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Alomone Labs anti-trpv1 antibody
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OriGene trpv1
Identification of the principal ECS elements in UB/OC1 cells. Western blots of eCB receptors (A) CB 1 R, (B) CB 2 R, (C) <t>TRPV1,</t> (D) PPARα, (E) PPARδ, and (F) PPARγ. Western blots of the AEA biosynthetic enzymes (G) NAPE‐PLD and (H) ABHD4, and of the AEA degradative enzymes (I) FAAH and (J) NAAA. Western blots of the primary 2‐AG metabolic enzymes (K) DAGLα, (L) DAGLβ, and (M) MAGL, and of the additional 2‐AG hydrolases (N) ABHD6 and (O) ABHD12. Each protein is shown alongside positive controls from mouse tissues with respective GAPDH housekeeping. The whole Western blot bands are reported in Figures . (P) Endogenous levels of AEA and 2‐AG and of (Q) eCB‐like compounds in UB/OC1 cells quantified by UHPLC–MS/MS. The data are presented as a box plot with whiskers ranging from min to max values. Each eCB is presented alongside its chemical structure. (R) Levels of eCBs and eCB‐like compounds in UB/OC1 cells are represented as a heatmap ( n = 4). 2‐AG, 2‐arachidonoylglycerol; AEA, N ‐arachidonoylethanolamine; ABHD4/6/12, α/β hydrolase domain‐containing protein; B, brain; CB 1 R, cannabinoid receptor 1; CB 2 R, cannabinoid receptor 2; DAGLα/β, diacylglycerol lipases α and β; DHEA, docosahexaenoylethanolamine; EPEA, N ‐epoxyeicosatetraenoylethanolamine; FAAH, fatty acid amide hydrolase; GAPDH, glyceraldehyde‐3‐phosphate dehydrogenase; H, heart; L, liver; LEA, N ‐linoleoylethanolamine; MAGL, monoacylglycerol lipase; NAPE‐PLD, N ‐acyl‐phosphatidylethanolamines‐specific phospholipase D; NAAA, N ‐acylethanolamine acid amidase; OEA, N ‐oleoylethanolamine; PEA, N ‐palmitoylethanolamine; POEA, N ‐palmitoleoylethanolamine; PPARα/γ/δ, peroxisome proliferator‐activated nuclear receptors α, γ, δ; SEA, N ‐stearoylethanolamine; <t>TRPV1,</t> transient receptor potential <t>vanilloid</t> <t>receptor</t> 1.
Trpv1, supplied by OriGene, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Changes in <t>TRPV1</t> mRNA and protein expression after agonist and antagonist administration in CTX-induced skeletal muscle injury in mice. A-D Representative Western blot and relative protein level of TRPV1 in normal muscle tissue after CAP and CPZ administration ( n = 3 animals per experimental group; mean ± SD; One-way ANOVA). E Representative Western blot of TRPV1 in CTX-induced muscle tissue after treatment with CAP and CPZ at different points in time. F The relative protein level of TRPV1 in the CTX group at 2d, 4d, 6d ( n = 3 animals per experimental group; mean ± SD; One-way ANOVA). G The expression of TRPV1 in the CTX group at 2d, 4d, 6d according to qPCR ( n = 3 animals per experimental group; mean ± SD; One-way ANOVA). H The relative protein level of TRPV1 in CTX-induced muscle tissue after treatment with CAP and CPZ at different points in time. ( n = 3 animals per experimental group; mean ± SD; Two-way ANOVA). Statistical significance was set at P < 0.05. * P < 0.05; ** P < 0.01; *** P < 0.001; **** P < 0.0001
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Changes in <t>TRPV1</t> mRNA and protein expression after agonist and antagonist administration in CTX-induced skeletal muscle injury in mice. A-D Representative Western blot and relative protein level of TRPV1 in normal muscle tissue after CAP and CPZ administration ( n = 3 animals per experimental group; mean ± SD; One-way ANOVA). E Representative Western blot of TRPV1 in CTX-induced muscle tissue after treatment with CAP and CPZ at different points in time. F The relative protein level of TRPV1 in the CTX group at 2d, 4d, 6d ( n = 3 animals per experimental group; mean ± SD; One-way ANOVA). G The expression of TRPV1 in the CTX group at 2d, 4d, 6d according to qPCR ( n = 3 animals per experimental group; mean ± SD; One-way ANOVA). H The relative protein level of TRPV1 in CTX-induced muscle tissue after treatment with CAP and CPZ at different points in time. ( n = 3 animals per experimental group; mean ± SD; Two-way ANOVA). Statistical significance was set at P < 0.05. * P < 0.05; ** P < 0.01; *** P < 0.001; **** P < 0.0001
Anti Trpv1 Vr1 Polyclonal Antibody Rabbit, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Alomone Labs rabbit anti trpv1 polyclonal antiserum
Changes in <t>TRPV1</t> mRNA and protein expression after agonist and antagonist administration in CTX-induced skeletal muscle injury in mice. A-D Representative Western blot and relative protein level of TRPV1 in normal muscle tissue after CAP and CPZ administration ( n = 3 animals per experimental group; mean ± SD; One-way ANOVA). E Representative Western blot of TRPV1 in CTX-induced muscle tissue after treatment with CAP and CPZ at different points in time. F The relative protein level of TRPV1 in the CTX group at 2d, 4d, 6d ( n = 3 animals per experimental group; mean ± SD; One-way ANOVA). G The expression of TRPV1 in the CTX group at 2d, 4d, 6d according to qPCR ( n = 3 animals per experimental group; mean ± SD; One-way ANOVA). H The relative protein level of TRPV1 in CTX-induced muscle tissue after treatment with CAP and CPZ at different points in time. ( n = 3 animals per experimental group; mean ± SD; Two-way ANOVA). Statistical significance was set at P < 0.05. * P < 0.05; ** P < 0.01; *** P < 0.001; **** P < 0.0001
Rabbit Anti Trpv1 Polyclonal Antiserum, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Alomone Labs rabbit anti trpv1 polyclonal primary antibody
(A-F) . Pain behavioral assessment of <t>Trpv1-Cre</t> DTA and <t>Trpv1-Cre</t> VGLUT2 cKO mice and their respective littermate controls. (A) Latency to withdrawal to radiant heat. n=9 (5M/4F) for Control and n=5 (4M/1F) for DTA; n=9 (4M/5F) for Control and n=11 (6M/5F) for VGLUT2 cKO. (B) Temperature of first lick and jump on Ramping Hot Plate. n=16 (5M/11F) for Control and n=6 (4M/2F) for DTA; n=9 (4M/5F) for Control and n=11 (6M/5F) for VGLUT2 cKO. (C) Latency to withdrawal on Static Hot Plate. n=9 (5M/4F) for Control and n=5 (4M/1F) for DTA; n=18 (11M/7F) for Control and n=9 (6M/3F) for VGLUT2 cKO. (D) Latency to withdrawal to dry ice. n=9 (5M/4F) for Control and n=5 (4M/1F) for DTA; n=9 (4M/5F) for Control and n=11 (6M/5F) for VGLUT2 cKO. (E) Ethogram and summary data showing time spent licking paw injected with capsaicin. n=9 (5M/4F) for Control and n=5 (4M/1F) for DTA; n=5 (3M/2F) for Control and n=7 (5M/2F) for VGLUT2 cKO. (F) Ethogram and summary data showing time spent licking paw injected with mustard oil. n=9 (5M/4F) for Control and n=5 (4M/1F) for DTA; n=10 (3M/7F) for Control and n=12 (5M/7F) for VGLUT2 cKO. Bars represent mean ± SEM. Means were compared by One-WAY ANOVA, with Holm-Sidak multiple comparisons test used to compare DTA and VGLUT2 cKO with one another, and with their respective littermate controls. * p <0.05, ** p <0.01 *** p <0.001.
Rabbit Anti Trpv1 Polyclonal Primary Antibody, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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(A-F) . Pain behavioral assessment of <t>Trpv1-Cre</t> DTA and <t>Trpv1-Cre</t> VGLUT2 cKO mice and their respective littermate controls. (A) Latency to withdrawal to radiant heat. n=9 (5M/4F) for Control and n=5 (4M/1F) for DTA; n=9 (4M/5F) for Control and n=11 (6M/5F) for VGLUT2 cKO. (B) Temperature of first lick and jump on Ramping Hot Plate. n=16 (5M/11F) for Control and n=6 (4M/2F) for DTA; n=9 (4M/5F) for Control and n=11 (6M/5F) for VGLUT2 cKO. (C) Latency to withdrawal on Static Hot Plate. n=9 (5M/4F) for Control and n=5 (4M/1F) for DTA; n=18 (11M/7F) for Control and n=9 (6M/3F) for VGLUT2 cKO. (D) Latency to withdrawal to dry ice. n=9 (5M/4F) for Control and n=5 (4M/1F) for DTA; n=9 (4M/5F) for Control and n=11 (6M/5F) for VGLUT2 cKO. (E) Ethogram and summary data showing time spent licking paw injected with capsaicin. n=9 (5M/4F) for Control and n=5 (4M/1F) for DTA; n=5 (3M/2F) for Control and n=7 (5M/2F) for VGLUT2 cKO. (F) Ethogram and summary data showing time spent licking paw injected with mustard oil. n=9 (5M/4F) for Control and n=5 (4M/1F) for DTA; n=10 (3M/7F) for Control and n=12 (5M/7F) for VGLUT2 cKO. Bars represent mean ± SEM. Means were compared by One-WAY ANOVA, with Holm-Sidak multiple comparisons test used to compare DTA and VGLUT2 cKO with one another, and with their respective littermate controls. * p <0.05, ** p <0.01 *** p <0.001.
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(A-F) . Pain behavioral assessment of <t>Trpv1-Cre</t> DTA and <t>Trpv1-Cre</t> VGLUT2 cKO mice and their respective littermate controls. (A) Latency to withdrawal to radiant heat. n=9 (5M/4F) for Control and n=5 (4M/1F) for DTA; n=9 (4M/5F) for Control and n=11 (6M/5F) for VGLUT2 cKO. (B) Temperature of first lick and jump on Ramping Hot Plate. n=16 (5M/11F) for Control and n=6 (4M/2F) for DTA; n=9 (4M/5F) for Control and n=11 (6M/5F) for VGLUT2 cKO. (C) Latency to withdrawal on Static Hot Plate. n=9 (5M/4F) for Control and n=5 (4M/1F) for DTA; n=18 (11M/7F) for Control and n=9 (6M/3F) for VGLUT2 cKO. (D) Latency to withdrawal to dry ice. n=9 (5M/4F) for Control and n=5 (4M/1F) for DTA; n=9 (4M/5F) for Control and n=11 (6M/5F) for VGLUT2 cKO. (E) Ethogram and summary data showing time spent licking paw injected with capsaicin. n=9 (5M/4F) for Control and n=5 (4M/1F) for DTA; n=5 (3M/2F) for Control and n=7 (5M/2F) for VGLUT2 cKO. (F) Ethogram and summary data showing time spent licking paw injected with mustard oil. n=9 (5M/4F) for Control and n=5 (4M/1F) for DTA; n=10 (3M/7F) for Control and n=12 (5M/7F) for VGLUT2 cKO. Bars represent mean ± SEM. Means were compared by One-WAY ANOVA, with Holm-Sidak multiple comparisons test used to compare DTA and VGLUT2 cKO with one another, and with their respective littermate controls. * p <0.05, ** p <0.01 *** p <0.001.
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Image Search Results


