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Proteintech rabbit igg
Rabbit Igg, supplied by Proteintech, used in various techniques. Bioz Stars score: 95/100, based on 150 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/rabbit+anti+optn+antibody/OPTN+Antibody/pmc12786331-9-2-8
Average 95 stars, based on 150 article reviews

rabbit igg - by Bioz Stars, 2026-11

95/100 stars

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Western Blot:

Article Title: Autophagy Receptor-Inspired Antibody-Fusion Proteins for Targeted Intracellular Degradation.
Article Snippet: .. List of additional primary antibodies for western blots (diluted in TBS blocking buffer containing 0.1% Tween-20): Mouse anti-BNIP3 antibody, Proteintech, Cat# 68091-1-Ig, 1:500 diluted; Mouse anti-NIX antibody, Proteintech, Cat# 68118-1-Ig, 1:500 diluted; Rabbit anti-TAX1BP1 antibody, Proteintech, Cat# 14424-1-AP, 1:1000 diluted; Rabbit anti-BCL2L13 antibody, Proteintech, Cat# 16612-1-AP, 1:1000 diluted; Rabbit anti-FKBP8 antibody, Proteintech, Cat# 11173-1-AP, 1:1000 diluted; Rabbit anti-OPTN antibody, Proteintech, Cat# 10837-1-AP, 1:1000 diluted; Rabbit anti-NDP52 antibody, Proteintech, Cat# 12229-1-AP, 1:1000 diluted; Rabbit anti-NBR1 antibody, Proteintech, Cat# 16004-1-AP, 1:1000 diluted; Rabbit anti-PINK1 antibody, Proteintech, Cat# 23274-1-AP, 1:1000 diluted; Mouse anti-TOMM40 antibody, Proteintech, Cat# 66658-1-Ig, 1:1000 diluted; Mouse anti-MFN2 antibody, Proteintech, Cat# 67487-1-Ig, 1:1000 diluted; Rabbit anti-ULK1 antibody, CST, Cat# 8054, 1:1000 diluted. ..

Blocking Assay:

other:

Article Title: CDKL5 regulates p62-mediated selective autophagy and host antiviral defense
Article Snippet: The following antibodies were used: rabbit anti-LC3B (Novus Biologicals, NB100-2220), guinea pig anti-p62/SQSTM1 (C-terminus) (Progen, GP62-C), mouse anti-SQSTM1 (Abnova, H00008878-M01), rabbit anti-phospho-SQSTM1/p62 (Thr269/Ser272) (Cell Signaling Technology, 13121), rabbit anti-phospho-SQSTM1/p62 (Ser403) (Cell Signaling Technology, 39786), mouse anti-actin antibody (C4) HRP (Santa Cruz Biotechnology (SCBT), sc-47778 HRP), mouse anti-CDKL5 (D-12) antibody (SCBT, sc-376314), rabbit anti-ATG7 polyclonal antibody (Sigma-Aldrich A2856), rabbit anti-TBK1/NAK antibody (Cell Signaling Technology, 3013), rabbit anti SINV capsid antibody (Gift from Diane Griffin) , rabbit anti-HA tag (C29F4) antibody (Cell Signaling Technology, 3724), mouse anti-NBRI antibody, clone 6B11 (Abnova, H00004077-M01), rabbit anti-NDP52 antibody (Cell Signaling Technology, 60732S), rabbit anti-OPTN antibody (Proteintech, 10837-1-AP), rabbit anti-TAX1BP1 antibody (4H2L18) (Thermo Fisher, 702840), mouse anti-Flag M2 antibody (Sigma, F1804), donkey anti-rabbit IgG HRP-conjugate species-adsorbed (Millipore Sigma, AP182P), goat anti-mouse IgG (H+L) HRP (Millipore Sigma, AP308P), donkey anti-mouse IgG (H+L) highly cross-adsorbed secondary antibody Alexa Fluor 488 (Thermo Fisher Scientific, A21202), donkey anti-rabbit IgG (H+L) highly cross-adsorbed secondary antibody Alexa Fluor 488 (Thermo Fisher Scientific, A-21206), and donkey anti-rabbit IgG (H+L) highly cross-adsorbed secondary antibody Alexa Fluor 594 (Thermo Fisher Scientific, A21207).

