ryr3  (Alomone Labs)


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    Alomone Labs ryr3
    Identification of an SMC-specific <t>Ryr3</t> regulated by SRF. (A) A genomic map view of Ryr3 variants expressed in JSMCs and CSMCs. Three variants TCONS_00167498 (V498, blue), TCONS_00152671 (V671, green), and TCONS_00166589 (V589, red) are indicated by arrows. (B) Expression levels of total Ryr3 in SMCs. (C) Expression levels of each Ryr3 vaiant in SMCs. Variants are arranged on the X-axis from longest (left) to shortest (right) in length. The three variants shown on A are also indicated by the color arrows. (D) A topological map of RYR3 variants. Each circle denotes the corresponding amino acid. Colors on amino acid sequence show distinct regions and domains: red, missing or inserted peptides from differentially spliced exons; green, start codons found in differentially spliced variants. Seven transmembrane domains 1–7 and a pore region (magenta) are shown. MR1-5 (blue), SPRY1-3 (dark green), FKBP1A (orange), CALM (purple), and a residue E (black) that is required for Ca 2+ binding (Ca 2+ ) are also indicated. The topology map was drawn based on the longest peptide variant V498. V671 is a C-terminal truncated variant (V671CT) that is missing Ca 2+ binding and transmembrane domains after the CALM domain while V589 is an N-terminal truncated variant (V589NT) that is missing the N-terminal domains (N-ter to CALM domain). (E) Western blot showing that RYR3 protein expression decreased in jejunum SM of inducible SMC-specific Srf KO mice as SRF protein was depleted 5, 10, 15, and 20 days following tamoxifen administration. UBE1 was used as an endogenous control.
    Ryr3, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 86/100, based on 15 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ryr3/product/Alomone Labs
    Average 86 stars, based on 15 article reviews
    Price from $9.99 to $1999.99
    ryr3 - by Bioz Stars, 2022-12
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    Images

    1) Product Images from "Smooth Muscle Cell Genome Browser: Enabling the Identification of Novel Serum Response Factor Target Genes"

    Article Title: Smooth Muscle Cell Genome Browser: Enabling the Identification of Novel Serum Response Factor Target Genes

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0133751

    Identification of an SMC-specific Ryr3 regulated by SRF. (A) A genomic map view of Ryr3 variants expressed in JSMCs and CSMCs. Three variants TCONS_00167498 (V498, blue), TCONS_00152671 (V671, green), and TCONS_00166589 (V589, red) are indicated by arrows. (B) Expression levels of total Ryr3 in SMCs. (C) Expression levels of each Ryr3 vaiant in SMCs. Variants are arranged on the X-axis from longest (left) to shortest (right) in length. The three variants shown on A are also indicated by the color arrows. (D) A topological map of RYR3 variants. Each circle denotes the corresponding amino acid. Colors on amino acid sequence show distinct regions and domains: red, missing or inserted peptides from differentially spliced exons; green, start codons found in differentially spliced variants. Seven transmembrane domains 1–7 and a pore region (magenta) are shown. MR1-5 (blue), SPRY1-3 (dark green), FKBP1A (orange), CALM (purple), and a residue E (black) that is required for Ca 2+ binding (Ca 2+ ) are also indicated. The topology map was drawn based on the longest peptide variant V498. V671 is a C-terminal truncated variant (V671CT) that is missing Ca 2+ binding and transmembrane domains after the CALM domain while V589 is an N-terminal truncated variant (V589NT) that is missing the N-terminal domains (N-ter to CALM domain). (E) Western blot showing that RYR3 protein expression decreased in jejunum SM of inducible SMC-specific Srf KO mice as SRF protein was depleted 5, 10, 15, and 20 days following tamoxifen administration. UBE1 was used as an endogenous control.
    Figure Legend Snippet: Identification of an SMC-specific Ryr3 regulated by SRF. (A) A genomic map view of Ryr3 variants expressed in JSMCs and CSMCs. Three variants TCONS_00167498 (V498, blue), TCONS_00152671 (V671, green), and TCONS_00166589 (V589, red) are indicated by arrows. (B) Expression levels of total Ryr3 in SMCs. (C) Expression levels of each Ryr3 vaiant in SMCs. Variants are arranged on the X-axis from longest (left) to shortest (right) in length. The three variants shown on A are also indicated by the color arrows. (D) A topological map of RYR3 variants. Each circle denotes the corresponding amino acid. Colors on amino acid sequence show distinct regions and domains: red, missing or inserted peptides from differentially spliced exons; green, start codons found in differentially spliced variants. Seven transmembrane domains 1–7 and a pore region (magenta) are shown. MR1-5 (blue), SPRY1-3 (dark green), FKBP1A (orange), CALM (purple), and a residue E (black) that is required for Ca 2+ binding (Ca 2+ ) are also indicated. The topology map was drawn based on the longest peptide variant V498. V671 is a C-terminal truncated variant (V671CT) that is missing Ca 2+ binding and transmembrane domains after the CALM domain while V589 is an N-terminal truncated variant (V589NT) that is missing the N-terminal domains (N-ter to CALM domain). (E) Western blot showing that RYR3 protein expression decreased in jejunum SM of inducible SMC-specific Srf KO mice as SRF protein was depleted 5, 10, 15, and 20 days following tamoxifen administration. UBE1 was used as an endogenous control.

