anti mouse detection module for jess (Protein Simple Inc)

Protein Simple Inc anti mouse detection module for jess

Anti Mouse Detection Module For Jess, supplied by Protein Simple Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/anti mouse detection module for jess/product/Protein Simple Inc
Average 94 stars, based on 1 article reviews

anti mouse detection module for jess - by Bioz Stars, 2026-04

94/100 stars

Buy from Supplier

data analysis ht software version 12 0 1 55 (Sartorius AG)

Sartorius AG data analysis ht software version 12 0 1 55

Data Analysis Ht Software Version 12 0 1 55, supplied by Sartorius AG, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/data analysis ht software version 12 0 1 55/product/Sartorius AG
Average 86 stars, based on 1 article reviews

data analysis ht software version 12 0 1 55 - by Bioz Stars, 2026-04

86/100 stars

Buy from Supplier

pgc1 α (Proteintech)

Proteintech pgc1 α

GSTK1 promotes mitochondrial biosynthesis and mitochondrial fusion, while inhibiting mitochondrial fission and mitophagy. ( A-B ) Representative TEM images of mitochondria in HCC cells lines related to Fig. (bar = 5–1 μm). ( C ) Immunoblotting analysis of MFN1, MFN2, DRP1, p-DRP1, <t>PGC1-α,</t> P62, LC3II: I ratio, TOMM20, GSTK1, and β-actin in HCC cells lines related to Fig. . ( D ) Immunofluorescent staining of p-DRP1(S616) in HCC cells lines related to Fig. (bar = 10 μm). ( E ) Immunofluorescent staining of TOMM20 in HepG2 and HCC-LM3 cells stably transfected (mRFP-EGFP-LC3B), then transiently transfected (OE-GSTK1 or shGSTK1 [bar = 10 μm]). ( F ) Immunoblotting analysis of Mfn1, Mfn2, Drp1, p-Drp1, Pgc1-α, p62, LC3II/I, Tomm20, GSTK1, and β-actin in mice tumor tissues related to Fig. . ( G ) Immunofluorescent staining of GSTK1 and p-Drp1(S616) in liver sections from DEN/CCl 4 - or DEN/HFFCD-treated various mice related to Fig. (bar = 20 μm). n.s, no significance, * P < 0.05

Pgc1 α, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/pgc1 α/product/Proteintech
Average 96 stars, based on 1 article reviews

pgc1 α - by Bioz Stars, 2026-04

96/100 stars

Buy from Supplier

simulation software cst microwave studio (Cell Signaling Technology Inc)

Cell Signaling Technology Inc simulation software cst microwave studio

Simulation Software Cst Microwave Studio, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/simulation software cst microwave studio/product/Cell Signaling Technology Inc
Average 95 stars, based on 1 article reviews

simulation software cst microwave studio - by Bioz Stars, 2026-04

95/100 stars

Buy from Supplier

mouse monoclonal anti recoverin antibodies (Santa Cruz Biotechnology)

Santa Cruz Biotechnology mouse monoclonal anti recoverin antibodies
$Identification of multimeric oxidized forms of <t>recoverin</t> in the retina of albino rats and pigmented rabbits exposed to different doses of visual light illumination. Western blotting under non-reducing or reducing conditions of recoverin fractions extracted from the rat retinas illuminated in vivo for 14 h with metal halide lamp (2,500 lx, ‘exp’) (A) , and rabbit retinas illuminated in vivo for 3 h with halogen lamp following scheme 1 (2,200 lx, ‘exp S1’) or scheme 2 (30,000 lx, ‘exp S2’) (B) . The recoverin fractions obtained from the dark-adapted retinas were used as a control (‘contr’). ‘M,’ ‘M2,’ and ‘A’ denote monomeric, dimeric, and multimeric/aggregated forms of recoverin, respectively. Volumes of the loaded recoverin samples were chosen to ensure nearly equivalent bands of the monomeric protein. The numbers in left-hand columns indicate the molecular masses of protein markers in kDa. (C) The weight fractions of monomeric and dimeric forms of rabbit recoverin estimated from the Western blotting data from at least three independent in vivo experiments.$
Mouse Monoclonal Anti Recoverin Antibodies, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/mouse monoclonal anti recoverin antibodies/product/Santa Cruz Biotechnology
Average 93 stars, based on 1 article reviews

mouse monoclonal anti recoverin antibodies - by Bioz Stars, 2026-04

93/100 stars

Buy from Supplier

affinity suite version 2.16.0 (rem440 software module) (Interacoustics AS)

