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resource source identifier antibodies rabbit anti trpv1 alomone labs  (Alomone Labs)


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    Alomone Labs resource source identifier antibodies rabbit anti trpv1 alomone labs
    Resource Source Identifier Antibodies Rabbit Anti Trpv1 Alomone Labs, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 96/100, based on 218 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/trpv1+antibody/pm42024502-182-2-8?v=Alomone+Labs
    Average 96 stars, based on 218 article reviews
    resource source identifier antibodies rabbit anti trpv1 alomone labs - by Bioz Stars, 2026-07
    96/100 stars

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    ( A ) Bulk cortex TaqMan qPCR showing mean Ct values for Trpa1 and <t>Trpv1</t> in adult mouse cortex. Both transcripts are detected only at high Ct values. Red dashed line indicates Gapdh Ct. ( B ) TaqMan qPCR of FACS-sorted cortical cell populations showing mean Ct values by fraction: neurons (blue), astrocytes (orange), and NeuN⁺/ACSA2⁺ double-positive cells (grey). Dashed lines indicate fraction-specific Gapdh Ct. “‡” indicate no detectable amplification reactions. Trpv1 is neuron-only at high Ct; Trpa1 is rare/borderline. ( C, D ) Subcellular fractionation and immunoblotting for TRPA1 and TRPV1, respectively. Cortex lysates (n = 3) were separated into supernatant (S) and membrane pellet (P) fractions; Ladder (L). Faint immunoreactive bands near the expected molecular weight (∼130–140 and ∼95 kDa, respectively) are preferentially enriched in pellet fractions. GAPDH (∼37 kDa) was used as a loading control. Kidney, DRG, and testes processed in parallel serve as positive control tissues. Note: Lysates and controls were processed in the same experiment and run on the same gels/blots. ( E, F ) Immunoprecipitation (IP) from cortex (C) and DRG (D) lysates followed by SDS–PAGE/Western blotting and LC–MS/MS. As shown in Supplementary Fig. 12f, no TRPA1 peptides were detected, and only extremely low-intensity TRPV1 protein-group signals were observed without replicate consistency.
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    ( A ) Bulk cortex TaqMan qPCR showing mean Ct values for Trpa1 and <t>Trpv1</t> in adult mouse cortex. Both transcripts are detected only at high Ct values. Red dashed line indicates Gapdh Ct. ( B ) TaqMan qPCR of FACS-sorted cortical cell populations showing mean Ct values by fraction: neurons (blue), astrocytes (orange), and NeuN⁺/ACSA2⁺ double-positive cells (grey). Dashed lines indicate fraction-specific Gapdh Ct. “‡” indicate no detectable amplification reactions. Trpv1 is neuron-only at high Ct; Trpa1 is rare/borderline. ( C, D ) Subcellular fractionation and immunoblotting for TRPA1 and TRPV1, respectively. Cortex lysates (n = 3) were separated into supernatant (S) and membrane pellet (P) fractions; Ladder (L). Faint immunoreactive bands near the expected molecular weight (∼130–140 and ∼95 kDa, respectively) are preferentially enriched in pellet fractions. GAPDH (∼37 kDa) was used as a loading control. Kidney, DRG, and testes processed in parallel serve as positive control tissues. Note: Lysates and controls were processed in the same experiment and run on the same gels/blots. ( E, F ) Immunoprecipitation (IP) from cortex (C) and DRG (D) lysates followed by SDS–PAGE/Western blotting and LC–MS/MS. As shown in Supplementary Fig. 12f, no TRPA1 peptides were detected, and only extremely low-intensity TRPV1 protein-group signals were observed without replicate consistency.
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    acc  (Alomone Labs)
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    ( A ) Bulk cortex TaqMan qPCR showing mean Ct values for Trpa1 and <t>Trpv1</t> in adult mouse cortex. Both transcripts are detected only at high Ct values. Red dashed line indicates Gapdh Ct. ( B ) TaqMan qPCR of FACS-sorted cortical cell populations showing mean Ct values by fraction: neurons (blue), astrocytes (orange), and NeuN⁺/ACSA2⁺ double-positive cells (grey). Dashed lines indicate fraction-specific Gapdh Ct. “‡” indicate no detectable amplification reactions. Trpv1 is neuron-only at high Ct; Trpa1 is rare/borderline. ( C, D ) Subcellular fractionation and immunoblotting for TRPA1 and TRPV1, respectively. Cortex lysates (n = 3) were separated into supernatant (S) and membrane pellet (P) fractions; Ladder (L). Faint immunoreactive bands near the expected molecular weight (∼130–140 and ∼95 kDa, respectively) are preferentially enriched in pellet fractions. GAPDH (∼37 kDa) was used as a loading control. Kidney, DRG, and testes processed in parallel serve as positive control tissues. Note: Lysates and controls were processed in the same experiment and run on the same gels/blots. ( E, F ) Immunoprecipitation (IP) from cortex (C) and DRG (D) lysates followed by SDS–PAGE/Western blotting and LC–MS/MS. As shown in Supplementary Fig. 12f, no TRPA1 peptides were detected, and only extremely low-intensity TRPV1 protein-group signals were observed without replicate consistency.
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    ( A ) Bulk cortex TaqMan qPCR showing mean Ct values for Trpa1 and Trpv1 in adult mouse cortex. Both transcripts are detected only at high Ct values. Red dashed line indicates Gapdh Ct. ( B ) TaqMan qPCR of FACS-sorted cortical cell populations showing mean Ct values by fraction: neurons (blue), astrocytes (orange), and NeuN⁺/ACSA2⁺ double-positive cells (grey). Dashed lines indicate fraction-specific Gapdh Ct. “‡” indicate no detectable amplification reactions. Trpv1 is neuron-only at high Ct; Trpa1 is rare/borderline. ( C, D ) Subcellular fractionation and immunoblotting for TRPA1 and TRPV1, respectively. Cortex lysates (n = 3) were separated into supernatant (S) and membrane pellet (P) fractions; Ladder (L). Faint immunoreactive bands near the expected molecular weight (∼130–140 and ∼95 kDa, respectively) are preferentially enriched in pellet fractions. GAPDH (∼37 kDa) was used as a loading control. Kidney, DRG, and testes processed in parallel serve as positive control tissues. Note: Lysates and controls were processed in the same experiment and run on the same gels/blots. ( E, F ) Immunoprecipitation (IP) from cortex (C) and DRG (D) lysates followed by SDS–PAGE/Western blotting and LC–MS/MS. As shown in Supplementary Fig. 12f, no TRPA1 peptides were detected, and only extremely low-intensity TRPV1 protein-group signals were observed without replicate consistency.