    Techniques Used: Expressing, Sequencing, Binding Assay, Variant Assay, Western Blot, Mouse Assay

    2) Product Images from "Smooth Muscle Cell Genome Browser: Enabling the Identification of Novel Serum Response Factor Target Genes"

    Article Title: Smooth Muscle Cell Genome Browser: Enabling the Identification of Novel Serum Response Factor Target Genes

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0133751

    Identification of an SMC-specific Ryr3 regulated by SRF. (A) A genomic map view of Ryr3 variants expressed in JSMCs and CSMCs. Three variants TCONS_00167498 (V498, blue), TCONS_00152671 (V671, green), and TCONS_00166589 (V589, red) are indicated by arrows. (B) Expression levels of total Ryr3 in SMCs. (C) Expression levels of each Ryr3 vaiant in SMCs. Variants are arranged on the X-axis from longest (left) to shortest (right) in length. The three variants shown on A are also indicated by the color arrows. (D) A topological map of RYR3 variants. Each circle denotes the corresponding amino acid. Colors on amino acid sequence show distinct regions and domains: red, missing or inserted peptides from differentially spliced exons; green, start codons found in differentially spliced variants. Seven transmembrane domains 1–7 and a pore region (magenta) are shown. MR1-5 (blue), SPRY1-3 (dark green), FKBP1A (orange), CALM (purple), and a residue E (black) that is required for Ca 2+ binding (Ca 2+ ) are also indicated. The topology map was drawn based on the longest peptide variant V498. V671 is a C-terminal truncated variant (V671CT) that is missing Ca 2+ binding and transmembrane domains after the CALM domain while V589 is an N-terminal truncated variant (V589NT) that is missing the N-terminal domains (N-ter to CALM domain). (E) Western blot showing that RYR3 protein expression decreased in jejunum SM of inducible SMC-specific Srf KO mice as SRF protein was depleted 5, 10, 15, and 20 days following tamoxifen administration. UBE1 was used as an endogenous control.
    Figure Legend Snippet: Identification of an SMC-specific Ryr3 regulated by SRF. (A) A genomic map view of Ryr3 variants expressed in JSMCs and CSMCs. Three variants TCONS_00167498 (V498, blue), TCONS_00152671 (V671, green), and TCONS_00166589 (V589, red) are indicated by arrows. (B) Expression levels of total Ryr3 in SMCs. (C) Expression levels of each Ryr3 vaiant in SMCs. Variants are arranged on the X-axis from longest (left) to shortest (right) in length. The three variants shown on A are also indicated by the color arrows. (D) A topological map of RYR3 variants. Each circle denotes the corresponding amino acid. Colors on amino acid sequence show distinct regions and domains: red, missing or inserted peptides from differentially spliced exons; green, start codons found in differentially spliced variants. Seven transmembrane domains 1–7 and a pore region (magenta) are shown. MR1-5 (blue), SPRY1-3 (dark green), FKBP1A (orange), CALM (purple), and a residue E (black) that is required for Ca 2+ binding (Ca 2+ ) are also indicated. The topology map was drawn based on the longest peptide variant V498. V671 is a C-terminal truncated variant (V671CT) that is missing Ca 2+ binding and transmembrane domains after the CALM domain while V589 is an N-terminal truncated variant (V589NT) that is missing the N-terminal domains (N-ter to CALM domain). (E) Western blot showing that RYR3 protein expression decreased in jejunum SM of inducible SMC-specific Srf KO mice as SRF protein was depleted 5, 10, 15, and 20 days following tamoxifen administration. UBE1 was used as an endogenous control.