Interacoustics AS affinity suite version 2.16.0 (rem440 software module)
$Identification of multimeric oxidized forms of <t>recoverin</t> in the retina of albino rats and pigmented rabbits exposed to different doses of visual light illumination. Western blotting under non-reducing or reducing conditions of recoverin fractions extracted from the rat retinas illuminated in vivo for 14 h with metal halide lamp (2,500 lx, ‘exp’) (A) , and rabbit retinas illuminated in vivo for 3 h with halogen lamp following scheme 1 (2,200 lx, ‘exp S1’) or scheme 2 (30,000 lx, ‘exp S2’) (B) . The recoverin fractions obtained from the dark-adapted retinas were used as a control (‘contr’). ‘M,’ ‘M2,’ and ‘A’ denote monomeric, dimeric, and multimeric/aggregated forms of recoverin, respectively. Volumes of the loaded recoverin samples were chosen to ensure nearly equivalent bands of the monomeric protein. The numbers in left-hand columns indicate the molecular masses of protein markers in kDa. (C) The weight fractions of monomeric and dimeric forms of rabbit recoverin estimated from the Western blotting data from at least three independent in vivo experiments.$
Affinity Suite Version 2.16.0 (Rem440 Software Module), supplied by Interacoustics AS, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/affinity suite version 2.16.0 (rem440 software module)/product/Interacoustics AS
Average 90 stars, based on 1 article reviews

affinity suite version 2.16.0 (rem440 software module) - by Bioz Stars, 2026-04

90/100 stars

Buy from Supplier

s200 control software lmw kinetics/affinity multi-cycle module (Biacore)

Biacore s200 control software lmw kinetics/affinity multi-cycle module
$Identification of multimeric oxidized forms of <t>recoverin</t> in the retina of albino rats and pigmented rabbits exposed to different doses of visual light illumination. Western blotting under non-reducing or reducing conditions of recoverin fractions extracted from the rat retinas illuminated in vivo for 14 h with metal halide lamp (2,500 lx, ‘exp’) (A) , and rabbit retinas illuminated in vivo for 3 h with halogen lamp following scheme 1 (2,200 lx, ‘exp S1’) or scheme 2 (30,000 lx, ‘exp S2’) (B) . The recoverin fractions obtained from the dark-adapted retinas were used as a control (‘contr’). ‘M,’ ‘M2,’ and ‘A’ denote monomeric, dimeric, and multimeric/aggregated forms of recoverin, respectively. Volumes of the loaded recoverin samples were chosen to ensure nearly equivalent bands of the monomeric protein. The numbers in left-hand columns indicate the molecular masses of protein markers in kDa. (C) The weight fractions of monomeric and dimeric forms of rabbit recoverin estimated from the Western blotting data from at least three independent in vivo experiments.$
S200 Control Software Lmw Kinetics/Affinity Multi Cycle Module, supplied by Biacore, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/s200 control software lmw kinetics/affinity multi-cycle module/product/Biacore
Average 90 stars, based on 1 article reviews

s200 control software lmw kinetics/affinity multi-cycle module - by Bioz Stars, 2026-04

90/100 stars

Buy from Supplier

Image Search Results

Journal: iScience

Article Title: Structurally-discovered KLF4 variants accelerate and stabilize reprogramming to pluripotency

doi: 10.1016/j.isci.2021.103525

Figure Lengend Snippet:

Article Snippet: Anti-Mouse Detection Module for Jess, Wes, Peggy Sue or Sally Sue , ProteinSimple , Cat#DM-002.