Journal: Cell Reports Medicine

Article Title: A biomimetic hybrid membrane vesicle nanoplatform attenuates tendinopathy through neuroinflammation modulation and tendon regeneration

doi: 10.1016/j.xcrm.2026.102937

Figure Lengend Snippet:

Article Snippet: Rabbit Polyclonal anti-TRPV1 , ABclonal , Cat# A8564; RRID: AB_2772734.

Techniques: Recombinant, Lysis, Hydroxyproline Assay, Enzyme-linked Immunosorbent Assay, Isolation, SYBR Green Assay, Bicinchoninic Acid Protein Assay, Staining, Software

Identification of the principal ECS elements in UB/OC1 cells. Western blots of eCB receptors (A) CB 1 R, (B) CB 2 R, (C) TRPV1, (D) PPARα, (E) PPARδ, and (F) PPARγ. Western blots of the AEA biosynthetic enzymes (G) NAPE‐PLD and (H) ABHD4, and of the AEA degradative enzymes (I) FAAH and (J) NAAA. Western blots of the primary 2‐AG metabolic enzymes (K) DAGLα, (L) DAGLβ, and (M) MAGL, and of the additional 2‐AG hydrolases (N) ABHD6 and (O) ABHD12. Each protein is shown alongside positive controls from mouse tissues with respective GAPDH housekeeping. The whole Western blot bands are reported in Figures . (P) Endogenous levels of AEA and 2‐AG and of (Q) eCB‐like compounds in UB/OC1 cells quantified by UHPLC–MS/MS. The data are presented as a box plot with whiskers ranging from min to max values. Each eCB is presented alongside its chemical structure. (R) Levels of eCBs and eCB‐like compounds in UB/OC1 cells are represented as a heatmap ( n = 4). 2‐AG, 2‐arachidonoylglycerol; AEA, N ‐arachidonoylethanolamine; ABHD4/6/12, α/β hydrolase domain‐containing protein; B, brain; CB 1 R, cannabinoid receptor 1; CB 2 R, cannabinoid receptor 2; DAGLα/β, diacylglycerol lipases α and β; DHEA, docosahexaenoylethanolamine; EPEA, N ‐epoxyeicosatetraenoylethanolamine; FAAH, fatty acid amide hydrolase; GAPDH, glyceraldehyde‐3‐phosphate dehydrogenase; H, heart; L, liver; LEA, N ‐linoleoylethanolamine; MAGL, monoacylglycerol lipase; NAPE‐PLD, N ‐acyl‐phosphatidylethanolamines‐specific phospholipase D; NAAA, N ‐acylethanolamine acid amidase; OEA, N ‐oleoylethanolamine; PEA, N ‐palmitoylethanolamine; POEA, N ‐palmitoleoylethanolamine; PPARα/γ/δ, peroxisome proliferator‐activated nuclear receptors α, γ, δ; SEA, N ‐stearoylethanolamine; TRPV1, transient receptor potential vanilloid receptor 1.