Article Title: Oligomerization of Optineurin and Its Oxidative Stress- or E50K Mutation-Driven Covalent Cross-Linking: Possible Relationship with Glaucoma Pathology
Article Snippet: The antibodies used in this study included rabbit anti-OPTN antibody (Cat. No. 10837-1-AP; ProteinTech Group, Inc., Chicago, IL, USA), mouse anti-FLAG M2 monoclonal antibody (F3165; Sigma-Aldrich), rabbit anti-GFP antibody (MBL International Corporation, Woburn, MA, USA), monoclonal anti-α-tubulin antibody (T8203; Sigma-Aldrich), goat anti-mouse IgG/HRP (P0447; DAKO, Tokyo, Japan), goat anti-rabbit IgG/HRP (P0448; DAKO), and rabbit anti-goat IgG/HRP (P0449; DAKO), and AlexaFluor488-conjugated donkey anti-mouse IgG (A21202; Invitrogen, Carlsbad, CA, USA).

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Characterization of Rab1 binding to the FHF complex and CALCOCO1. (A) Coomassie gel showing an in vitro–binding assay using beads coated with GST-Rab1A and purified FHF complex containing FHIP2A. Both GTP- and GDP-locked Rab1A proteins were used as indicated. (B) Representative Coomassie blue–stained gel showing expression of either WT or Rab1-binding mutant GFP-CALCOCO1. Proteins were purified from the same amount of starting material, and equal protein amounts were loaded on the gel. (C) GUV-binding assay using GTP- or GDP-locked Rab1A bound to GUVs before applying GFP-CALCOCO1 WT or Rab1-binding mutant. Each large (colored) datapoint in the graph depicts the average mean fluorescence intensity of GFP-CALCOCO1 WT or Rab1-binding mutant on a selection of GUV membrane and represents an independent experiment ( n = 3), with smaller gray datapoints representing all the technical replicates (AU, arbitrary units). The mean ± SD is indicated. ***P < 0.001 (one-way ANOVA with Tukey’s multiple comparisons test). (D) Sulfo-NHS-diazarine (SDA) intra-protein and dimer cross-links (purple and orange lines) mapped onto the AlphaFold 3 predicted structure of the OPTN homodimer. Intra-protein cross-links mapped onto the structure are pictured as a green dashed line; dimer cross-links are pictured as a cyan dashed line. (E) Representative Coomassie blue–stained gel showing expression of either WT or Rab1-binding mutant GFP-OPTN. Proteins were purified from the same amount of starting material, and equal protein amounts were loaded on the gel. Source data are available for this figure: .

Journal: The Journal of Cell Biology

Article Title: A Rab1 interactome illuminates a dual role in autophagy and membrane trafficking

doi: 10.1083/jcb.202507084

Figure Lengend Snippet: Characterization of Rab1 binding to the FHF complex and CALCOCO1. (A) Coomassie gel showing an in vitro–binding assay using beads coated with GST-Rab1A and purified FHF complex containing FHIP2A. Both GTP- and GDP-locked Rab1A proteins were used as indicated. (B) Representative Coomassie blue–stained gel showing expression of either WT or Rab1-binding mutant GFP-CALCOCO1. Proteins were purified from the same amount of starting material, and equal protein amounts were loaded on the gel. (C) GUV-binding assay using GTP- or GDP-locked Rab1A bound to GUVs before applying GFP-CALCOCO1 WT or Rab1-binding mutant. Each large (colored) datapoint in the graph depicts the average mean fluorescence intensity of GFP-CALCOCO1 WT or Rab1-binding mutant on a selection of GUV membrane and represents an independent experiment ( n = 3), with smaller gray datapoints representing all the technical replicates (AU, arbitrary units). The mean ± SD is indicated. ***P < 0.001 (one-way ANOVA with Tukey’s multiple comparisons test). (D) Sulfo-NHS-diazarine (SDA) intra-protein and dimer cross-links (purple and orange lines) mapped onto the AlphaFold 3 predicted structure of the OPTN homodimer. Intra-protein cross-links mapped onto the structure are pictured as a green dashed line; dimer cross-links are pictured as a cyan dashed line. (E) Representative Coomassie blue–stained gel showing expression of either WT or Rab1-binding mutant GFP-OPTN. Proteins were purified from the same amount of starting material, and equal protein amounts were loaded on the gel. Source data are available for this figure: .

Article Snippet: Antibodies used in this study were RABEP1 (610676; BD Transduction Laboratories, RRID: AB_398003), PPP1R37 (HPA041500; Atlas Antibodies, RRID: AB_10795122), CLEC16A (26257-1-AP; Proteintech, RRID: AB_2880449), Rab1A (13075; Cell Signaling Technologies, RRID: AB_2665537), HA (3F10; Roche, RRID: AB_2314622), TOM20 (ab56783; Abcam, RRID: AB_945896), Flag M2 (F1804; Sigma-Aldrich, RRID), CALCOCO1 (HPA038313; Atlas Antibodies, RRID: AB_10675794), GAPDH (60004-1; Proteintech, RRID: AB_2107436), OPTN (70928; Cell Signaling Technologies, RRID: AB_3073769), and α-tubulin (YL1/2, RRID: AB_305328).