Techniques: Affinity Purification, Produced, Control, Recombinant, Magnetic Beads, Transfection, Mutagenesis, Chromatin Immunoprecipitation, DNA Purification, Real-time Polymerase Chain Reaction, Isolation, Transgenic Assay, Retroviral, Plasmid Preparation, Software

Journal: Journal of Experimental & Clinical Cancer Research : CR

Article Title: GSTK1 suppresses HCC aggravation via L-carnitine metabolism by PGAM5/DRP1 complex-mediated mitochondrial quality control

doi: 10.1186/s13046-025-03580-8

Figure Lengend Snippet: GSTK1 promotes mitochondrial biosynthesis and mitochondrial fusion, while inhibiting mitochondrial fission and mitophagy. ( A-B ) Representative TEM images of mitochondria in HCC cells lines related to Fig. (bar = 5–1 μm). ( C ) Immunoblotting analysis of MFN1, MFN2, DRP1, p-DRP1, PGC1-α, P62, LC3II: I ratio, TOMM20, GSTK1, and β-actin in HCC cells lines related to Fig. . ( D ) Immunofluorescent staining of p-DRP1(S616) in HCC cells lines related to Fig. (bar = 10 μm). ( E ) Immunofluorescent staining of TOMM20 in HepG2 and HCC-LM3 cells stably transfected (mRFP-EGFP-LC3B), then transiently transfected (OE-GSTK1 or shGSTK1 [bar = 10 μm]). ( F ) Immunoblotting analysis of Mfn1, Mfn2, Drp1, p-Drp1, Pgc1-α, p62, LC3II/I, Tomm20, GSTK1, and β-actin in mice tumor tissues related to Fig. . ( G ) Immunofluorescent staining of GSTK1 and p-Drp1(S616) in liver sections from DEN/CCl 4 - or DEN/HFFCD-treated various mice related to Fig. (bar = 20 μm). n.s, no significance, * P < 0.05

Article Snippet: Rabbit antibody to CPT1A (15184-1-AP [RRID: AB_2084676]), CPT2 (26555-1-AP [RRID: AB_2880551]), BBOX1 (16099-1-AP [RRID: AB_2243498]), SLC25A20 (19363-1-AP [RRID: AB_10642001]), GSTK1 (14535-1-AP [RRID: AB_2115910]), PGAM5 (28445-1-AP [RRID: AB_2881143]) and mouse antibody to PGC1-α (66369-1-Ig [RRID: AB_2828002]), PGAM5 (68116-1-Ig [RRID: AB_2923645]) and beta-actin (66009-1-Ig [RRID: AB_2687938]) were obtained from Proteintech.

Techniques: Western Blot, Staining, Stable Transfection, Transfection

GSTK1 competes with DRP1 for binding to PGAM5. ( A-B ) Mass spectrometry (MS) analysis of GSTK1-associated proteins. Total cell extracts of HepG2 cells stably overexpressing GSTK1 was subjected to affinity purification with anti-GSTK1 antibody. The purified protein complex was resolved on SDS-PAGE and Coomassie brilliant blue staining, then the bands were excised and analyzed by mass spectrometry. ( C ) Immunoprecipitation and immunoblotting analysis of the GSTK1 and PGAM5 interaction in HepG2 cells overexpressing GSTK1 or stably transfected Flag-PGAM5. ( D ) Immunofluorescent staining of the GSTK1 and PGAM5 interaction in HepG2 and Hep3B cells (bar = 10 μm). ( E ) Immunoprecipitation and immunoblotting analysis of the PGAM5 and DRP1 interaction in HepG2 cells overexpressing GSTK1 or transiently transfected knockdown GSTK1. ( F ) The prediction of specific binding sites for the GSTK1 and PGAM5 interaction detected by PLIP software. ( G ) Immunoprecipitation and immunoblotting analysis of the GSTK1 and PGAM5 interaction in HepG2 cells transiently transfected point mutation plasmids. ( H ) Immunoblotting analysis of MFN1, MFN2, DRP1, p-DRP1, PGC1-α, P62, the LC3II: I ratio, TOMM20, GSTK1, and β-actin in HepG2 cells overexpressing GSTK1 and a TYR-18 point mutation. ( I-J ) Representative TEM images of HepG2 cells overexpressing GSTK1 and a TYR-18 point mutation (bar = 5–1 μm). ( K-L ) Representative TEM images of HCC-LM3 cells and GSTK1 knockdown and a TYR-18 point mutation (bar = 5–1 μm). n.s, no significance, * P < 0.05, ** P < 0.01