Journal: The FASEB Journal

Article Title: Unraveling Endocannabinoid Signaling Pathways in Cisplatin‐Induced Ototoxicity

doi: 10.1096/fj.202502888RR

Figure Lengend Snippet: Identification of the principal ECS elements in UB/OC1 cells. Western blots of eCB receptors (A) CB 1 R, (B) CB 2 R, (C) TRPV1, (D) PPARα, (E) PPARδ, and (F) PPARγ. Western blots of the AEA biosynthetic enzymes (G) NAPE‐PLD and (H) ABHD4, and of the AEA degradative enzymes (I) FAAH and (J) NAAA. Western blots of the primary 2‐AG metabolic enzymes (K) DAGLα, (L) DAGLβ, and (M) MAGL, and of the additional 2‐AG hydrolases (N) ABHD6 and (O) ABHD12. Each protein is shown alongside positive controls from mouse tissues with respective GAPDH housekeeping. The whole Western blot bands are reported in Figures . (P) Endogenous levels of AEA and 2‐AG and of (Q) eCB‐like compounds in UB/OC1 cells quantified by UHPLC–MS/MS. The data are presented as a box plot with whiskers ranging from min to max values. Each eCB is presented alongside its chemical structure. (R) Levels of eCBs and eCB‐like compounds in UB/OC1 cells are represented as a heatmap ( n = 4). 2‐AG, 2‐arachidonoylglycerol; AEA, N ‐arachidonoylethanolamine; ABHD4/6/12, α/β hydrolase domain‐containing protein; B, brain; CB 1 R, cannabinoid receptor 1; CB 2 R, cannabinoid receptor 2; DAGLα/β, diacylglycerol lipases α and β; DHEA, docosahexaenoylethanolamine; EPEA, N ‐epoxyeicosatetraenoylethanolamine; FAAH, fatty acid amide hydrolase; GAPDH, glyceraldehyde‐3‐phosphate dehydrogenase; H, heart; L, liver; LEA, N ‐linoleoylethanolamine; MAGL, monoacylglycerol lipase; NAPE‐PLD, N ‐acyl‐phosphatidylethanolamines‐specific phospholipase D; NAAA, N ‐acylethanolamine acid amidase; OEA, N ‐oleoylethanolamine; PEA, N ‐palmitoylethanolamine; POEA, N ‐palmitoleoylethanolamine; PPARα/γ/δ, peroxisome proliferator‐activated nuclear receptors α, γ, δ; SEA, N ‐stearoylethanolamine; TRPV1, transient receptor potential vanilloid receptor 1.

Article Snippet: TRPV1 , OriGene TA336871 , Rabbit , 1:1000 , Nonfat dry milk 5% , Super Signal West Pico Plus.

Techniques: Western Blot, Tandem Mass Spectroscopy

Analysis of eCB receptors in UB/OC1 cells upon cisplatin treatment. (A–F) Representative Western blot bands and densitometric quantification of CB 1 R (A), CB 2 R (B), TRPV1 (C), PPARα (D), PPARδ (E), and PPARγ (F) with respective GAPDH housekeeping in VEH and CIS‐treated cells. Data is presented as mean ± SEM. Statistical analysis was performed using a two‐tailed unpaired Student's t ‐test ( n = 3) (*** p ≤ 0.001 vs VEH). Whole Western blot bands are reported in Figures . (G) Schematic representation of the immunofluorescence staining method using anti‐CB 2 R antibody. (H–J) Representative confocal images of VEH‐treated cells immunostained with anti‐CB 2 R (red) and counterstained with Hoechst nuclear dye (blue); (K–M) Representative confocal images of CIS‐ treated cells immunostained with anti‐CB2R (red) and counterstained with Hoechst nuclear dye (blue). Scale bar: 20 μm. (N) Schematic representation of the CB 2 R selective probe SiR‐8 live‐cell staining. (O–Q) Representative confocal microscopy images of VEH‐treated cells stained with CB 2 R SiR‐8 probe (red) and counterstained with Hoechst nuclear dye (blue); (R–T) Representative confocal microscopy images of CIS‐treated cells stained with CB 2 R SiR‐8 probe (red) and counterstained with Hoechst nuclear dye (blue). Scale bar: 75 μm. White dotted boxes show zoomed‐in views of UB/OC1 cells, and the corresponding fluorescence intensity histograms are representative of the yellow circle‐marked areas. Live‐cell time‐lapse video is provided in the . CB 1 R, cannabinoid receptor 1; CB 2 R, cannabinoid receptor 2; CIS, cisplatin; eCBs, endocannabinoids; GAPDH, glyceraldehyde‐3‐phosphate dehydrogenase; PPAR α, γ, δ, peroxisome proliferator‐activated nuclear receptors α, γ, δ; TRPV1, transient receptor potential vanilloid receptor 1; VEH, vehicle.

Journal: The FASEB Journal

Article Title: Unraveling Endocannabinoid Signaling Pathways in Cisplatin‐Induced Ototoxicity

doi: 10.1096/fj.202502888RR

Figure Lengend Snippet: Analysis of eCB receptors in UB/OC1 cells upon cisplatin treatment. (A–F) Representative Western blot bands and densitometric quantification of CB 1 R (A), CB 2 R (B), TRPV1 (C), PPARα (D), PPARδ (E), and PPARγ (F) with respective GAPDH housekeeping in VEH and CIS‐treated cells. Data is presented as mean ± SEM. Statistical analysis was performed using a two‐tailed unpaired Student's t ‐test ( n = 3) (*** p ≤ 0.001 vs VEH). Whole Western blot bands are reported in Figures . (G) Schematic representation of the immunofluorescence staining method using anti‐CB 2 R antibody. (H–J) Representative confocal images of VEH‐treated cells immunostained with anti‐CB 2 R (red) and counterstained with Hoechst nuclear dye (blue); (K–M) Representative confocal images of CIS‐ treated cells immunostained with anti‐CB2R (red) and counterstained with Hoechst nuclear dye (blue). Scale bar: 20 μm. (N) Schematic representation of the CB 2 R selective probe SiR‐8 live‐cell staining. (O–Q) Representative confocal microscopy images of VEH‐treated cells stained with CB 2 R SiR‐8 probe (red) and counterstained with Hoechst nuclear dye (blue); (R–T) Representative confocal microscopy images of CIS‐treated cells stained with CB 2 R SiR‐8 probe (red) and counterstained with Hoechst nuclear dye (blue). Scale bar: 75 μm. White dotted boxes show zoomed‐in views of UB/OC1 cells, and the corresponding fluorescence intensity histograms are representative of the yellow circle‐marked areas. Live‐cell time‐lapse video is provided in the . CB 1 R, cannabinoid receptor 1; CB 2 R, cannabinoid receptor 2; CIS, cisplatin; eCBs, endocannabinoids; GAPDH, glyceraldehyde‐3‐phosphate dehydrogenase; PPAR α, γ, δ, peroxisome proliferator‐activated nuclear receptors α, γ, δ; TRPV1, transient receptor potential vanilloid receptor 1; VEH, vehicle.

