigmentosa 4, autosomal dominant)
, opsin 2, rod pigment
, rod opsin
, L opsin
, LWS opsin
, Long Wavelength Sensitive opsin
, Red Opsin
, Rod Opsin
, opsin 2
, Rhodopsin (retinitis pigmentosa 4, autosomal dominant)
, retinal rod opsin pigment rh1.1