    Techniques Used: Expressing, Sequencing, Binding Assay, Variant Assay, Western Blot, Mouse Assay

    3) Product Images from "Smooth Muscle Cell Genome Browser: Enabling the Identification of Novel Serum Response Factor Target Genes"

    Article Title: Smooth Muscle Cell Genome Browser: Enabling the Identification of Novel Serum Response Factor Target Genes

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0133751

    Identification of an SMC-specific Ryr3 regulated by SRF. (A) A genomic map view of Ryr3 variants expressed in JSMCs and CSMCs. Three variants TCONS_00167498 (V498, blue), TCONS_00152671 (V671, green), and TCONS_00166589 (V589, red) are indicated by arrows. (B) Expression levels of total Ryr3 in SMCs. (C) Expression levels of each Ryr3 vaiant in SMCs. Variants are arranged on the X-axis from longest (left) to shortest (right) in length. The three variants shown on A are also indicated by the color arrows. (D) A topological map of RYR3 variants. Each circle denotes the corresponding amino acid. Colors on amino acid sequence show distinct regions and domains: red, missing or inserted peptides from differentially spliced exons; green, start codons found in differentially spliced variants. Seven transmembrane domains 1–7 and a pore region (magenta) are shown. MR1-5 (blue), SPRY1-3 (dark green), FKBP1A (orange), CALM (purple), and a residue E (black) that is required for Ca 2+ binding (Ca 2+ ) are also indicated. The topology map was drawn based on the longest peptide variant V498. V671 is a C-terminal truncated variant (V671CT) that is missing Ca 2+ binding and transmembrane domains after the CALM domain while V589 is an N-terminal truncated variant (V589NT) that is missing the N-terminal domains (N-ter to CALM domain). (E) Western blot showing that RYR3 protein expression decreased in jejunum SM of inducible SMC-specific Srf KO mice as SRF protein was depleted 5, 10, 15, and 20 days following tamoxifen administration. UBE1 was used as an endogenous control.
    Figure Legend Snippet: Identification of an SMC-specific Ryr3 regulated by SRF. (A) A genomic map view of Ryr3 variants expressed in JSMCs and CSMCs. Three variants TCONS_00167498 (V498, blue), TCONS_00152671 (V671, green), and TCONS_00166589 (V589, red) are indicated by arrows. (B) Expression levels of total Ryr3 in SMCs. (C) Expression levels of each Ryr3 vaiant in SMCs. Variants are arranged on the X-axis from longest (left) to shortest (right) in length. The three variants shown on A are also indicated by the color arrows. (D) A topological map of RYR3 variants. Each circle denotes the corresponding amino acid. Colors on amino acid sequence show distinct regions and domains: red, missing or inserted peptides from differentially spliced exons; green, start codons found in differentially spliced variants. Seven transmembrane domains 1–7 and a pore region (magenta) are shown. MR1-5 (blue), SPRY1-3 (dark green), FKBP1A (orange), CALM (purple), and a residue E (black) that is required for Ca 2+ binding (Ca 2+ ) are also indicated. The topology map was drawn based on the longest peptide variant V498. V671 is a C-terminal truncated variant (V671CT) that is missing Ca 2+ binding and transmembrane domains after the CALM domain while V589 is an N-terminal truncated variant (V589NT) that is missing the N-terminal domains (N-ter to CALM domain). (E) Western blot showing that RYR3 protein expression decreased in jejunum SM of inducible SMC-specific Srf KO mice as SRF protein was depleted 5, 10, 15, and 20 days following tamoxifen administration. UBE1 was used as an endogenous control.