Article Snippet: TRPV1 , OriGene TA336871 , Rabbit , 1:1000 , Nonfat dry milk 5% , Super Signal West Pico Plus.

Techniques: Western Blot, Two Tailed Test, Immunofluorescence, Staining, Confocal Microscopy, Fluorescence

Changes in TRPV1 mRNA and protein expression after agonist and antagonist administration in CTX-induced skeletal muscle injury in mice. A-D Representative Western blot and relative protein level of TRPV1 in normal muscle tissue after CAP and CPZ administration ( n = 3 animals per experimental group; mean ± SD; One-way ANOVA). E Representative Western blot of TRPV1 in CTX-induced muscle tissue after treatment with CAP and CPZ at different points in time. F The relative protein level of TRPV1 in the CTX group at 2d, 4d, 6d ( n = 3 animals per experimental group; mean ± SD; One-way ANOVA). G The expression of TRPV1 in the CTX group at 2d, 4d, 6d according to qPCR ( n = 3 animals per experimental group; mean ± SD; One-way ANOVA). H The relative protein level of TRPV1 in CTX-induced muscle tissue after treatment with CAP and CPZ at different points in time. ( n = 3 animals per experimental group; mean ± SD; Two-way ANOVA). Statistical significance was set at P < 0.05. * P < 0.05; ** P < 0.01; *** P < 0.001; **** P < 0.0001

Journal: Skeletal Muscle

Article Title: TRPV1 manipulating polarization of M1/M2 macrophages to promote skeletal muscle regeneration

doi: 10.1186/s13395-026-00417-6

Figure Lengend Snippet: Changes in TRPV1 mRNA and protein expression after agonist and antagonist administration in CTX-induced skeletal muscle injury in mice. A-D Representative Western blot and relative protein level of TRPV1 in normal muscle tissue after CAP and CPZ administration ( n = 3 animals per experimental group; mean ± SD; One-way ANOVA). E Representative Western blot of TRPV1 in CTX-induced muscle tissue after treatment with CAP and CPZ at different points in time. F The relative protein level of TRPV1 in the CTX group at 2d, 4d, 6d ( n = 3 animals per experimental group; mean ± SD; One-way ANOVA). G The expression of TRPV1 in the CTX group at 2d, 4d, 6d according to qPCR ( n = 3 animals per experimental group; mean ± SD; One-way ANOVA). H The relative protein level of TRPV1 in CTX-induced muscle tissue after treatment with CAP and CPZ at different points in time. ( n = 3 animals per experimental group; mean ± SD; Two-way ANOVA). Statistical significance was set at P < 0.05. * P < 0.05; ** P < 0.01; *** P < 0.001; **** P < 0.0001

Article Snippet: Deparaffinized sections were blocked with 5% bovine serum albumin (BSA) and incubated overnight at 4 °C with the following primary antibodies: mouse anti-CD86 monoclonal antibody (1:200, Santa Cruz Biotechnology, sc-28347); mouse anti-CD206 polyclonal antibody (1:200, Santa Cruz Biotechnology, sc-58986); rat anti-F4/80 monoclonal antibody (1:100, Abcam, ab1691); rabbit anti-F4/80 monoclonal antibody (1:200, Proteintech, #27044-1-AP); rabbit anti-TRPV1 polyclonal antibody (1:200, ABclonal, A8564); and mouse anti-MyoD monoclonal antibody (1:100, Santa Cruz Biotechnology, sc-377460).

Techniques: Expressing, Western Blot

TRPV1 activation facilitates myogenesis and inhibits the fibrotic process in the CTX-induced skeletal muscle injury in mice. A Flow diagram of the experiment in each group of mice, the red markings indicate the time points for drug injections. B Representative H&E images show the proportion of CNF and CSA distribution in CTX-induced muscle tissue treated with CAP and CPZ at different days. C , D The proportion of centrally nucleated fibers and the cross-sectional area of regenerating myofibers in CTX-induced muscle tissue treated with CAP and CPZ at 4d, 6d and 8d. ( n = 5 animals per experimental group; mean ± SD; Two-way ANOVA). E - G Representative Sirius Red staining images show the collagen fiber deposition in CTX-induced muscle tissue treated with CAP and CPZ at 8d and 10d. ( n = 5 animals per experimental group; mean ± SD; One-way ANOVA). Statistical significance was set at P < 0.05. * P < 0.05; ** P < 0.01; *** P < 0.001; **** P < 0.0001. Scale bar, 100 μm

Journal: Skeletal Muscle

Article Title: TRPV1 manipulating polarization of M1/M2 macrophages to promote skeletal muscle regeneration

doi: 10.1186/s13395-026-00417-6

Figure Lengend Snippet: TRPV1 activation facilitates myogenesis and inhibits the fibrotic process in the CTX-induced skeletal muscle injury in mice. A Flow diagram of the experiment in each group of mice, the red markings indicate the time points for drug injections. B Representative H&E images show the proportion of CNF and CSA distribution in CTX-induced muscle tissue treated with CAP and CPZ at different days. C , D The proportion of centrally nucleated fibers and the cross-sectional area of regenerating myofibers in CTX-induced muscle tissue treated with CAP and CPZ at 4d, 6d and 8d. ( n = 5 animals per experimental group; mean ± SD; Two-way ANOVA). E - G Representative Sirius Red staining images show the collagen fiber deposition in CTX-induced muscle tissue treated with CAP and CPZ at 8d and 10d. ( n = 5 animals per experimental group; mean ± SD; One-way ANOVA). Statistical significance was set at P < 0.05. * P < 0.05; ** P < 0.01; *** P < 0.001; **** P < 0.0001. Scale bar, 100 μm

Article Snippet: Deparaffinized sections were blocked with 5% bovine serum albumin (BSA) and incubated overnight at 4 °C with the following primary antibodies: mouse anti-CD86 monoclonal antibody (1:200, Santa Cruz Biotechnology, sc-28347); mouse anti-CD206 polyclonal antibody (1:200, Santa Cruz Biotechnology, sc-58986); rat anti-F4/80 monoclonal antibody (1:100, Abcam, ab1691); rabbit anti-F4/80 monoclonal antibody (1:200, Proteintech, #27044-1-AP); rabbit anti-TRPV1 polyclonal antibody (1:200, ABclonal, A8564); and mouse anti-MyoD monoclonal antibody (1:100, Santa Cruz Biotechnology, sc-377460).