Techniques: Binding Assay, In Vitro, Purification, Staining, Expressing, Mutagenesis, Fluorescence, Selection, Membrane

Rab1A-GTP binds directly to CALCOCO1 and OPTN. (A and B) Coomassie gels showing in vitro binding to GST-Rab1A–coated beads of either purified GFP-CALCOCO1 (A) or GFP-OPTN (B), with GFP as a negative control. Rab1A was in GTP- or GDP-locked forms as indicated. (C and D) GUV-binding assay using GTP- or GDP-locked Rab1A on the GUV with applied GFP-CALCOCO1 (C) or GFP-OPTN (D). Each large datapoint in the graph depicts the average mean fluorescence intensity of GFP-CALCOCO1 or GFP-OPTN on a selection of GUV membrane and represents an independent experiment ( n = 3), with smaller gray datapoints representing all the technical replicates (AU, arbitrary units). The mean ± SD is indicated. **P < 0.01 (unpaired t test). Source data are available for this figure: .

Journal: The Journal of Cell Biology

Article Title: A Rab1 interactome illuminates a dual role in autophagy and membrane trafficking

doi: 10.1083/jcb.202507084

Figure Lengend Snippet: Rab1A-GTP binds directly to CALCOCO1 and OPTN. (A and B) Coomassie gels showing in vitro binding to GST-Rab1A–coated beads of either purified GFP-CALCOCO1 (A) or GFP-OPTN (B), with GFP as a negative control. Rab1A was in GTP- or GDP-locked forms as indicated. (C and D) GUV-binding assay using GTP- or GDP-locked Rab1A on the GUV with applied GFP-CALCOCO1 (C) or GFP-OPTN (D). Each large datapoint in the graph depicts the average mean fluorescence intensity of GFP-CALCOCO1 or GFP-OPTN on a selection of GUV membrane and represents an independent experiment ( n = 3), with smaller gray datapoints representing all the technical replicates (AU, arbitrary units). The mean ± SD is indicated. **P < 0.01 (unpaired t test). Source data are available for this figure: .

Techniques: In Vitro, Binding Assay, Purification, Negative Control, Fluorescence, Selection, Membrane

Molecular characterization of the Rab1A-binding site on CALCOCO1 and OPTN. (A) Structure of the Rab1A:GTP:Mg 2+ :CALCOCO1 complex formed by two copies of CALCOCO1 and one copy of Rab1A as predicted by AlphaFold 3, with accompanying PAE plot. (B) Sulfo-NHS-diazirine (SDA) interprotein cross-links (green dashed lines) mapped onto the predicted structure of the Rab1A–CALCOCO1 complex. (C) The contact interface between Rab1A and the CALCOCO1 dimer, showing ChimeraX calculated contact residues of CALCOCO1 mediating the binding interface (red labels). (D) Structure of the Rab1A:GTP:Mg 2+ :OPTN complex formed by two copies of OPTN and one copy of Rab1A as predicted by AlphaFold 3, with accompanying PAE plot. (E) SDA interprotein cross-links (green dashed lines) mapped onto the predicted structure of the Rab1A–OPTN complex. (F) Magnified image of the contact interface between Rab1A and the OPTN dimer, showing ChimeraX calculated contact residues of OPTN mediating the binding interface (orange labels).

Journal: The Journal of Cell Biology

Article Title: A Rab1 interactome illuminates a dual role in autophagy and membrane trafficking

doi: 10.1083/jcb.202507084

Figure Lengend Snippet: Molecular characterization of the Rab1A-binding site on CALCOCO1 and OPTN. (A) Structure of the Rab1A:GTP:Mg 2+ :CALCOCO1 complex formed by two copies of CALCOCO1 and one copy of Rab1A as predicted by AlphaFold 3, with accompanying PAE plot. (B) Sulfo-NHS-diazirine (SDA) interprotein cross-links (green dashed lines) mapped onto the predicted structure of the Rab1A–CALCOCO1 complex. (C) The contact interface between Rab1A and the CALCOCO1 dimer, showing ChimeraX calculated contact residues of CALCOCO1 mediating the binding interface (red labels). (D) Structure of the Rab1A:GTP:Mg 2+ :OPTN complex formed by two copies of OPTN and one copy of Rab1A as predicted by AlphaFold 3, with accompanying PAE plot. (E) SDA interprotein cross-links (green dashed lines) mapped onto the predicted structure of the Rab1A–OPTN complex. (F) Magnified image of the contact interface between Rab1A and the OPTN dimer, showing ChimeraX calculated contact residues of OPTN mediating the binding interface (orange labels).