Journal: Journal of Experimental & Clinical Cancer Research : CR

Article Title: GSTK1 suppresses HCC aggravation via L-carnitine metabolism by PGAM5/DRP1 complex-mediated mitochondrial quality control

doi: 10.1186/s13046-025-03580-8

Figure Lengend Snippet: GSTK1 competes with DRP1 for binding to PGAM5. ( A-B ) Mass spectrometry (MS) analysis of GSTK1-associated proteins. Total cell extracts of HepG2 cells stably overexpressing GSTK1 was subjected to affinity purification with anti-GSTK1 antibody. The purified protein complex was resolved on SDS-PAGE and Coomassie brilliant blue staining, then the bands were excised and analyzed by mass spectrometry. ( C ) Immunoprecipitation and immunoblotting analysis of the GSTK1 and PGAM5 interaction in HepG2 cells overexpressing GSTK1 or stably transfected Flag-PGAM5. ( D ) Immunofluorescent staining of the GSTK1 and PGAM5 interaction in HepG2 and Hep3B cells (bar = 10 μm). ( E ) Immunoprecipitation and immunoblotting analysis of the PGAM5 and DRP1 interaction in HepG2 cells overexpressing GSTK1 or transiently transfected knockdown GSTK1. ( F ) The prediction of specific binding sites for the GSTK1 and PGAM5 interaction detected by PLIP software. ( G ) Immunoprecipitation and immunoblotting analysis of the GSTK1 and PGAM5 interaction in HepG2 cells transiently transfected point mutation plasmids. ( H ) Immunoblotting analysis of MFN1, MFN2, DRP1, p-DRP1, PGC1-α, P62, the LC3II: I ratio, TOMM20, GSTK1, and β-actin in HepG2 cells overexpressing GSTK1 and a TYR-18 point mutation. ( I-J ) Representative TEM images of HepG2 cells overexpressing GSTK1 and a TYR-18 point mutation (bar = 5–1 μm). ( K-L ) Representative TEM images of HCC-LM3 cells and GSTK1 knockdown and a TYR-18 point mutation (bar = 5–1 μm). n.s, no significance, * P < 0.05, ** P < 0.01

Techniques: Binding Assay, Mass Spectrometry, Stable Transfection, Affinity Purification, Purification, SDS Page, Staining, Immunoprecipitation, Western Blot, Transfection, Knockdown, Software, Mutagenesis

$Identification of multimeric oxidized forms of recoverin in the retina of albino rats and pigmented rabbits exposed to different doses of visual light illumination. Western blotting under non-reducing or reducing conditions of recoverin fractions extracted from the rat retinas illuminated in vivo for 14 h with metal halide lamp (2,500 lx, ‘exp’) (A) , and rabbit retinas illuminated in vivo for 3 h with halogen lamp following scheme 1 (2,200 lx, ‘exp S1’) or scheme 2 (30,000 lx, ‘exp S2’) (B) . The recoverin fractions obtained from the dark-adapted retinas were used as a control (‘contr’). ‘M,’ ‘M2,’ and ‘A’ denote monomeric, dimeric, and multimeric/aggregated forms of recoverin, respectively. Volumes of the loaded recoverin samples were chosen to ensure nearly equivalent bands of the monomeric protein. The numbers in left-hand columns indicate the molecular masses of protein markers in kDa. (C) The weight fractions of monomeric and dimeric forms of rabbit recoverin estimated from the Western blotting data from at least three independent in vivo experiments.$

Journal: Frontiers in Molecular Neuroscience

Article Title: Light-Induced Thiol Oxidation of Recoverin Affects Rhodopsin Desensitization

doi: 10.3389/fnmol.2018.00474

Figure Lengend Snippet: Identification of multimeric oxidized forms of recoverin in the retina of albino rats and pigmented rabbits exposed to different doses of visual light illumination. Western blotting under non-reducing or reducing conditions of recoverin fractions extracted from the rat retinas illuminated in vivo for 14 h with metal halide lamp (2,500 lx, ‘exp’) (A) , and rabbit retinas illuminated in vivo for 3 h with halogen lamp following scheme 1 (2,200 lx, ‘exp S1’) or scheme 2 (30,000 lx, ‘exp S2’) (B) . The recoverin fractions obtained from the dark-adapted retinas were used as a control (‘contr’). ‘M,’ ‘M2,’ and ‘A’ denote monomeric, dimeric, and multimeric/aggregated forms of recoverin, respectively. Volumes of the loaded recoverin samples were chosen to ensure nearly equivalent bands of the monomeric protein. The numbers in left-hand columns indicate the molecular masses of protein markers in kDa. (C) The weight fractions of monomeric and dimeric forms of rabbit recoverin estimated from the Western blotting data from at least three independent in vivo experiments.