Techniques: Activation Assay, Staining

Activation of TRPV1 facilitates myogenesis during the process of muscle regeneration in vivo. A-C Representative western blot and relative protein level of MyoD and myogenin in CTX-induced muscle tissue after treatment with CAP and CPZ at different points in time ( n = 3 animals per experimental group; mean ± SD; Two-way ANOVA). D , F The expression level of MyoD and myogenin mRNA in each group at different points in time ( n = 3 animals per experimental group; mean ± SD; Two-way ANOVA). E Representative immunofluorescence images of MyoD in CTX-induced muscle tissue after treatment with CAP and CPZ at 4d. G-H The relative fluorescence intensity of MyoD and the proportion of MyoD+ /DAPI + double-positive cells in each group ( n = 5 animals per experimental group; mean ± SD; One-way ANOVA). Statistical significance was set at P < 0.05. * P < 0.05; ** P < 0.01; *** P < 0.001; **** P < 0.0001. Scale bar, 50 μm

Journal: Skeletal Muscle

Article Title: TRPV1 manipulating polarization of M1/M2 macrophages to promote skeletal muscle regeneration

doi: 10.1186/s13395-026-00417-6

Figure Lengend Snippet: Activation of TRPV1 facilitates myogenesis during the process of muscle regeneration in vivo. A-C Representative western blot and relative protein level of MyoD and myogenin in CTX-induced muscle tissue after treatment with CAP and CPZ at different points in time ( n = 3 animals per experimental group; mean ± SD; Two-way ANOVA). D , F The expression level of MyoD and myogenin mRNA in each group at different points in time ( n = 3 animals per experimental group; mean ± SD; Two-way ANOVA). E Representative immunofluorescence images of MyoD in CTX-induced muscle tissue after treatment with CAP and CPZ at 4d. G-H The relative fluorescence intensity of MyoD and the proportion of MyoD+ /DAPI + double-positive cells in each group ( n = 5 animals per experimental group; mean ± SD; One-way ANOVA). Statistical significance was set at P < 0.05. * P < 0.05; ** P < 0.01; *** P < 0.001; **** P < 0.0001. Scale bar, 50 μm

Article Snippet: Deparaffinized sections were blocked with 5% bovine serum albumin (BSA) and incubated overnight at 4 °C with the following primary antibodies: mouse anti-CD86 monoclonal antibody (1:200, Santa Cruz Biotechnology, sc-28347); mouse anti-CD206 polyclonal antibody (1:200, Santa Cruz Biotechnology, sc-58986); rat anti-F4/80 monoclonal antibody (1:100, Abcam, ab1691); rabbit anti-F4/80 monoclonal antibody (1:200, Proteintech, #27044-1-AP); rabbit anti-TRPV1 polyclonal antibody (1:200, ABclonal, A8564); and mouse anti-MyoD monoclonal antibody (1:100, Santa Cruz Biotechnology, sc-377460).

Techniques: Activation Assay, In Vivo, Western Blot, Expressing, Immunofluorescence, Fluorescence

TRPV1 activation leads to a difference in macrophage infiltration with a remarkable increase of M1 and a decrease of M2 in number in vivo. A Representative immunofluorescence images of F4/80 after treatment with CAP and CPZ in CTX-induced muscle tissue at 4d. B The percentage of F4/80-positive cells between four groups at 4d post-injury ( n = 5 animals per experimental group; mean ± SD; One-way ANOVA). C , D Representative immunofluorescence images showed the relative fluorescence intensity of TRPV1 in these F4/80 + macrophages in each group ( n = 5 animals per experimental group; mean ± SD; One-way ANOVA). E , F Representative immunofluorescence images showed the infiltration of numbers of M1 (F4/80 + and CD86+) and M2 (F4/80 + and CD206+) macrophages in different groups at different intervals. G , H The proportion of M1 (F4/80 + and CD86+) macrophages and M2 macrophages (F4/80 + and CD206+) between four groups at 2-8days post-injury ( n = 5 animals per experimental group; mean ± SD; Two-way ANOVA). Statistical significance was set at P < 0.05. * P < 0.05; ** P < 0.01; *** P < 0.001; **** P < 0.0001. Scale bar, 50 μm

Journal: Skeletal Muscle

Article Title: TRPV1 manipulating polarization of M1/M2 macrophages to promote skeletal muscle regeneration

doi: 10.1186/s13395-026-00417-6

Figure Lengend Snippet: TRPV1 activation leads to a difference in macrophage infiltration with a remarkable increase of M1 and a decrease of M2 in number in vivo. A Representative immunofluorescence images of F4/80 after treatment with CAP and CPZ in CTX-induced muscle tissue at 4d. B The percentage of F4/80-positive cells between four groups at 4d post-injury ( n = 5 animals per experimental group; mean ± SD; One-way ANOVA). C , D Representative immunofluorescence images showed the relative fluorescence intensity of TRPV1 in these F4/80 + macrophages in each group ( n = 5 animals per experimental group; mean ± SD; One-way ANOVA). E , F Representative immunofluorescence images showed the infiltration of numbers of M1 (F4/80 + and CD86+) and M2 (F4/80 + and CD206+) macrophages in different groups at different intervals. G , H The proportion of M1 (F4/80 + and CD86+) macrophages and M2 macrophages (F4/80 + and CD206+) between four groups at 2-8days post-injury ( n = 5 animals per experimental group; mean ± SD; Two-way ANOVA). Statistical significance was set at P < 0.05. * P < 0.05; ** P < 0.01; *** P < 0.001; **** P < 0.0001. Scale bar, 50 μm

Article Snippet: Deparaffinized sections were blocked with 5% bovine serum albumin (BSA) and incubated overnight at 4 °C with the following primary antibodies: mouse anti-CD86 monoclonal antibody (1:200, Santa Cruz Biotechnology, sc-28347); mouse anti-CD206 polyclonal antibody (1:200, Santa Cruz Biotechnology, sc-58986); rat anti-F4/80 monoclonal antibody (1:100, Abcam, ab1691); rabbit anti-F4/80 monoclonal antibody (1:200, Proteintech, #27044-1-AP); rabbit anti-TRPV1 polyclonal antibody (1:200, ABclonal, A8564); and mouse anti-MyoD monoclonal antibody (1:100, Santa Cruz Biotechnology, sc-377460).

Techniques: Activation Assay, In Vivo, Immunofluorescence, Fluorescence

TRPV1 activation modulate protein expression of markers and cytokines associated with M1 and M2 in vivo, respectively. A Representative Western blot of CD86(M1); Arg1(M2). B-E The protein expression or mRNA level of CD86 and the protein expression of IL-6(M1) ( n = 3 animals per experimental group; mean ± SD; Two-way ANOVA). F , G The protein expression of Arg1 ( n = 3 animals per experimental group; mean ± SD; Two-way ANOVA). H , I The mRNA level or protein expression of CD206(M2) ( n = 3 animals per experimental group; mean ± SD; Two-way ANOVA). Statistical significance was set at P < 0.05. * P < 0.05; ** P < 0.01; *** P < 0.001; **** P < 0.0001

Journal: Skeletal Muscle

Article Title: TRPV1 manipulating polarization of M1/M2 macrophages to promote skeletal muscle regeneration

doi: 10.1186/s13395-026-00417-6

Figure Lengend Snippet: TRPV1 activation modulate protein expression of markers and cytokines associated with M1 and M2 in vivo, respectively. A Representative Western blot of CD86(M1); Arg1(M2). B-E The protein expression or mRNA level of CD86 and the protein expression of IL-6(M1) ( n = 3 animals per experimental group; mean ± SD; Two-way ANOVA). F , G The protein expression of Arg1 ( n = 3 animals per experimental group; mean ± SD; Two-way ANOVA). H , I The mRNA level or protein expression of CD206(M2) ( n = 3 animals per experimental group; mean ± SD; Two-way ANOVA). Statistical significance was set at P < 0.05. * P < 0.05; ** P < 0.01; *** P < 0.001; **** P < 0.0001

Article Snippet: Deparaffinized sections were blocked with 5% bovine serum albumin (BSA) and incubated overnight at 4 °C with the following primary antibodies: mouse anti-CD86 monoclonal antibody (1:200, Santa Cruz Biotechnology, sc-28347); mouse anti-CD206 polyclonal antibody (1:200, Santa Cruz Biotechnology, sc-58986); rat anti-F4/80 monoclonal antibody (1:100, Abcam, ab1691); rabbit anti-F4/80 monoclonal antibody (1:200, Proteintech, #27044-1-AP); rabbit anti-TRPV1 polyclonal antibody (1:200, ABclonal, A8564); and mouse anti-MyoD monoclonal antibody (1:100, Santa Cruz Biotechnology, sc-377460).

