Anti trpc3

Manufactured by Alomone

Sourced in Israel

Anti-TRPC3 is a selective inhibitor of the TRPC3 channel. TRPC3 is a member of the transient receptor potential (TRP) channel family and plays a role in calcium signaling.

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Lab products found in correlation

Anti trpc6, by Alomone (5 mentions) Anti stim1, by Abcam (3 mentions) Anti α actin, by Abcam (3 mentions) Anti orai1, by Abcam (3 mentions) Anti dhpr, by Abcam (3 mentions) Anti trpc1, by Alomone (3 mentions) Anti trpc4, by Alomone (3 mentions) Anti gapdh, by Santa Cruz Biotechnology (3 mentions) Anti ryr1, by Thermo Fisher Scientific (3 mentions) Anti serca1a, by Thermo Fisher Scientific (3 mentions) Anti jp1, by Thermo Fisher Scientific (3 mentions) Anti jp2, by Thermo Fisher Scientific (3 mentions) Anti stim2, by Abcam (2 mentions) Anti cam1, by Thermo Fisher Scientific (2 mentions) Collagenase type 2, by Worthington (1 mentions) Recombinant human tgf β1, by Cell Signaling Technology (1 mentions) Anti akt, by Cell Signaling Technology (1 mentions) Anti snail1, by Cell Signaling Technology (1 mentions) Anti aqp1, by Proteintech (1 mentions) Anti e cad, by Cell Signaling Technology (1 mentions)

Spelling variants of this product

TRPC3 (4 citations) Rabbit anti-TRPC3 (3 citations) Anti-TRPC3 antibody (2 citations)

8 protocols using anti trpc3

Antibody Identification for Kidney Research

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Sources of antibodies and reagents were as follows:
Anti-AKT (Cell Signaling Technology, Danvers, MA, USA), anti-p-AKT (Ser473) (Cell Signaling Technology, Danvers, MA, USA), anti-p-ERK1/2 (Cell Signaling Technology, Danvers, MA, USA), anti-ERK1/2 (Cell Signaling Technology, Danvers, MA, USA), anti-p-mTOR (Cell Signaling Technology, Danvers, MA, USA), anti-mTOR (Cell Signaling Technology, Danvers, MA, USA), anti-E-cad (Cell Signaling Technology, Danvers, MA, USA), anti-Cadh16 (Proteintech, Chicago, Illinois, USA), anti-snail1(Cell Signaling Technology:3879s), anti-α-SMA (Boster, Wuhan, Hubei, China), anti-AQP1 (Proteintech, Chicago, Illinois, USA), anti-ATP (Proteintech, Chicago, Illinois, USA), anti-TGF-β1 (Proteintech, Chicago, Illinois, USA), anti-GAPDH (Proteintech, Chicago, Illinois, USA), anti-TRPC6 (Alomone, Jerusalem, Israel), anti-TRPC3 (Alomone:ACC-016), anti-mouse IgG (KeRui, Wuhan, Hubei, China), anti-rabbit IgG antibody (KeRui, Wuhan, Hubei, China), recombinant human TGF-β1 (Cell Signaling Technology, Danvers, MA, USA), HYP9 (MedChem, Shanghai, China), and type-2 collagenase (Worthington Biochemical Corporation, Lakewood, Colorado, USA).
DMEM/f12 and FBS were purchased from Invitrogen (Chicago, California, USA). The whole sagittal section of the kidney was scanned by Biossci Biotechnology Company (Wuhan, Hubei, China).

Zhang Y., Yin N., Sun A., Wu Q., Hu W., Hou X., Zeng X., Zhu M, & Liao Y. (2021). Transient Receptor Potential Channel 6 Knockout Ameliorates Kidney Fibrosis by Inhibition of Epithelial–Mesenchymal Transition. Frontiers in Cell and Developmental Biology, 8, 602703.

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Protein Interactions in Muscle Differentiation

Cited 4 times

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Mouse primary skeletal myotubes were solubilized in lysis buffer, as previously described [10 (link),22 (link),38 (link),41 (link),42 (link),44 (link)]. For the coimmunoprecipitation assay [22 (link),41 (link),42 (link),44 (link)], solubilized myotube lysate (100 µg of total protein) and anti-CASQ1 (Affinity BioReagents, Golden, CO, USA) or anit-Orai1 antibody (Abcam, Cambridge, MA, USA) were used. The immunoprecipitate was subjected to immunoblot assays with anti-CASQ1, anti-Orai1, or anti-STIM2 antibody (Abcam). For the immunoblot assay, solubilized myotube lysate (10 μg of total protein) was subjected to SDS–PAGE (8, 10, or 12% gel) [10 (link),22 (link),38 (link),41 (link),42 (link),44 (link),46 (link)]. The anti-RyR1, anti-SERCA1a, anti-CASQ1, anti-CaM1, anti-JP1, and anti-JP2 antibodies were obtained from Affinity BioReagents. The anti-TRPC1, anti-TRPC3, anti-TRPC4, and anti-TRPC6 antibodies were obtained from Alomone Laboratories (Jerusalem, Israel). The anti-TRIM32, anti-MyoD, and anti-myogenin antibodies were obtained from Santa Cruz Biotechnology (Dallas, TX, USA). The anti-DHPR, anti-STIM1, anti-STIM2, and anti-α-actin antibodies were obtained from Abcam.