Article Snippet: The resulting protein samples were adjusted to pH 6.2, concentrated and analyzed by non-reducing or reducing Western blotting using affinity-purified rabbit polyclonal anti-recoverin antibodies ( ) or mouse monoclonal anti-recoverin antibodies (Santa Cruz Biotechnology), for rat and rabbit retinal extracts, respectively.

Techniques: Western Blot, In Vivo, Control

Identification of monomeric oxidized forms of recoverin in the retina of pigmented rabbits exposed to different doses of visual light illumination. MALDI-TOF/TOF mass spectra of monomeric recoverin ([MH] + molecular ions of full-length proteins) extracted from the rabbit retinas illuminated in vivo for 3 h with halogen lamp following scheme 1 (2,200 lx) (A) or scheme 2 (30,000 lx) (B) .

Journal: Frontiers in Molecular Neuroscience

Article Title: Light-Induced Thiol Oxidation of Recoverin Affects Rhodopsin Desensitization

doi: 10.3389/fnmol.2018.00474

Figure Lengend Snippet: Identification of monomeric oxidized forms of recoverin in the retina of pigmented rabbits exposed to different doses of visual light illumination. MALDI-TOF/TOF mass spectra of monomeric recoverin ([MH] + molecular ions of full-length proteins) extracted from the rabbit retinas illuminated in vivo for 3 h with halogen lamp following scheme 1 (2,200 lx) (A) or scheme 2 (30,000 lx) (B) .

Techniques: In Vivo

The parameters of Ca 2+ -binding, thermal denaturation and membrane association of the recoverin variants.

Journal: Frontiers in Molecular Neuroscience

Article Title: Light-Induced Thiol Oxidation of Recoverin Affects Rhodopsin Desensitization

doi: 10.3389/fnmol.2018.00474

Figure Lengend Snippet: The parameters of Ca 2+ -binding, thermal denaturation and membrane association of the recoverin variants.

Techniques: Binding Assay, Membrane

Structural properties of recoverin forms. (A,B) Far-UV CD spectra of Ca 2+ -free (A) or Ca 2+ -loaded (B) RmRec (4 μM, solid curves), OmRec (4 μM, dotted curves) and dRec (2 μM, thick solid curves) at 20°C, pH 8.2. (C) Thermal dependencies of fluorescence spectrum maximum position for Ca 2+ -free (open symbols) and Ca 2+ -loaded (filled symbols) RmRec (14 μM, squares), OmRec (14 μM, circles) and dRec (7 μM, triangles) samples at pH 7.3. (D) The binding of bis-ANS (1 μM) to Ca 2+ -free (dashed curves) or Ca 2+ -loaded (solid curves) RmRec (6 μM, medium curves), C39D mutant (6 μM, thin curves) and dRec (3 μM, thick curves) monitored by fluorescence emission spectrum of the dye at 20°C, pH 7.3.

Journal: Frontiers in Molecular Neuroscience

Article Title: Light-Induced Thiol Oxidation of Recoverin Affects Rhodopsin Desensitization

doi: 10.3389/fnmol.2018.00474

Figure Lengend Snippet: Structural properties of recoverin forms. (A,B) Far-UV CD spectra of Ca 2+ -free (A) or Ca 2+ -loaded (B) RmRec (4 μM, solid curves), OmRec (4 μM, dotted curves) and dRec (2 μM, thick solid curves) at 20°C, pH 8.2. (C) Thermal dependencies of fluorescence spectrum maximum position for Ca 2+ -free (open symbols) and Ca 2+ -loaded (filled symbols) RmRec (14 μM, squares), OmRec (14 μM, circles) and dRec (7 μM, triangles) samples at pH 7.3. (D) The binding of bis-ANS (1 μM) to Ca 2+ -free (dashed curves) or Ca 2+ -loaded (solid curves) RmRec (6 μM, medium curves), C39D mutant (6 μM, thin curves) and dRec (3 μM, thick curves) monitored by fluorescence emission spectrum of the dye at 20°C, pH 7.3.