Techniques: Activation Assay, Expressing, In Vivo, Western Blot

TRPV1 inhibits M1 polarization and promotes M2 polarization in vitro. A , C Representative western blot of CD86(M1); Arg1(M2). B , D The expression of CD86 and Arg-1 in response to LPS/IFN-γ and IL-4/IL-10 stimulation at the protein level, respectively ( n = 3 independent replicates in cells; mean ± SD; One-way ANOVA). E Representative Western blot of IL-6 and CD86(M1) after treatment with CAP and CPZ in vitro. F-I The protein expression of IL-6 and CD86 in different groups ( n = 3 independent replicates in cells; mean ± SD; One-way ANOVA). J Representative western blot of CD206 and Arg1 (M2) after treatment with CAP and CPZ in vitro. K-N The protein expression of CD206 and Arg1 in each group ( n = 3 independent replicates in cells; mean ± SD; One-way ANOVA). Statistical significance was set at P < 0.05. * P < 0.05; ** P < 0.01; *** P < 0.001; **** P < 0.0001

Journal: Skeletal Muscle

Article Title: TRPV1 manipulating polarization of M1/M2 macrophages to promote skeletal muscle regeneration

doi: 10.1186/s13395-026-00417-6

Figure Lengend Snippet: TRPV1 inhibits M1 polarization and promotes M2 polarization in vitro. A , C Representative western blot of CD86(M1); Arg1(M2). B , D The expression of CD86 and Arg-1 in response to LPS/IFN-γ and IL-4/IL-10 stimulation at the protein level, respectively ( n = 3 independent replicates in cells; mean ± SD; One-way ANOVA). E Representative Western blot of IL-6 and CD86(M1) after treatment with CAP and CPZ in vitro. F-I The protein expression of IL-6 and CD86 in different groups ( n = 3 independent replicates in cells; mean ± SD; One-way ANOVA). J Representative western blot of CD206 and Arg1 (M2) after treatment with CAP and CPZ in vitro. K-N The protein expression of CD206 and Arg1 in each group ( n = 3 independent replicates in cells; mean ± SD; One-way ANOVA). Statistical significance was set at P < 0.05. * P < 0.05; ** P < 0.01; *** P < 0.001; **** P < 0.0001

Article Snippet: Deparaffinized sections were blocked with 5% bovine serum albumin (BSA) and incubated overnight at 4 °C with the following primary antibodies: mouse anti-CD86 monoclonal antibody (1:200, Santa Cruz Biotechnology, sc-28347); mouse anti-CD206 polyclonal antibody (1:200, Santa Cruz Biotechnology, sc-58986); rat anti-F4/80 monoclonal antibody (1:100, Abcam, ab1691); rabbit anti-F4/80 monoclonal antibody (1:200, Proteintech, #27044-1-AP); rabbit anti-TRPV1 polyclonal antibody (1:200, ABclonal, A8564); and mouse anti-MyoD monoclonal antibody (1:100, Santa Cruz Biotechnology, sc-377460).

Techniques: In Vitro, Western Blot, Expressing

The influence of TRPV1 in the C2C12 myoblasts differentiation. A-C The relative fluorescence intensity of TRPV1( n = 5 independent random fields of cells; mean ± SD; One-way ANOVA). D Representative western blot of TRPV1 after treatment with CAP and CPZ in vitro. E The protein expression of TRPV1 ( n = 3 independent replicates in cells; mean ± SD; One-way ANOVA). F Representative western blot of MyoD and myogenin after treatment with CAP and CPZ in differentiation medium at different intervals. G , H The protein expression of MyoD and myogenin among each group ( n = 3 independent replicates in cells; mean ± SD; Two-way ANOVA). I , J The relative fluorescence intensity of MYH3 in multinucleated myotubes in each group time-dependently ( n = 5 independent random fields of cells; mean ± SD; Two-way ANOVA). K Representative Giemsa staining images showed the effect of TRPV1 activation individually on multinucleated myotubes ( n = 5 independent random fields of cells). Statistical significance was set at P < 0.05. * P < 0.05; ** P < 0.01; *** P < 0.001; **** P < 0.0001. Scale bar, 50 μm, 100 μm

Journal: Skeletal Muscle

Article Title: TRPV1 manipulating polarization of M1/M2 macrophages to promote skeletal muscle regeneration

doi: 10.1186/s13395-026-00417-6

Figure Lengend Snippet: The influence of TRPV1 in the C2C12 myoblasts differentiation. A-C The relative fluorescence intensity of TRPV1( n = 5 independent random fields of cells; mean ± SD; One-way ANOVA). D Representative western blot of TRPV1 after treatment with CAP and CPZ in vitro. E The protein expression of TRPV1 ( n = 3 independent replicates in cells; mean ± SD; One-way ANOVA). F Representative western blot of MyoD and myogenin after treatment with CAP and CPZ in differentiation medium at different intervals. G , H The protein expression of MyoD and myogenin among each group ( n = 3 independent replicates in cells; mean ± SD; Two-way ANOVA). I , J The relative fluorescence intensity of MYH3 in multinucleated myotubes in each group time-dependently ( n = 5 independent random fields of cells; mean ± SD; Two-way ANOVA). K Representative Giemsa staining images showed the effect of TRPV1 activation individually on multinucleated myotubes ( n = 5 independent random fields of cells). Statistical significance was set at P < 0.05. * P < 0.05; ** P < 0.01; *** P < 0.001; **** P < 0.0001. Scale bar, 50 μm, 100 μm

Article Snippet: Deparaffinized sections were blocked with 5% bovine serum albumin (BSA) and incubated overnight at 4 °C with the following primary antibodies: mouse anti-CD86 monoclonal antibody (1:200, Santa Cruz Biotechnology, sc-28347); mouse anti-CD206 polyclonal antibody (1:200, Santa Cruz Biotechnology, sc-58986); rat anti-F4/80 monoclonal antibody (1:100, Abcam, ab1691); rabbit anti-F4/80 monoclonal antibody (1:200, Proteintech, #27044-1-AP); rabbit anti-TRPV1 polyclonal antibody (1:200, ABclonal, A8564); and mouse anti-MyoD monoclonal antibody (1:100, Santa Cruz Biotechnology, sc-377460).