    Techniques Used: Expressing, Sequencing, Binding Assay, Variant Assay, Western Blot, Mouse Assay

    4) Product Images from "Smooth Muscle Cell Genome Browser: Enabling the Identification of Novel Serum Response Factor Target Genes"

    Article Title: Smooth Muscle Cell Genome Browser: Enabling the Identification of Novel Serum Response Factor Target Genes

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0133751

    Identification of an SMC-specific Ryr3 regulated by SRF. (A) A genomic map view of Ryr3 variants expressed in JSMCs and CSMCs. Three variants TCONS_00167498 (V498, blue), TCONS_00152671 (V671, green), and TCONS_00166589 (V589, red) are indicated by arrows. (B) Expression levels of total Ryr3 in SMCs. (C) Expression levels of each Ryr3 vaiant in SMCs. Variants are arranged on the X-axis from longest (left) to shortest (right) in length. The three variants shown on A are also indicated by the color arrows. (D) A topological map of RYR3 variants. Each circle denotes the corresponding amino acid. Colors on amino acid sequence show distinct regions and domains: red, missing or inserted peptides from differentially spliced exons; green, start codons found in differentially spliced variants. Seven transmembrane domains 1–7 and a pore region (magenta) are shown. MR1-5 (blue), SPRY1-3 (dark green), FKBP1A (orange), CALM (purple), and a residue E (black) that is required for Ca 2+ binding (Ca 2+ ) are also indicated. The topology map was drawn based on the longest peptide variant V498. V671 is a C-terminal truncated variant (V671CT) that is missing Ca 2+ binding and transmembrane domains after the CALM domain while V589 is an N-terminal truncated variant (V589NT) that is missing the N-terminal domains (N-ter to CALM domain). (E) Western blot showing that RYR3 protein expression decreased in jejunum SM of inducible SMC-specific Srf KO mice as SRF protein was depleted 5, 10, 15, and 20 days following tamoxifen administration. UBE1 was used as an endogenous control.
    Figure Legend Snippet: Identification of an SMC-specific Ryr3 regulated by SRF. (A) A genomic map view of Ryr3 variants expressed in JSMCs and CSMCs. Three variants TCONS_00167498 (V498, blue), TCONS_00152671 (V671, green), and TCONS_00166589 (V589, red) are indicated by arrows. (B) Expression levels of total Ryr3 in SMCs. (C) Expression levels of each Ryr3 vaiant in SMCs. Variants are arranged on the X-axis from longest (left) to shortest (right) in length. The three variants shown on A are also indicated by the color arrows. (D) A topological map of RYR3 variants. Each circle denotes the corresponding amino acid. Colors on amino acid sequence show distinct regions and domains: red, missing or inserted peptides from differentially spliced exons; green, start codons found in differentially spliced variants. Seven transmembrane domains 1–7 and a pore region (magenta) are shown. MR1-5 (blue), SPRY1-3 (dark green), FKBP1A (orange), CALM (purple), and a residue E (black) that is required for Ca 2+ binding (Ca 2+ ) are also indicated. The topology map was drawn based on the longest peptide variant V498. V671 is a C-terminal truncated variant (V671CT) that is missing Ca 2+ binding and transmembrane domains after the CALM domain while V589 is an N-terminal truncated variant (V589NT) that is missing the N-terminal domains (N-ter to CALM domain). (E) Western blot showing that RYR3 protein expression decreased in jejunum SM of inducible SMC-specific Srf KO mice as SRF protein was depleted 5, 10, 15, and 20 days following tamoxifen administration. UBE1 was used as an endogenous control.