    Journal: bioRxiv

    Article Title: Integrated transcriptomics and proteomics define the TRP channel hierarchy in mouse cortex

    doi: 10.64898/2026.04.07.716663

    Figure Lengend Snippet: ( A ) Bulk cortex TaqMan qPCR showing mean Ct values for Trpa1 and Trpv1 in adult mouse cortex. Both transcripts are detected only at high Ct values. Red dashed line indicates Gapdh Ct. ( B ) TaqMan qPCR of FACS-sorted cortical cell populations showing mean Ct values by fraction: neurons (blue), astrocytes (orange), and NeuN⁺/ACSA2⁺ double-positive cells (grey). Dashed lines indicate fraction-specific Gapdh Ct. “‡” indicate no detectable amplification reactions. Trpv1 is neuron-only at high Ct; Trpa1 is rare/borderline. ( C, D ) Subcellular fractionation and immunoblotting for TRPA1 and TRPV1, respectively. Cortex lysates (n = 3) were separated into supernatant (S) and membrane pellet (P) fractions; Ladder (L). Faint immunoreactive bands near the expected molecular weight (∼130–140 and ∼95 kDa, respectively) are preferentially enriched in pellet fractions. GAPDH (∼37 kDa) was used as a loading control. Kidney, DRG, and testes processed in parallel serve as positive control tissues. Note: Lysates and controls were processed in the same experiment and run on the same gels/blots. ( E, F ) Immunoprecipitation (IP) from cortex (C) and DRG (D) lysates followed by SDS–PAGE/Western blotting and LC–MS/MS. As shown in Supplementary Fig. 12f, no TRPA1 peptides were detected, and only extremely low-intensity TRPV1 protein-group signals were observed without replicate consistency.

    Article Snippet: In the first approach, sections were incubated overnight at 4 °C with primary antibodies against TRPA1 (Alomone Labs, ACC-037) or TRPV1 (Alomone Labs, ACC-030), diluted 1:200 in blocking buffer.

    Techniques: Amplification, Fractionation, Western Blot, Membrane, Molecular Weight, Control, Positive Control, Immunoprecipitation, SDS Page, Liquid Chromatography with Mass Spectroscopy