Techniques: Binding Assay

Mutation of the Rab1-binding site in OPTN does not affect its dimerization or binding to LC3 or ubiquitin. (A) Micrographs of beads coated with GST-4×ubiquitin (GST-4xUb) and incubated with either 1 μM GFP-OPTN (WT) or versions with mutations in the Rab1 or ubiquitin-binding sites. Each large datapoint in the bar graph depicts the average mean fluorescence intensity on a selection of beads and represents an independent experiment ( n = 3), with smaller gray datapoints representing all the technical replicates (AU, arbitrary units). The mean ± SD is indicated. ***P < 0.001 (one-way ANOVA with Tukey’s multiple comparisons test). (B) Micrographs of beads coated with GST-LC3B and incubated with either 1 μM GFP-OPTN (WT) or versions with mutations in the Rab1 or LC3 (LIR)-binding sites. Each large datapoint in the bar graph depicts the average mean fluorescence intensity on a selection of beads and represents an independent experiment ( n = 3), with smaller gray datapoints representing all the technical replicates (AU, arbitrary units). The mean ± SD is indicated. ***P < 0.001 (one-way ANOVA with Tukey’s multiple comparisons test). (C) Immunoblot of cell lysates of pentaKO HeLa cells stably expressing WT OPTN or the OPTN Rab1-binding mutant (representative of three repeats). Lysates were incubated with increasing concentrations of the cross-linker bis(sulfosuccinimidyl)suberate (BS3) at RT and quenched at 50 mM Tris-HCl prior to SDS-PAGE and blotting. With cross-linker, OPTN dimers are readily detected. GAPDH is a loading control and a negative control as it does not readily dimerize. Source data are available for this figure: .

Journal: The Journal of Cell Biology

Article Title: A Rab1 interactome illuminates a dual role in autophagy and membrane trafficking

doi: 10.1083/jcb.202507084

Figure Lengend Snippet: Mutation of the Rab1-binding site in OPTN does not affect its dimerization or binding to LC3 or ubiquitin. (A) Micrographs of beads coated with GST-4×ubiquitin (GST-4xUb) and incubated with either 1 μM GFP-OPTN (WT) or versions with mutations in the Rab1 or ubiquitin-binding sites. Each large datapoint in the bar graph depicts the average mean fluorescence intensity on a selection of beads and represents an independent experiment ( n = 3), with smaller gray datapoints representing all the technical replicates (AU, arbitrary units). The mean ± SD is indicated. ***P < 0.001 (one-way ANOVA with Tukey’s multiple comparisons test). (B) Micrographs of beads coated with GST-LC3B and incubated with either 1 μM GFP-OPTN (WT) or versions with mutations in the Rab1 or LC3 (LIR)-binding sites. Each large datapoint in the bar graph depicts the average mean fluorescence intensity on a selection of beads and represents an independent experiment ( n = 3), with smaller gray datapoints representing all the technical replicates (AU, arbitrary units). The mean ± SD is indicated. ***P < 0.001 (one-way ANOVA with Tukey’s multiple comparisons test). (C) Immunoblot of cell lysates of pentaKO HeLa cells stably expressing WT OPTN or the OPTN Rab1-binding mutant (representative of three repeats). Lysates were incubated with increasing concentrations of the cross-linker bis(sulfosuccinimidyl)suberate (BS3) at RT and quenched at 50 mM Tris-HCl prior to SDS-PAGE and blotting. With cross-linker, OPTN dimers are readily detected. GAPDH is a loading control and a negative control as it does not readily dimerize. Source data are available for this figure: .

Techniques: Mutagenesis, Binding Assay, Ubiquitin Proteomics, Incubation, Fluorescence, Selection, Western Blot, Stable Transfection, Expressing, SDS Page, Control, Negative Control