Techniques: Circular Dichroism, Fluorescence, Binding Assay, Mutagenesis

$The secondary structure fractions for the recoverin forms estimated from the far-UV CD data shown in Figures <xref ref-type=$ 6A,B using CDPro software package ( Sreerama et al., 2000 )." width="100%" height="100%">

Journal: Frontiers in Molecular Neuroscience

Article Title: Light-Induced Thiol Oxidation of Recoverin Affects Rhodopsin Desensitization

doi: 10.3389/fnmol.2018.00474

Figure Lengend Snippet: The secondary structure fractions for the recoverin forms estimated from the far-UV CD data shown in Figures 6A,B using CDPro software package ( Sreerama et al., 2000 ).

Techniques: Software

$Functional properties of the recoverin forms. (A) The binding of 30 μM RmRec (open circles) and 15 μM dRec (open squares) to photoreceptor membranes. Recoverin was mixed with urea-washed photoreceptor membranes in the presence of 0.11–500 μM [Ca 2+ ] free at 37°C, pH 8.0 and the membranes were separated by ultracentrifugation. The fractions of membrane-bound protein evaluated by SDS-PAGE were plotted versus [Ca 2+ ] free and the plots were fitted to the 4-parameter Hill equation. Solid and dashed curves represent best fits for RmRec and dRec, respectively. The inset: fractions of the Ca 2+ -free and Ca 2+ -saturated protein bound to the membranes. (B) Inhibition of GRK1 by RmRec or C39D mutant (40 μM), or dRec (20 μM). Rhodopsin phosphorylation by GRK1 in the presence of [γ - 32 P]ATP was monitored at high [Ca 2+ ] free (200 μM Ca 2+ , filled bars) or low [Ca 2+ ] free (0.01 μM, open bars) by phosphorimaging radioautography.$

Journal: Frontiers in Molecular Neuroscience

Article Title: Light-Induced Thiol Oxidation of Recoverin Affects Rhodopsin Desensitization

doi: 10.3389/fnmol.2018.00474

Figure Lengend Snippet: Functional properties of the recoverin forms. (A) The binding of 30 μM RmRec (open circles) and 15 μM dRec (open squares) to photoreceptor membranes. Recoverin was mixed with urea-washed photoreceptor membranes in the presence of 0.11–500 μM [Ca 2+ ] free at 37°C, pH 8.0 and the membranes were separated by ultracentrifugation. The fractions of membrane-bound protein evaluated by SDS-PAGE were plotted versus [Ca 2+ ] free and the plots were fitted to the 4-parameter Hill equation. Solid and dashed curves represent best fits for RmRec and dRec, respectively. The inset: fractions of the Ca 2+ -free and Ca 2+ -saturated protein bound to the membranes. (B) Inhibition of GRK1 by RmRec or C39D mutant (40 μM), or dRec (20 μM). Rhodopsin phosphorylation by GRK1 in the presence of [γ - 32 P]ATP was monitored at high [Ca 2+ ] free (200 μM Ca 2+ , filled bars) or low [Ca 2+ ] free (0.01 μM, open bars) by phosphorimaging radioautography.

Techniques: Functional Assay, Binding Assay, Membrane, SDS Page, Inhibition, Mutagenesis, Phospho-proteomics

The affinity of Ca 2+ -bound recoverin variants to N-terminal domain of GRK1 (N-GRK1) and its fragment corresponding to the residues M1-S25 (1-25GRK1), estimated using SPR spectroscopy according to the heterogeneous ligand model (1).

Journal: Frontiers in Molecular Neuroscience

Article Title: Light-Induced Thiol Oxidation of Recoverin Affects Rhodopsin Desensitization

doi: 10.3389/fnmol.2018.00474

Figure Lengend Snippet: The affinity of Ca 2+ -bound recoverin variants to N-terminal domain of GRK1 (N-GRK1) and its fragment corresponding to the residues M1-S25 (1-25GRK1), estimated using SPR spectroscopy according to the heterogeneous ligand model (1).

Techniques: Spectroscopy

Position of C39 in three-dimensional structure of recoverin bound to membrane and GRK1. (A) Topology of recoverin on membrane surface built based on NMR structures of myristoylated Ca 2+ -bound protein [PDB entry 1JSA ( ; )]. C39 (orange), calcium ions (yellow), myristoyl residue (green) and the basic residues (K5, K11, K37, R43, and K84) in close contact with the membrane are indicated. (B) The structure of recoverin complex with GRK1 [PDB entry 2I94 ]. N-terminal amphipathic helix of GRK1 (magenta), calcium ions (yellow) and C39 (orange) are indicated. The images were created using PyMol Molecular Graphics System v.1.4.1 (Schrödinger, LLC).

