acc-125 Search Results


sf 9 cells  (DSMZ)
93
DSMZ sf 9 cells
Sf 9 Cells, supplied by DSMZ, 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/product/acc-125/pmc09663877-347-0-13?v=DSMZ
Average 93 stars, based on 1 article reviews
sf 9 cells - by Bioz Stars, 2026-08
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channel auxiliary subunit γ8  (Alomone Labs)
92
Alomone Labs channel auxiliary subunit γ8
Fig. 1. Identification of differentially palmitoylated proteins after cFC. (A) Quantification of freezing behavior in fear-conditioned and control mice to assess the efficacy of the fear conditioning protocol. Data are means ± SEM from n = <t>8</t> control and 8 cFC mice. *P < 0.05 by unpaired Student’s t test. (B) Schematic representation of the acyl-RAC assay used to isolate palmitoylated proteins. (C) Schematic illustration of the experimental design: A memory retrieval test was done 1 hour after cFC, and hippocampi were immediately collected. Acyl-RAC assays were done on membrane-enriched samples to isolate palmitoylated proteins. Input, (+)HAM, and (−)HAM samples were run on LFQ LC-MS/MS to identify and quantify palmitoylated proteins. cFC, contextual fear conditioning; HAM, hydroxylamine; LC-MS/MS, liquid chroma- tography–tandem mass spectrometry. (D) Quantification of pairwise correlation values between all control replicates and all FC replicates. (E) Representative correlation of two control replicates (Pearson R = 0.70). (F) Representative correlation of two FC replicates (Pearson R = 0.90). Correlation of replicates was assessed with Pearson correlation of log-transformed LFQ values. Each dot corresponds to the intensity of the same peptide that was identified in the first (vertical axis) and second (horizontal axis) biological replicates.
Channel Auxiliary Subunit γ8, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/acc-125/pm36473050-247-11-16?v=Alomone+Labs
Average 92 stars, based on 1 article reviews
channel auxiliary subunit γ8 - by Bioz Stars, 2026-08
92/100 stars
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Image Search Results


Fig. 1. Identification of differentially palmitoylated proteins after cFC. (A) Quantification of freezing behavior in fear-conditioned and control mice to assess the efficacy of the fear conditioning protocol. Data are means ± SEM from n = 8 control and 8 cFC mice. *P < 0.05 by unpaired Student’s t test. (B) Schematic representation of the acyl-RAC assay used to isolate palmitoylated proteins. (C) Schematic illustration of the experimental design: A memory retrieval test was done 1 hour after cFC, and hippocampi were immediately collected. Acyl-RAC assays were done on membrane-enriched samples to isolate palmitoylated proteins. Input, (+)HAM, and (−)HAM samples were run on LFQ LC-MS/MS to identify and quantify palmitoylated proteins. cFC, contextual fear conditioning; HAM, hydroxylamine; LC-MS/MS, liquid chroma- tography–tandem mass spectrometry. (D) Quantification of pairwise correlation values between all control replicates and all FC replicates. (E) Representative correlation of two control replicates (Pearson R = 0.70). (F) Representative correlation of two FC replicates (Pearson R = 0.90). Correlation of replicates was assessed with Pearson correlation of log-transformed LFQ values. Each dot corresponds to the intensity of the same peptide that was identified in the first (vertical axis) and second (horizontal axis) biological replicates.

Journal: Science signaling

Article Title: Synaptic activity-dependent changes in the hippocampal palmitoylome.

doi: 10.1126/scisignal.add2519

Figure Lengend Snippet: Fig. 1. Identification of differentially palmitoylated proteins after cFC. (A) Quantification of freezing behavior in fear-conditioned and control mice to assess the efficacy of the fear conditioning protocol. Data are means ± SEM from n = 8 control and 8 cFC mice. *P < 0.05 by unpaired Student’s t test. (B) Schematic representation of the acyl-RAC assay used to isolate palmitoylated proteins. (C) Schematic illustration of the experimental design: A memory retrieval test was done 1 hour after cFC, and hippocampi were immediately collected. Acyl-RAC assays were done on membrane-enriched samples to isolate palmitoylated proteins. Input, (+)HAM, and (−)HAM samples were run on LFQ LC-MS/MS to identify and quantify palmitoylated proteins. cFC, contextual fear conditioning; HAM, hydroxylamine; LC-MS/MS, liquid chroma- tography–tandem mass spectrometry. (D) Quantification of pairwise correlation values between all control replicates and all FC replicates. (E) Representative correlation of two control replicates (Pearson R = 0.70). (F) Representative correlation of two FC replicates (Pearson R = 0.90). Correlation of replicates was assessed with Pearson correlation of log-transformed LFQ values. Each dot corresponds to the intensity of the same peptide that was identified in the first (vertical axis) and second (horizontal axis) biological replicates.

