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anti-Human Rhodopsin Antibodies:
anti-Rat (Rattus) Rhodopsin Antibodies:
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Mouse (Murine) Polyclonal Rhodopsin Primary Antibody for IHC, ELISA - ABIN1532407
Petersen, Olsen, Christensen, Hansen, Christensen, Brandslund: Rhodopsin in plasma from patients with diabetic retinopathy - development and validation of digital ELISA by Single Molecule Array (Simoa) technology. in Journal of immunological methods 2017
Chemical Monoclonal Rhodopsin Primary Antibody for ELISA, ICC - ABIN4350402
Cubizolle, Guillou, Mollereau, Hamel, Brabet: Fatty acid transport protein 1 regulates retinoid metabolism and photoreceptor development in mouse retina. in PLoS ONE 2017
Chemical Monoclonal Rhodopsin Primary Antibody for IF, IHC - ABIN4995405
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
Chemical Monoclonal Rhodopsin Primary Antibody for 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 for ICC, IF - ABIN863083
Molday, Hicks, Molday: Peripherin. A rim-specific membrane protein of rod outer segment discs. in Investigative ophthalmology & visual science 1987
Show all 4 Pubmed References
Chemical Monoclonal Rhodopsin Primary Antibody for 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
Show all 4 Pubmed References
data provide the first evidence that T17M rhodopsin mutant disrupts C3 secretion via the induction of ROS (show ROS1 Antibodies) and the suppression of TWIST1 (show TWIST1 Antibodies).
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 (show PRKAA1 Antibodies) to improve protein function in other protein misfolding diseases
Study reports an X-ray free electron laser crystal structure of the rhodopsin-arrestin (show SAG Antibodies) complex, in which the phosphorylated C terminus of rhodopsin forms an extended intermolecular beta sheet with the N-terminal beta strands of arrestin (show SAG Antibodies). 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 (show CSN2 Antibodies) 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.
overexpression of full-length rhodopsin or its cytoplasmic tail domain, but not of rhodopsin lacking the cytoplasmic tail, exacerbated rod degeneration in kif3a (show KIF3A Antibodies) 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 (show TGFB3 Antibodies) and protein kinase A regulate rhodopsin transcription through parallel signal transduction pathways
Photoactivation of rhodopsin increases near-Infrared backscattering from rods and causes lengthening of their rod outer segment.
Specific visible radiation facilitates lipolysis in mature 3T3-L1 adipocytes via rhodopsin-dependent beta3-adrenergic signaling.
Rab8a (show RAB8A Antibodies) and Rab11a (show RAB11A Antibodies) 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 (show PTPN2 Antibodies)-induced dopaminergic neurons damage by regulating Sema3A (show SEMA3A Antibodies), PlexinA and NRP-1 (show NRP1 Antibodies) 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 (show CNGB1 Antibodies) and reducing RDS (show PRPH2 Antibodies) leads to additive defects in RDS (show PRPH2 Antibodies) expression levels and rod electroretinogram (ERG (show ERG Antibodies)) function, (e.g., Cngb1 (show CNGB1 Antibodies)-/-/rds (show PRPH2 Antibodies)+/- versus rds (show PRPH2 Antibodies)+/- or Cngb1 (show CNGB1 Antibodies)-/-) 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.
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 (show RACGAP1 Antibodies) Arf4 (show ARF4 Antibodies) and regulates its association with the trans-Golgi network.
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 (show GRK1 Antibodies).
The study shows that, compared to the inactive 11-cis (show CISH Antibodies)-retinal case, trans-retinal rhodopsin is able to undergo protonated Schiff base (PSB) deprotonation due to a change in the conformation of the retinal and a consequent alteration in the hydrogen-bond (HB) network in which PSB and the counterion Glu113 are embedded.
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 (show GNAT1 Antibodies) (T-alpha-1, Gnb1 (show GNB1 Antibodies), Gngt1 (show GNGT1 Antibodies)); 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 (show CISH Antibodies)-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 (show LYZ Antibodies) in the retinal binding pocket and suggest that an evolutionary intermediate with two Lys (show LYZ Antibodies) could allow migration of the Schiff base Lys (show LYZ Antibodies) 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 form-deprived experimental myopia groups showed an increased expression of rhodopsin and its mRNA compared to the controls.
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.
opsin 2, rod pigment
, Rhodopsin (retinitis pigmentosa 4, autosomal dominant)
, retinal rod opsin pigment rh1.1
, rod opsin
, L opsin
, LWS opsin
, Long Wavelength Sensitive opsin
, Red Opsin
, Rod Opsin
, opsin 2
, rhodopsin (opsin 2, rod pigment) (retinitis pigmentosa 4, autosomal dominant)