Techniques: Fluorescence, Western Blot, In Vitro, Expressing, Staining, Activation Assay

TRPV1 regulates M1/M2 macrophage polarization to promote myogenic differentiation in C2C12 cells. A C2C12 myoblasts were co-cultured with M1 or M2 macrophages for 4 days via a transwell cell culture insert. B Representative Western blot bands of MyoD and MYH3 in C2C12 myoblasts after being co-cultured with M1 or M2 macrophages for 4 days. C , D The protein expression of MyoD and MYH3 in those C2C12 myoblasts which were co-cultured with M1or M2 macrophages after CAP and CPZ treatment ( n = 3 independent replicates in cells; mean ± SD; Two-way ANOVA). E , F Representative immunofluorescence images showed myotubes fusion index in C2C12 cells ( n = 5 independent random fields of cells; mean ± SD; Two-way ANOVA). Statistical significance was set at P < 0.05. * P < 0.05; ** P < 0.01; *** P < 0.001; **** P < 0.0001. Scale bar, 50 μm

Journal: Skeletal Muscle

Article Title: TRPV1 manipulating polarization of M1/M2 macrophages to promote skeletal muscle regeneration

doi: 10.1186/s13395-026-00417-6

Figure Lengend Snippet: TRPV1 regulates M1/M2 macrophage polarization to promote myogenic differentiation in C2C12 cells. A C2C12 myoblasts were co-cultured with M1 or M2 macrophages for 4 days via a transwell cell culture insert. B Representative Western blot bands of MyoD and MYH3 in C2C12 myoblasts after being co-cultured with M1 or M2 macrophages for 4 days. C , D The protein expression of MyoD and MYH3 in those C2C12 myoblasts which were co-cultured with M1or M2 macrophages after CAP and CPZ treatment ( n = 3 independent replicates in cells; mean ± SD; Two-way ANOVA). E , F Representative immunofluorescence images showed myotubes fusion index in C2C12 cells ( n = 5 independent random fields of cells; mean ± SD; Two-way ANOVA). Statistical significance was set at P < 0.05. * P < 0.05; ** P < 0.01; *** P < 0.001; **** P < 0.0001. Scale bar, 50 μm

Article Snippet: Deparaffinized sections were blocked with 5% bovine serum albumin (BSA) and incubated overnight at 4 °C with the following primary antibodies: mouse anti-CD86 monoclonal antibody (1:200, Santa Cruz Biotechnology, sc-28347); mouse anti-CD206 polyclonal antibody (1:200, Santa Cruz Biotechnology, sc-58986); rat anti-F4/80 monoclonal antibody (1:100, Abcam, ab1691); rabbit anti-F4/80 monoclonal antibody (1:200, Proteintech, #27044-1-AP); rabbit anti-TRPV1 polyclonal antibody (1:200, ABclonal, A8564); and mouse anti-MyoD monoclonal antibody (1:100, Santa Cruz Biotechnology, sc-377460).

Techniques: Cell Characterization, Cell Culture, Western Blot, Expressing, Immunofluorescence

(A-F) . Pain behavioral assessment of Trpv1-Cre DTA and Trpv1-Cre VGLUT2 cKO mice and their respective littermate controls. (A) Latency to withdrawal to radiant heat. n=9 (5M/4F) for Control and n=5 (4M/1F) for DTA; n=9 (4M/5F) for Control and n=11 (6M/5F) for VGLUT2 cKO. (B) Temperature of first lick and jump on Ramping Hot Plate. n=16 (5M/11F) for Control and n=6 (4M/2F) for DTA; n=9 (4M/5F) for Control and n=11 (6M/5F) for VGLUT2 cKO. (C) Latency to withdrawal on Static Hot Plate. n=9 (5M/4F) for Control and n=5 (4M/1F) for DTA; n=18 (11M/7F) for Control and n=9 (6M/3F) for VGLUT2 cKO. (D) Latency to withdrawal to dry ice. n=9 (5M/4F) for Control and n=5 (4M/1F) for DTA; n=9 (4M/5F) for Control and n=11 (6M/5F) for VGLUT2 cKO. (E) Ethogram and summary data showing time spent licking paw injected with capsaicin. n=9 (5M/4F) for Control and n=5 (4M/1F) for DTA; n=5 (3M/2F) for Control and n=7 (5M/2F) for VGLUT2 cKO. (F) Ethogram and summary data showing time spent licking paw injected with mustard oil. n=9 (5M/4F) for Control and n=5 (4M/1F) for DTA; n=10 (3M/7F) for Control and n=12 (5M/7F) for VGLUT2 cKO. Bars represent mean ± SEM. Means were compared by One-WAY ANOVA, with Holm-Sidak multiple comparisons test used to compare DTA and VGLUT2 cKO with one another, and with their respective littermate controls. * p <0.05, ** p <0.01 *** p <0.001.

Journal: bioRxiv

Article Title: Nociceptors use multiple neurotransmitters to drive pain

doi: 10.1101/2025.09.09.675093

Figure Lengend Snippet: (A-F) . Pain behavioral assessment of Trpv1-Cre DTA and Trpv1-Cre VGLUT2 cKO mice and their respective littermate controls. (A) Latency to withdrawal to radiant heat. n=9 (5M/4F) for Control and n=5 (4M/1F) for DTA; n=9 (4M/5F) for Control and n=11 (6M/5F) for VGLUT2 cKO. (B) Temperature of first lick and jump on Ramping Hot Plate. n=16 (5M/11F) for Control and n=6 (4M/2F) for DTA; n=9 (4M/5F) for Control and n=11 (6M/5F) for VGLUT2 cKO. (C) Latency to withdrawal on Static Hot Plate. n=9 (5M/4F) for Control and n=5 (4M/1F) for DTA; n=18 (11M/7F) for Control and n=9 (6M/3F) for VGLUT2 cKO. (D) Latency to withdrawal to dry ice. n=9 (5M/4F) for Control and n=5 (4M/1F) for DTA; n=9 (4M/5F) for Control and n=11 (6M/5F) for VGLUT2 cKO. (E) Ethogram and summary data showing time spent licking paw injected with capsaicin. n=9 (5M/4F) for Control and n=5 (4M/1F) for DTA; n=5 (3M/2F) for Control and n=7 (5M/2F) for VGLUT2 cKO. (F) Ethogram and summary data showing time spent licking paw injected with mustard oil. n=9 (5M/4F) for Control and n=5 (4M/1F) for DTA; n=10 (3M/7F) for Control and n=12 (5M/7F) for VGLUT2 cKO. Bars represent mean ± SEM. Means were compared by One-WAY ANOVA, with Holm-Sidak multiple comparisons test used to compare DTA and VGLUT2 cKO with one another, and with their respective littermate controls. * p <0.05, ** p <0.01 *** p <0.001.

Article Snippet: Afterward, sections were incubated in blocking solution containing a subset of the following primary antibodies: 1:500 or 1.1000 goat anti-CGRP polyclonal primary antibody (Abcam, #ab36001), 1:500 rat anti-Substance P polyclonal primary antibody (Abcam, #ab67006), 1:500 rabbit anti-TRPV1 polyclonal primary antibody (Alomone Labs, #ACC-030), 1:500 chicken anti-Peripherin polyclonal primary antibody (Invitrogen, #PA1-10012), 1:1000 guinea pig anti-VGlut2 polyclonal primary antibody (Millpore Sigma, #AB2251-I), and 1:1500 rabbit anti-PAM polyclonal primary antibody (Proteintech, #26972) on a shaker at room temperature overnight.