Article Snippet: Primary antibodies used in this study were as follows: calcium voltage-gated channel auxiliary subunit γ8 (1:500, Alomone Labs, ACC-125, RRID:AB_2756551), calnexin (1:500, Santa Cruz Biotechnology, sc-23954, RRID:AB_626783), calcium/calmodulin-dependent protein kinase IIa (CaMKIIa) (1:1000, Invitrogen, MA11048, RRID:AB_325403), CaMKv (1:500, Abcam, ab69564, RRID:AB_1267918), CRMP4 (1:500, Millipore, AB5454, RRID:AB_91876), guanine nucleotide–binding protein subunit α11 (1:1000, GeneTex, GTX118876, RRID:AB_11168804), guanine nucleotide–binding protein G(q) subunit α (1:1000, Abcam, ab75825, RRID:AB_1925009), HA (1:1000 for Western blotting, Cell Signaling Technology, #3724, RRID:AB_1549585; 1:1000 for immunocytochemistry, Sigma-Aldrich, H9658, RRID:AB_260092), paralemmin (1:1000, Acris-OriGene, TA335984), PRG-1 (1:1000 for Western blotting, Abcam, ab104104, RRID:AB_10710953), PSD-95 (1:1000 for Western blotting, Calbiochem, CP35, RRID:AB_2092542; 1:500 for immunocytochemistry, Abcam, ab2723, RRID:AB_303248), Sbf1 (1:1000, Abcam, ab181106), septin 8 (1:500, Abcam, ab154112), Slc32a1 (1:1000, Invitrogen, PA1-4701, RRID:AB_2301981), Smpd3 (1:500, LSBio, LS-C496905), synaptic vesicle protein 2A (1:500, Abcam, ab32942, RRID:AB_778192), syntaxin-1a (1:500, Abcam, ab41453, RRID:AB_956343), and VGLUT1 (1:1000, Abcam, ab77822, RRID:AB_2187677).

Techniques: Control, Membrane, Liquid Chromatography with Mass Spectroscopy, Mass Spectrometry, Transformation Assay

Fig. 2. Identification of 121 differentially palmitoylated proteins after cFC. (A and B) Quantification of proteins in the (+)HAM control (A) and (+)HAM cFC (B) samples relative to the respective (−)HAM samples. Graphs depict fold change (FC) in protein abundance (x axis) and the statistical significance of the enrichment in the (+)HAM compared with that in the (−)HAM (y axis) sample, determined by two-tailed t test. (C) Quantification of fold change in the abundance of palmitoylated proteins in cFC samples compared to control. Each dot represents an individual protein; pink denotes increased palmitoylation, and blue denotes decreased palmitoylation relative to control. Vertical lines mark the twofold increase and decrease thresholds, respectively; horizontal line marks the statistical significance threshold, determined by two- tailed t test. Data in (A) to (C) are representative of n = 8 control and 8 cFC mice.

Journal: Science signaling

Article Title: Synaptic activity-dependent changes in the hippocampal palmitoylome.

doi: 10.1126/scisignal.add2519

Figure Lengend Snippet: Fig. 2. Identification of 121 differentially palmitoylated proteins after cFC. (A and B) Quantification of proteins in the (+)HAM control (A) and (+)HAM cFC (B) samples relative to the respective (−)HAM samples. Graphs depict fold change (FC) in protein abundance (x axis) and the statistical significance of the enrichment in the (+)HAM compared with that in the (−)HAM (y axis) sample, determined by two-tailed t test. (C) Quantification of fold change in the abundance of palmitoylated proteins in cFC samples compared to control. Each dot represents an individual protein; pink denotes increased palmitoylation, and blue denotes decreased palmitoylation relative to control. Vertical lines mark the twofold increase and decrease thresholds, respectively; horizontal line marks the statistical significance threshold, determined by two- tailed t test. Data in (A) to (C) are representative of n = 8 control and 8 cFC mice.