The Rab1A – OPTN interaction is required for mitophagy. (A) GUV-binding assay using GTP- or GDP-locked Rab1A bound to GUVs before applying GFP-OPTN WT or Rab1-binding mutant. Each large datapoint in the graph depicts the average mean fluorescence intensity of GFP-OPTN WT or Rab1-binding mutant on a selection of GUV membrane and represents an independent experiment ( n = 3), with smaller gray datapoints representing all the technical replicates (AU, arbitrary units). The mean ± SD is indicated. ***P < 0.001 (one-way ANOVA with Tukey’s multiple comparisons test). (B) Representative immunoblot of Rab1 interactors following MitoID in HEK293A cells where Rab1A MitoID constructs (detected using anti HA) and 3xFlag-OPTN proteins (detected using anti Flag) were transiently expressed. Endogenous CALCOCO1 was used as a positive control. Each datapoint in the graph represents the normalized ratio between the OPTN and MitoID construct immunoblot intensities and depicts an independent experiment ( n = 3). The mean ± SD is indicated. ****P < 0.0001; (one-way ANOVA with Dunnett’s multiple comparisons test). (C) Schematic of the overall structure of OPTN, with different binding regions annotated (TBK1, TBK1-binding domain; Rab1, the Rab1-binding domain; LIR, LC3 interacting-region; UBAN, ubiquitin-binding domain in ABIN proteins and NEMO; ZF: zinc finger domain). The predicted coiled-coil regions of OPTN are also illustrated as predicted by MARCOIL . (D) Representative immunoblot and in-gel fluorescence analysis of cell lysates of pentaKO HeLa cells stably expressing pSu9-HaloTag-mGFP and Parkin and either mock transfected (/) or expressing OPTN WT, or the mutant constructs OPTN Rab1, OPTN Ub (unable to bind ubiquitin), or OPTN LIR (unable to bind ATG8/LC3 family proteins). To assay mitophagy, cells were pulse-labelled with 100 nM TMR HaloTag ligand and incubated in medium containing 1 μM oligomycin and 5 μM antimycin for 24 h to induce mitophagy (O + A). Each datapoint in the bar graph is an independent experiment representing the normalized ratio between the free HaloTag and the combined pSu9-HaloTag-mGFP + free HaloTag fluorescence intensities ( n = 3). The mean ± SD is indicated. ****P < 0.001 (one-way ANOVA with Tukey’s multiple comparisons test). Source data are available for this figure: .

Journal: The Journal of Cell Biology

Article Title: A Rab1 interactome illuminates a dual role in autophagy and membrane trafficking

doi: 10.1083/jcb.202507084

Figure Lengend Snippet: The Rab1A – OPTN interaction is required for mitophagy. (A) GUV-binding assay using GTP- or GDP-locked Rab1A bound to GUVs before applying GFP-OPTN WT or Rab1-binding mutant. Each large datapoint in the graph depicts the average mean fluorescence intensity of GFP-OPTN WT or Rab1-binding mutant on a selection of GUV membrane and represents an independent experiment ( n = 3), with smaller gray datapoints representing all the technical replicates (AU, arbitrary units). The mean ± SD is indicated. ***P < 0.001 (one-way ANOVA with Tukey’s multiple comparisons test). (B) Representative immunoblot of Rab1 interactors following MitoID in HEK293A cells where Rab1A MitoID constructs (detected using anti HA) and 3xFlag-OPTN proteins (detected using anti Flag) were transiently expressed. Endogenous CALCOCO1 was used as a positive control. Each datapoint in the graph represents the normalized ratio between the OPTN and MitoID construct immunoblot intensities and depicts an independent experiment ( n = 3). The mean ± SD is indicated. ****P < 0.0001; (one-way ANOVA with Dunnett’s multiple comparisons test). (C) Schematic of the overall structure of OPTN, with different binding regions annotated (TBK1, TBK1-binding domain; Rab1, the Rab1-binding domain; LIR, LC3 interacting-region; UBAN, ubiquitin-binding domain in ABIN proteins and NEMO; ZF: zinc finger domain). The predicted coiled-coil regions of OPTN are also illustrated as predicted by MARCOIL . (D) Representative immunoblot and in-gel fluorescence analysis of cell lysates of pentaKO HeLa cells stably expressing pSu9-HaloTag-mGFP and Parkin and either mock transfected (/) or expressing OPTN WT, or the mutant constructs OPTN Rab1, OPTN Ub (unable to bind ubiquitin), or OPTN LIR (unable to bind ATG8/LC3 family proteins). To assay mitophagy, cells were pulse-labelled with 100 nM TMR HaloTag ligand and incubated in medium containing 1 μM oligomycin and 5 μM antimycin for 24 h to induce mitophagy (O + A). Each datapoint in the bar graph is an independent experiment representing the normalized ratio between the free HaloTag and the combined pSu9-HaloTag-mGFP + free HaloTag fluorescence intensities ( n = 3). The mean ± SD is indicated. ****P < 0.001 (one-way ANOVA with Tukey’s multiple comparisons test). Source data are available for this figure: .

Techniques: Binding Assay, Mutagenesis, Fluorescence, Selection, Membrane, Western Blot, Construct, Positive Control, Ubiquitin Proteomics, Stable Transfection, Expressing, Transfection, Incubation

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