    Techniques Used: Expressing, Sequencing, Binding Assay, Variant Assay, Western Blot, Mouse Assay

    5) Product Images from "Smooth Muscle Cell Genome Browser: Enabling the Identification of Novel Serum Response Factor Target Genes"

    Article Title: Smooth Muscle Cell Genome Browser: Enabling the Identification of Novel Serum Response Factor Target Genes

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0133751

    Identification of an SMC-specific Ryr3 regulated by SRF. (A) A genomic map view of Ryr3 variants expressed in JSMCs and CSMCs. Three variants TCONS_00167498 (V498, blue), TCONS_00152671 (V671, green), and TCONS_00166589 (V589, red) are indicated by arrows. (B) Expression levels of total Ryr3 in SMCs. (C) Expression levels of each Ryr3 vaiant in SMCs. Variants are arranged on the X-axis from longest (left) to shortest (right) in length. The three variants shown on A are also indicated by the color arrows. (D) A topological map of RYR3 variants. Each circle denotes the corresponding amino acid. Colors on amino acid sequence show distinct regions and domains: red, missing or inserted peptides from differentially spliced exons; green, start codons found in differentially spliced variants. Seven transmembrane domains 1–7 and a pore region (magenta) are shown. MR1-5 (blue), SPRY1-3 (dark green), FKBP1A (orange), CALM (purple), and a residue E (black) that is required for Ca 2+ binding (Ca 2+ ) are also indicated. The topology map was drawn based on the longest peptide variant V498. V671 is a C-terminal truncated variant (V671CT) that is missing Ca 2+ binding and transmembrane domains after the CALM domain while V589 is an N-terminal truncated variant (V589NT) that is missing the N-terminal domains (N-ter to CALM domain). (E) Western blot showing that RYR3 protein expression decreased in jejunum SM of inducible SMC-specific Srf KO mice as SRF protein was depleted 5, 10, 15, and 20 days following tamoxifen administration. UBE1 was used as an endogenous control.
    Figure Legend Snippet: Identification of an SMC-specific Ryr3 regulated by SRF. (A) A genomic map view of Ryr3 variants expressed in JSMCs and CSMCs. Three variants TCONS_00167498 (V498, blue), TCONS_00152671 (V671, green), and TCONS_00166589 (V589, red) are indicated by arrows. (B) Expression levels of total Ryr3 in SMCs. (C) Expression levels of each Ryr3 vaiant in SMCs. Variants are arranged on the X-axis from longest (left) to shortest (right) in length. The three variants shown on A are also indicated by the color arrows. (D) A topological map of RYR3 variants. Each circle denotes the corresponding amino acid. Colors on amino acid sequence show distinct regions and domains: red, missing or inserted peptides from differentially spliced exons; green, start codons found in differentially spliced variants. Seven transmembrane domains 1–7 and a pore region (magenta) are shown. MR1-5 (blue), SPRY1-3 (dark green), FKBP1A (orange), CALM (purple), and a residue E (black) that is required for Ca 2+ binding (Ca 2+ ) are also indicated. The topology map was drawn based on the longest peptide variant V498. V671 is a C-terminal truncated variant (V671CT) that is missing Ca 2+ binding and transmembrane domains after the CALM domain while V589 is an N-terminal truncated variant (V589NT) that is missing the N-terminal domains (N-ter to CALM domain). (E) Western blot showing that RYR3 protein expression decreased in jejunum SM of inducible SMC-specific Srf KO mice as SRF protein was depleted 5, 10, 15, and 20 days following tamoxifen administration. UBE1 was used as an endogenous control.