Jeong S.Y., Oh M.R., Choi J.H., Woo J.S, & Lee E.H. (2021). Calsequestrin 1 Is an Active Partner of Stromal Interaction Molecule 2 in Skeletal Muscle. Cells, 10(11), 2821.

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Molecular Pathways of TGF-β1-Induced Fibrosis

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Human TGFβ1 (Solarbio, No. P00121) was suspended as recommended by the manufacturer, at 10 μg/mL stock concentration. Aliquots were kept frozen at −20°C until used. TRPC3 specific inhibitor Pyr3 was purchased from Sigma-Aldrich (St. Louis, MO).
Western blot assays were conducted as previously described [19 (link), 20 (link)]. The primary antibodies included anti-TRPC3 from Alomone Labs (Jerusalem, Israel); anti-TGFβ1 and anti-αSMA from Abcam (Cambridge, UK); anti-fibronectin, anti-NOX4, anti-phosphorylated Smad2/3 (pSmad2/3), anti-Smad2/3, and anti-GAPDH from Santa Cruz Biotechnology (Dallas, TX); anti-Col1a1 from Cell Signaling Technology; and antiphosphorylated pyruvate dehydrogenase E1a subunit (PDHE1a) (p-PDHE1α) from Merck-Millipore (Darmstadt, Germany).

Xia W., Wang Q., Lu Y., Hu Y., Zhang X., Zhang J., Liu D., Song J., Zhu Z., Liu D, & Zhang H. (2020). Transient Receptor Potential Channel Canonical Type 3 Deficiency Antagonizes Myofibroblast Transdifferentiation In Vivo. BioMed Research International, 2020, 1202189.

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Co-immunoprecipitation and Immunoblot Assays

Cited 3 times

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For the co-immunoprecipitation assay, the solubilized triad sample (50 µg of total protein) was incubated with anti-STIM2 antibody (Sigma-Aldrich) overnight at 4 °C, as previously described^{26 (link),80 (link),81 (link),83 (link)}. Anti-STIM1 (Abcam, Cambridge, MA, USA), anti-SERCA1a (Thermo Scientific Inc., Rockford, IL, USA), or anti-TRPC6 (Alomone Laboratories, Jerusalem 9104201, Israel) antibody was used for immunoblot assay. For the immunoblot assay, fully differentiated mouse primary skeletal myotubes on 10-cm plates on differentiation day 5 were solubilized, and the solubilized lysate (5 or 10 μg of total protein) was subjected to SDS-PAGE (8, 10, or 12% gel) and immunoblot assay, as previously described^{15 (link),26 (link),45 (link),80 (link),83 (link),87 (link)}. Anti-RyR1, anti-CSQ, anti-CaM1, anti-JP1, and anti-JP2 antibodies were obtained from Thermo Scientific Inc. Anti-TRPC1, anti-TRPC3, and anti-TRPC4 antibodies were obtained from Alomone Laboratories. Anti-DHPR, anti-Orai1, and anti-α-actin antibodies were obtained from Abcam. Horseradish peroxidase-conjugated anti-goat, anti-mouse, or anti-rabbit secondary antibodies were obtained from Jackson ImmunoResearch Laboratories (West Grove, PA, USA). The membranes were washed three times with PBS and developed using a SuperSignal Ultra Chemiluminescent substrate (Pierce, Rockford, IL, USA).

Oh M.R., Lee K.J., Huang M., Kim J.O., Kim D.H., Cho C.H, & Lee E.H. (2017). STIM2 regulates both intracellular Ca2+ distribution and Ca2+ movement in skeletal myotubes. Scientific Reports, 7, 17936.

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Western Blotting of TRPC3 Protein

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Western blotting was conducted as previously described.23 (link) Briefly, total proteins were extracted from cells or tissues and 30 to 60 μg proteins were loaded on gels and separated by electrophoresis. Then, the proteins were transferred to PVDF membranes, blocked and incubated with the corresponding primary and secondary antibodies. The final detection was performed using an electrochemiluminescence substrate (Merck-Millipore, Darmstadt, Germany). The primary antibodies used were anti-TRPC3 (Alomone Labs, Jerusalem, Israel) and anti-GAPDH (Santa Cruz Biotechnology, Dallas, TX, USA).

Liu Y., Liu X., Zhang X., Deng J., Zhang J, & Xing H. (2020). lncRNA DLX6-AS1 Promotes Proliferation of Laryngeal Cancer Cells by Targeting the miR-26a/TRPC3 Pathway. Cancer Management and Research, 12, 2685-2695.