Journal: Frontiers in Molecular Neuroscience

Article Title: Light-Induced Thiol Oxidation of Recoverin Affects Rhodopsin Desensitization

doi: 10.3389/fnmol.2018.00474

Figure Lengend Snippet: Position of C39 in three-dimensional structure of recoverin bound to membrane and GRK1. (A) Topology of recoverin on membrane surface built based on NMR structures of myristoylated Ca 2+ -bound protein [PDB entry 1JSA ( ; )]. C39 (orange), calcium ions (yellow), myristoyl residue (green) and the basic residues (K5, K11, K37, R43, and K84) in close contact with the membrane are indicated. (B) The structure of recoverin complex with GRK1 [PDB entry 2I94 ]. N-terminal amphipathic helix of GRK1 (magenta), calcium ions (yellow) and C39 (orange) are indicated. The images were created using PyMol Molecular Graphics System v.1.4.1 (Schrödinger, LLC).

Techniques: Membrane, Residue

Hypothetical scheme describing potential roles of disulfide dimer and thiol-oxidized monomer of recoverin in the mechanisms of photoreceptor apoptosis induced by visual light. The designations are as follows: Arr, arrestin; dArr, disulfide dimer of arrestin; GRK1, G-protein coupled kinase-1; Gt, transducin; PDE6, rod cGMP-specific 3’,5’-cyclic phosphodiesterase; Rho, rhodopsin; p Rho, phosphorylated rhodopsin; OmRec, monomeric recoverin with C39 converted into sulfinic acid; dRec, disulfide dimer of recoverin; JNK3, c-Jun N-terminal kinase 3; c-Jun/c-Fos (AP-1), activator protein 1 – heterodimeric transcription factor; nNOS, neuronal nitric oxide synthase 1; GC, guanylate cyclase; MDM2, mouse double minute 2 homolog – E3 ubiquitin-protein ligase; UPR, unfolded protein response; CHOP, C/EBP homologous protein – pro-apoptotic transcription factor; PERK, protein kinase R (PKR)-like endoplasmic reticulum kinase – translation initiation factor 2-alpha kinase 3; p eLF2α, phosphorylated translation initiation factor 2α; ATF4, activating transcription factor 4; Bcl2, B-cell lymphoma 2 – apoptosis regulator protein. For details, refer to section “Discussion.”

Journal: Frontiers in Molecular Neuroscience

Article Title: Light-Induced Thiol Oxidation of Recoverin Affects Rhodopsin Desensitization

doi: 10.3389/fnmol.2018.00474

Figure Lengend Snippet: Hypothetical scheme describing potential roles of disulfide dimer and thiol-oxidized monomer of recoverin in the mechanisms of photoreceptor apoptosis induced by visual light. The designations are as follows: Arr, arrestin; dArr, disulfide dimer of arrestin; GRK1, G-protein coupled kinase-1; Gt, transducin; PDE6, rod cGMP-specific 3’,5’-cyclic phosphodiesterase; Rho, rhodopsin; p Rho, phosphorylated rhodopsin; OmRec, monomeric recoverin with C39 converted into sulfinic acid; dRec, disulfide dimer of recoverin; JNK3, c-Jun N-terminal kinase 3; c-Jun/c-Fos (AP-1), activator protein 1 – heterodimeric transcription factor; nNOS, neuronal nitric oxide synthase 1; GC, guanylate cyclase; MDM2, mouse double minute 2 homolog – E3 ubiquitin-protein ligase; UPR, unfolded protein response; CHOP, C/EBP homologous protein – pro-apoptotic transcription factor; PERK, protein kinase R (PKR)-like endoplasmic reticulum kinase – translation initiation factor 2-alpha kinase 3; p eLF2α, phosphorylated translation initiation factor 2α; ATF4, activating transcription factor 4; Bcl2, B-cell lymphoma 2 – apoptosis regulator protein. For details, refer to section “Discussion.”

Techniques: Ubiquitin Proteomics

affinity module of the insight ii software package Search Results

Image Search Results