    Techniques Used: Expressing, Sequencing, Binding Assay, Variant Assay, Western Blot, Mouse Assay

    6) Product Images from "Smooth Muscle Cell Genome Browser: Enabling the Identification of Novel Serum Response Factor Target Genes"

    Article Title: Smooth Muscle Cell Genome Browser: Enabling the Identification of Novel Serum Response Factor Target Genes

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0133751

    Identification of an SMC-specific Ryr3 regulated by SRF. (A) A genomic map view of Ryr3 variants expressed in JSMCs and CSMCs. Three variants TCONS_00167498 (V498, blue), TCONS_00152671 (V671, green), and TCONS_00166589 (V589, red) are indicated by arrows. (B) Expression levels of total Ryr3 in SMCs. (C) Expression levels of each Ryr3 vaiant in SMCs. Variants are arranged on the X-axis from longest (left) to shortest (right) in length. The three variants shown on A are also indicated by the color arrows. (D) A topological map of RYR3 variants. Each circle denotes the corresponding amino acid. Colors on amino acid sequence show distinct regions and domains: red, missing or inserted peptides from differentially spliced exons; green, start codons found in differentially spliced variants. Seven transmembrane domains 1–7 and a pore region (magenta) are shown. MR1-5 (blue), SPRY1-3 (dark green), FKBP1A (orange), CALM (purple), and a residue E (black) that is required for Ca 2+ binding (Ca 2+ ) are also indicated. The topology map was drawn based on the longest peptide variant V498. V671 is a C-terminal truncated variant (V671CT) that is missing Ca 2+ binding and transmembrane domains after the CALM domain while V589 is an N-terminal truncated variant (V589NT) that is missing the N-terminal domains (N-ter to CALM domain). (E) Western blot showing that RYR3 protein expression decreased in jejunum SM of inducible SMC-specific Srf KO mice as SRF protein was depleted 5, 10, 15, and 20 days following tamoxifen administration. UBE1 was used as an endogenous control.
    Figure Legend Snippet: Identification of an SMC-specific Ryr3 regulated by SRF. (A) A genomic map view of Ryr3 variants expressed in JSMCs and CSMCs. Three variants TCONS_00167498 (V498, blue), TCONS_00152671 (V671, green), and TCONS_00166589 (V589, red) are indicated by arrows. (B) Expression levels of total Ryr3 in SMCs. (C) Expression levels of each Ryr3 vaiant in SMCs. Variants are arranged on the X-axis from longest (left) to shortest (right) in length. The three variants shown on A are also indicated by the color arrows. (D) A topological map of RYR3 variants. Each circle denotes the corresponding amino acid. Colors on amino acid sequence show distinct regions and domains: red, missing or inserted peptides from differentially spliced exons; green, start codons found in differentially spliced variants. Seven transmembrane domains 1–7 and a pore region (magenta) are shown. MR1-5 (blue), SPRY1-3 (dark green), FKBP1A (orange), CALM (purple), and a residue E (black) that is required for Ca 2+ binding (Ca 2+ ) are also indicated. The topology map was drawn based on the longest peptide variant V498. V671 is a C-terminal truncated variant (V671CT) that is missing Ca 2+ binding and transmembrane domains after the CALM domain while V589 is an N-terminal truncated variant (V589NT) that is missing the N-terminal domains (N-ter to CALM domain). (E) Western blot showing that RYR3 protein expression decreased in jejunum SM of inducible SMC-specific Srf KO mice as SRF protein was depleted 5, 10, 15, and 20 days following tamoxifen administration. UBE1 was used as an endogenous control.

    Techniques Used: Expressing, Sequencing, Binding Assay, Variant Assay, Western Blot, Mouse Assay

    7) Product Images from "Smooth Muscle Cell Genome Browser: Enabling the Identification of Novel Serum Response Factor Target Genes"

    Article Title: Smooth Muscle Cell Genome Browser: Enabling the Identification of Novel Serum Response Factor Target Genes