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Western Blot Protein Quantification

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Western blot assays were performed as described earlier [19 ]. A buffer was used to lyse cells or tissues, followed by 20 min of freezing at −20 °C. Insoluble debris from the sample was removed by centrifuging it at 12000×g at 4 °C for 20 min. Next, the supernatant samples were collected, and protein levels were calculated by the Bradford method (Bio-Rad Protein Assay). The gray value of Western blot was quantified and normalized to the internal reference (GAPDH or Actin) with ImageJ software (NIH). We utilized the following primary antibodies: anti-α-smooth muscle actin (1:1000, ab7817); anti-TRPC3 (1:1000, Alomone, ACC-016); anti-collagen I (1:1000, Cell Signaling Technology, ^#84336); anti-MLC (1:1000, Cell Signaling Technology, ^#3675); anti-pMLC (1:1000, Cell Signaling Technology, ^#3672); anti-MYPT1 (1:1000, Santa Cruz Biotechnology, Sc-51426); anti-pMYPT1 (Santa Cruz Biotechnology, Sc-33360); anti-Fibronectin (1:1000, Abcam, ab268020); anti-phosphorylated Ser695 pyruvate dehydrogenase E1a subunit (PDHE1a) anti-pPDHE1a (1:1000, Merck-Millipore) and anti-GAPDH from Santa Cruz Biotechnology.

Xia W., Wang Q., Lin S., Wang Y., Zhang J., Wang H., Yang X., Hu Y., Liang H., Lu Y., Zhu Z, & Liu D. (2023). A high-salt diet promotes hypertrophic scarring through TRPC3-mediated mitochondrial Ca2+ homeostasis dysfunction. Heliyon, 9(8), e18629.

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Co-immunoprecipitation Assay of Mouse Myotubes

Cited 3 times

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Mouse primary skeletal myotubes were solubilized in lysis buffer, as previously described^{6 (link),20 (link),27 (link),40 (link),63 (link),64 (link)}. For the co-immunoprecipitation assay^{20 (link),40 (link),63 (link)}, solubilized myotube lysate (80 or 100 µg of total protein) was used. The immunoprecipitate was subjected to immunoblot assays with anti-DHPR, anti-STIM1, or anti-GFP antibody (Abcam, Cambridge, MA, U.S.A., for detecting CFP-R429C). For the immunoblot assays, the solubilized myotube lysate (10 μg of total protein) was subjected to SDS-PAGE (8, 10, or 12% gel)^{6 (link),20 (link),27 (link),40 (link),63 (link),64 (link)}. Anti-RyR1, anti-SERCA1a, anti-CSQ1, anti-CaM1, anti-MG29, anti-MG53, anti-JP1, and anti-JP2 antibodies were obtained from Affinity BioReagents (Golden, CO, U.S.A.). Anti-TRPC1, anti-TRPC3, anti-TRPC4, and anti-TRPC6 antibodies were obtained from Alomone Laboratories (Jerusalem, Israel). Anti-Orai1, anti-STIM1, anti-STIM2, and anti-α-actin antibodies were obtained from Abcam. Anti-Drp-1, anti-Mfn1, anti-calcineurin and anti-CaMKII antibodies were obtained from Santa Cruz Biotechnology (Paso Robles, CA, U.S.A.).

Choi J.H., Huang M., Hyun C., Oh M.R., Lee K.J., Cho C.H, & Lee E.H. (2019). A muscular hypotonia-associated STIM1 mutant at R429 induces abnormalities in intracellular Ca2+ movement and extracellular Ca2+ entry in skeletal muscle. Scientific Reports, 9, 19140.

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Immunoblot Analysis of Renal Cortex

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Immunoblot of the renal cortex was carried out as described previously [13 (link)]. Monoclonal antibodies used in this study were: mouse anti-α-smooth muscle actin (α-SMA) clone 1 A4, used at a dilution of 1:1000, from Sigma-Aldrich, St. Louis, MO, USA; mouse anti-vimentin (used at 1:1000) from Dako Inc., Santa Clara, CA, USA; mouse anti-TRPC5 (used at 1:100) from NeuroMAB, Davis, CA, USA; mouse anti-pro-interleukin−1β (used at 1:1000) from Santa Cruz Biotechnology, Santa Cruz, CA, USA. Polyclonal anti-rabbit NLRP3 (used at 1:1000) was from Abcam (Cambridge, MA, USA; anti-TRPC6 (used at 1:1000), and anti-TRPC3 (used at 1:1000) was from Alomone Laboratories (Jerusalem, Israel). All experiments were quantified by densitometry using Image J™ software. Type I procollagen levels in serum were determined using a commercial assay (LSBio, Inc., Seattle, WA, USA) according to the manufacturer’s instructions. β2–microglobulin (β2–MG) levels in the urine were assessed using an assay from ICL Lab (Portland OR, USA). Albumin was measured in 24-h urine samples using a kit from Ethos Biosciences (Philadelphia, PA, USA).

Kim E.Y, & Dryer S.E. (2021). Effects of TRPC6 Inactivation on Glomerulosclerosis and Renal Fibrosis in Aging Rats. Cells, 10(4), 856.

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