Article Snippet: Primary antibodies used in this study were as follows: calcium voltage-gated channel auxiliary subunit γ8 (1:500, Alomone Labs, ACC-125, RRID:AB_2756551), calnexin (1:500, Santa Cruz Biotechnology, sc-23954, RRID:AB_626783), calcium/calmodulin-dependent protein kinase IIa (CaMKIIa) (1:1000, Invitrogen, MA11048, RRID:AB_325403), CaMKv (1:500, Abcam, ab69564, RRID:AB_1267918), CRMP4 (1:500, Millipore, AB5454, RRID:AB_91876), guanine nucleotide–binding protein subunit α11 (1:1000, GeneTex, GTX118876, RRID:AB_11168804), guanine nucleotide–binding protein G(q) subunit α (1:1000, Abcam, ab75825, RRID:AB_1925009), HA (1:1000 for Western blotting, Cell Signaling Technology, #3724, RRID:AB_1549585; 1:1000 for immunocytochemistry, Sigma-Aldrich, H9658, RRID:AB_260092), paralemmin (1:1000, Acris-OriGene, TA335984), PRG-1 (1:1000 for Western blotting, Abcam, ab104104, RRID:AB_10710953), PSD-95 (1:1000 for Western blotting, Calbiochem, CP35, RRID:AB_2092542; 1:500 for immunocytochemistry, Abcam, ab2723, RRID:AB_303248), Sbf1 (1:1000, Abcam, ab181106), septin 8 (1:500, Abcam, ab154112), Slc32a1 (1:1000, Invitrogen, PA1-4701, RRID:AB_2301981), Smpd3 (1:500, LSBio, LS-C496905), synaptic vesicle protein 2A (1:500, Abcam, ab32942, RRID:AB_778192), syntaxin-1a (1:500, Abcam, ab41453, RRID:AB_956343), and VGLUT1 (1:1000, Abcam, ab77822, RRID:AB_2187677).

Techniques: Control, Quantitative Proteomics, Two Tailed Test

Fig. 8. PRG-1 is differentially palmitoylated in response to cLTP. (A) Western blot and quantification of acyl-RAC assay performed on 14-DIV cultured hippocampal neurons. Lysates were collected after either mock cLTP or 5, 10, or 60 min after cLTP. Acyl-RAC Palm and Input fractions were immunoblotted for PRG-1. The input was reprobed by immunoblotting for β-actin as a loading control. Data for each cLTP time point are normalized to mock cLTP for that experiment. Data are means ± SEM from n = 4 blots from four independent cultures for 5 and 10 min after cLTP and n = 5 blots from five independent cultures for 1 hour after cLTP. *P < 0.05, ***P < 0.001 by one- way analysis of variance (ANOVA), Tukey’s post hoc test. (B) Western blot and quantification of APEGS assay performed on 14-DIV cultured hippocampal neurons 1 hour after cLTP stimulation. Hippocampal cultures were treated with either no mPEG and no HAM, mPEG and HAM, or mPEG with no HAM and immunoblotted for PRG-1. Data are means ± SEM from n = 4 blots from four independent cultures. (C) Western blot and quantification of acyl-RAC assay performed on 7-DIV cultured hippocampal neurons that were nucleofected at 0 DIV with human HA-PRG-1-WT or HA-PRG-1-C146-7S mutant constructs. Acyl-RAC Palm and Input fractions were immunoblotted for HA. The input was reprobed by immunoblotting for β-actin as a loading control. Data are means ± SEM from n = 3 blots from three independent cultures. *P < 0.05 by paired Student’s t test. (D) Western blot and quantification of HEK cells that were either untransfected or transfected with human HA-PRG-1-WT alone, control shRNA and HA-PRG-1-WT, or PRG-1 shRNA and HA-PRG-1-WT. Lysates were immunoblotted for HA and reprobed by immunoblotting for β-actin as a loading control. Data are means ± SEM from n = 4 blots from four independent cultures. **P < 0.01, ***P < 0.001, ****P < 0.0001 by one-way ANOVA, Tukey’s post hoc test. (E) Western blot and quantifi- cation of 7-DIV cultured hippocampal neurons that were nucleofected with control shRNA or PRG-1 shRNA at 0 DIV. Lysates were immunoblotted for PRG-1. Data for PRG- 1 shRNA bands are normalized to control shRNA for each molecular weight of PRG-1. Blots were reprobed by immunoblotting for β-actin antibody as a loading control. Data are means ± SEM from n = 3 blots from three independent cultures. *P < 0.05, **P < 0.01 by two-way ANOVA, Bonferroni’s post hoc test.