Techniques: Control, Injection

(A-F) Laser speckle contrast imaging was used to measure the blood flow in the paw following nociceptor stimulation with mustard oil. Images (A) , time course (B) and quantification (area under curve, normalized to control) (C) showing that mustard oil application evokes less blood flow in the paw of PAM cKO mice compared to controls. n=14 (5M/9F) for Control and n=10 (7M/3F) for PAM cKO. This response was completely lost in Trpv1-Cre DTA mice (D-F) . n=12 (5M/7F) for Control and n=6 (4M/2F) for DTA. Bars represent mean ± SEM. Normalized area under the curve was compared using an unpaired t test. * p <0.05, ** p <0.01 *** p <0.001.

Journal: bioRxiv

Article Title: Nociceptors use multiple neurotransmitters to drive pain

doi: 10.1101/2025.09.09.675093

Figure Lengend Snippet: (A-F) Laser speckle contrast imaging was used to measure the blood flow in the paw following nociceptor stimulation with mustard oil. Images (A) , time course (B) and quantification (area under curve, normalized to control) (C) showing that mustard oil application evokes less blood flow in the paw of PAM cKO mice compared to controls. n=14 (5M/9F) for Control and n=10 (7M/3F) for PAM cKO. This response was completely lost in Trpv1-Cre DTA mice (D-F) . n=12 (5M/7F) for Control and n=6 (4M/2F) for DTA. Bars represent mean ± SEM. Normalized area under the curve was compared using an unpaired t test. * p <0.05, ** p <0.01 *** p <0.001.

Article Snippet: Afterward, sections were incubated in blocking solution containing a subset of the following primary antibodies: 1:500 or 1.1000 goat anti-CGRP polyclonal primary antibody (Abcam, #ab36001), 1:500 rat anti-Substance P polyclonal primary antibody (Abcam, #ab67006), 1:500 rabbit anti-TRPV1 polyclonal primary antibody (Alomone Labs, #ACC-030), 1:500 chicken anti-Peripherin polyclonal primary antibody (Invitrogen, #PA1-10012), 1:1000 guinea pig anti-VGlut2 polyclonal primary antibody (Millpore Sigma, #AB2251-I), and 1:1500 rabbit anti-PAM polyclonal primary antibody (Proteintech, #26972) on a shaker at room temperature overnight.

Techniques: Imaging, Control

(A) Bulk RNA sequencing shows very few genes are differentially expressed between control and PAM cKO dorsal root ganglia. As expected, Cre was enriched in PAM cKO Trpv1 DRGs, and PAM was downregulated. n=4 (2M/2F) for Control; n=4 (2M/2F) for PAM cKO Trpv1 .

Journal: bioRxiv

Article Title: Nociceptors use multiple neurotransmitters to drive pain

doi: 10.1101/2025.09.09.675093

Figure Lengend Snippet: (A) Bulk RNA sequencing shows very few genes are differentially expressed between control and PAM cKO dorsal root ganglia. As expected, Cre was enriched in PAM cKO Trpv1 DRGs, and PAM was downregulated. n=4 (2M/2F) for Control; n=4 (2M/2F) for PAM cKO Trpv1 .

Article Snippet: Afterward, sections were incubated in blocking solution containing a subset of the following primary antibodies: 1:500 or 1.1000 goat anti-CGRP polyclonal primary antibody (Abcam, #ab36001), 1:500 rat anti-Substance P polyclonal primary antibody (Abcam, #ab67006), 1:500 rabbit anti-TRPV1 polyclonal primary antibody (Alomone Labs, #ACC-030), 1:500 chicken anti-Peripherin polyclonal primary antibody (Invitrogen, #PA1-10012), 1:1000 guinea pig anti-VGlut2 polyclonal primary antibody (Millpore Sigma, #AB2251-I), and 1:1500 rabbit anti-PAM polyclonal primary antibody (Proteintech, #26972) on a shaker at room temperature overnight.

Techniques: RNA Sequencing, Control

(A) Example confocal images of spinal cord dorsal horns showing that PAM deletion reduces the intensity of CGRP and Substance P (SP) staining in the terminal field of Trpv1 afferents. The dotted lines are traced from the region of Trpv1 staining. Note that only in the area of Trpv1 innervation would we expect to see reduced neuropeptide staining using the Trpv1-Cre approach.

Journal: bioRxiv

Article Title: Nociceptors use multiple neurotransmitters to drive pain

doi: 10.1101/2025.09.09.675093

Figure Lengend Snippet: (A) Example confocal images of spinal cord dorsal horns showing that PAM deletion reduces the intensity of CGRP and Substance P (SP) staining in the terminal field of Trpv1 afferents. The dotted lines are traced from the region of Trpv1 staining. Note that only in the area of Trpv1 innervation would we expect to see reduced neuropeptide staining using the Trpv1-Cre approach.

Article Snippet: Afterward, sections were incubated in blocking solution containing a subset of the following primary antibodies: 1:500 or 1.1000 goat anti-CGRP polyclonal primary antibody (Abcam, #ab36001), 1:500 rat anti-Substance P polyclonal primary antibody (Abcam, #ab67006), 1:500 rabbit anti-TRPV1 polyclonal primary antibody (Alomone Labs, #ACC-030), 1:500 chicken anti-Peripherin polyclonal primary antibody (Invitrogen, #PA1-10012), 1:1000 guinea pig anti-VGlut2 polyclonal primary antibody (Millpore Sigma, #AB2251-I), and 1:1500 rabbit anti-PAM polyclonal primary antibody (Proteintech, #26972) on a shaker at room temperature overnight.

Techniques: Staining

Example confocal images showing spinal cord dorsal horn staining for Trpv1 and cholera toxin B injected into the paw in Control (top) and PAM VGLUT2 cDKO mice (bottom).

Journal: bioRxiv

Article Title: Nociceptors use multiple neurotransmitters to drive pain

doi: 10.1101/2025.09.09.675093

Figure Lengend Snippet: Example confocal images showing spinal cord dorsal horn staining for Trpv1 and cholera toxin B injected into the paw in Control (top) and PAM VGLUT2 cDKO mice (bottom).

Article Snippet: Afterward, sections were incubated in blocking solution containing a subset of the following primary antibodies: 1:500 or 1.1000 goat anti-CGRP polyclonal primary antibody (Abcam, #ab36001), 1:500 rat anti-Substance P polyclonal primary antibody (Abcam, #ab67006), 1:500 rabbit anti-TRPV1 polyclonal primary antibody (Alomone Labs, #ACC-030), 1:500 chicken anti-Peripherin polyclonal primary antibody (Invitrogen, #PA1-10012), 1:1000 guinea pig anti-VGlut2 polyclonal primary antibody (Millpore Sigma, #AB2251-I), and 1:1500 rabbit anti-PAM polyclonal primary antibody (Proteintech, #26972) on a shaker at room temperature overnight.

Techniques: Staining, Injection, Control