Journal: Science signaling

Article Title: Synaptic activity-dependent changes in the hippocampal palmitoylome.

doi: 10.1126/scisignal.add2519

Figure Lengend Snippet: Fig. 8. PRG-1 is differentially palmitoylated in response to cLTP. (A) Western blot and quantification of acyl-RAC assay performed on 14-DIV cultured hippocampal neurons. Lysates were collected after either mock cLTP or 5, 10, or 60 min after cLTP. Acyl-RAC Palm and Input fractions were immunoblotted for PRG-1. The input was reprobed by immunoblotting for β-actin as a loading control. Data for each cLTP time point are normalized to mock cLTP for that experiment. Data are means ± SEM from n = 4 blots from four independent cultures for 5 and 10 min after cLTP and n = 5 blots from five independent cultures for 1 hour after cLTP. *P < 0.05, ***P < 0.001 by one- way analysis of variance (ANOVA), Tukey’s post hoc test. (B) Western blot and quantification of APEGS assay performed on 14-DIV cultured hippocampal neurons 1 hour after cLTP stimulation. Hippocampal cultures were treated with either no mPEG and no HAM, mPEG and HAM, or mPEG with no HAM and immunoblotted for PRG-1. Data are means ± SEM from n = 4 blots from four independent cultures. (C) Western blot and quantification of acyl-RAC assay performed on 7-DIV cultured hippocampal neurons that were nucleofected at 0 DIV with human HA-PRG-1-WT or HA-PRG-1-C146-7S mutant constructs. Acyl-RAC Palm and Input fractions were immunoblotted for HA. The input was reprobed by immunoblotting for β-actin as a loading control. Data are means ± SEM from n = 3 blots from three independent cultures. *P < 0.05 by paired Student’s t test. (D) Western blot and quantification of HEK cells that were either untransfected or transfected with human HA-PRG-1-WT alone, control shRNA and HA-PRG-1-WT, or PRG-1 shRNA and HA-PRG-1-WT. Lysates were immunoblotted for HA and reprobed by immunoblotting for β-actin as a loading control. Data are means ± SEM from n = 4 blots from four independent cultures. **P < 0.01, ***P < 0.001, ****P < 0.0001 by one-way ANOVA, Tukey’s post hoc test. (E) Western blot and quantifi- cation of 7-DIV cultured hippocampal neurons that were nucleofected with control shRNA or PRG-1 shRNA at 0 DIV. Lysates were immunoblotted for PRG-1. Data for PRG- 1 shRNA bands are normalized to control shRNA for each molecular weight of PRG-1. Blots were reprobed by immunoblotting for β-actin antibody as a loading control. Data are means ± SEM from n = 3 blots from three independent cultures. *P < 0.05, **P < 0.01 by two-way ANOVA, Bonferroni’s post hoc test.

Article Snippet: Primary antibodies used in this study were as follows: calcium voltage-gated channel auxiliary subunit γ8 (1:500, Alomone Labs, ACC-125, RRID:AB_2756551), calnexin (1:500, Santa Cruz Biotechnology, sc-23954, RRID:AB_626783), calcium/calmodulin-dependent protein kinase IIa (CaMKIIa) (1:1000, Invitrogen, MA11048, RRID:AB_325403), CaMKv (1:500, Abcam, ab69564, RRID:AB_1267918), CRMP4 (1:500, Millipore, AB5454, RRID:AB_91876), guanine nucleotide–binding protein subunit α11 (1:1000, GeneTex, GTX118876, RRID:AB_11168804), guanine nucleotide–binding protein G(q) subunit α (1:1000, Abcam, ab75825, RRID:AB_1925009), HA (1:1000 for Western blotting, Cell Signaling Technology, #3724, RRID:AB_1549585; 1:1000 for immunocytochemistry, Sigma-Aldrich, H9658, RRID:AB_260092), paralemmin (1:1000, Acris-OriGene, TA335984), PRG-1 (1:1000 for Western blotting, Abcam, ab104104, RRID:AB_10710953), PSD-95 (1:1000 for Western blotting, Calbiochem, CP35, RRID:AB_2092542; 1:500 for immunocytochemistry, Abcam, ab2723, RRID:AB_303248), Sbf1 (1:1000, Abcam, ab181106), septin 8 (1:500, Abcam, ab154112), Slc32a1 (1:1000, Invitrogen, PA1-4701, RRID:AB_2301981), Smpd3 (1:500, LSBio, LS-C496905), synaptic vesicle protein 2A (1:500, Abcam, ab32942, RRID:AB_778192), syntaxin-1a (1:500, Abcam, ab41453, RRID:AB_956343), and VGLUT1 (1:1000, Abcam, ab77822, RRID:AB_2187677).

Techniques: Western Blot, Cell Culture, Control, Mutagenesis, Construct, Transfection, shRNA, Molecular Weight