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0133751

    Identification of an SMC-specific Ryr3 regulated by SRF. (A) A genomic map view of Ryr3 variants expressed in JSMCs and CSMCs. Three variants TCONS_00167498 (V498, blue), TCONS_00152671 (V671, green), and TCONS_00166589 (V589, red) are indicated by arrows. (B) Expression levels of total Ryr3 in SMCs. (C) Expression levels of each Ryr3 vaiant in SMCs. Variants are arranged on the X-axis from longest (left) to shortest (right) in length. The three variants shown on A are also indicated by the color arrows. (D) A topological map of RYR3 variants. Each circle denotes the corresponding amino acid. Colors on amino acid sequence show distinct regions and domains: red, missing or inserted peptides from differentially spliced exons; green, start codons found in differentially spliced variants. Seven transmembrane domains 1–7 and a pore region (magenta) are shown. MR1-5 (blue), SPRY1-3 (dark green), FKBP1A (orange), CALM (purple), and a residue E (black) that is required for Ca 2+ binding (Ca 2+ ) are also indicated. The topology map was drawn based on the longest peptide variant V498. V671 is a C-terminal truncated variant (V671CT) that is missing Ca 2+ binding and transmembrane domains after the CALM domain while V589 is an N-terminal truncated variant (V589NT) that is missing the N-terminal domains (N-ter to CALM domain). (E) Western blot showing that RYR3 protein expression decreased in jejunum SM of inducible SMC-specific Srf KO mice as SRF protein was depleted 5, 10, 15, and 20 days following tamoxifen administration. UBE1 was used as an endogenous control.
    Figure Legend Snippet: Identification of an SMC-specific Ryr3 regulated by SRF. (A) A genomic map view of Ryr3 variants expressed in JSMCs and CSMCs. Three variants TCONS_00167498 (V498, blue), TCONS_00152671 (V671, green), and TCONS_00166589 (V589, red) are indicated by arrows. (B) Expression levels of total Ryr3 in SMCs. (C) Expression levels of each Ryr3 vaiant in SMCs. Variants are arranged on the X-axis from longest (left) to shortest (right) in length. The three variants shown on A are also indicated by the color arrows. (D) A topological map of RYR3 variants. Each circle denotes the corresponding amino acid. Colors on amino acid sequence show distinct regions and domains: red, missing or inserted peptides from differentially spliced exons; green, start codons found in differentially spliced variants. Seven transmembrane domains 1–7 and a pore region (magenta) are shown. MR1-5 (blue), SPRY1-3 (dark green), FKBP1A (orange), CALM (purple), and a residue E (black) that is required for Ca 2+ binding (Ca 2+ ) are also indicated. The topology map was drawn based on the longest peptide variant V498. V671 is a C-terminal truncated variant (V671CT) that is missing Ca 2+ binding and transmembrane domains after the CALM domain while V589 is an N-terminal truncated variant (V589NT) that is missing the N-terminal domains (N-ter to CALM domain). (E) Western blot showing that RYR3 protein expression decreased in jejunum SM of inducible SMC-specific Srf KO mice as SRF protein was depleted 5, 10, 15, and 20 days following tamoxifen administration. UBE1 was used as an endogenous control.

    Techniques Used: Expressing, Sequencing, Binding Assay, Variant Assay, Western Blot, Mouse Assay

    8) Product Images from "Smooth Muscle Cell Genome Browser: Enabling the Identification of Novel Serum Response Factor Target Genes"

    Article Title: Smooth Muscle Cell Genome Browser: Enabling the Identification of Novel Serum Response Factor Target Genes

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0133751

    Identification of an SMC-specific Ryr3 regulated by SRF. (A) A genomic map view of Ryr3 variants expressed in JSMCs and CSMCs. Three variants TCONS_00167498 (V498, blue), TCONS_00152671 (V671, green), and TCONS_00166589 (V589, red) are indicated by arrows. (B) Expression levels of total Ryr3 in SMCs. (C) Expression levels of each Ryr3 vaiant in SMCs. Variants are arranged on the X-axis from longest (left) to shortest (right) in length. The three variants shown on A are also indicated by the color arrows. (D) A topological map of RYR3 variants. Each circle denotes the corresponding amino acid. Colors on amino acid sequence show distinct regions and domains: red, missing or inserted peptides from differentially spliced exons; green, start codons found in differentially spliced variants. Seven transmembrane domains 1–7 and a pore region (magenta) are shown. MR1-5 (blue), SPRY1-3 (dark green), FKBP1A (orange), CALM (purple), and a residue E (black) that is required for Ca 2+ binding (Ca 2+ ) are also indicated. The topology map was drawn based on the longest peptide variant V498. V671 is a C-terminal truncated variant (V671CT) that is missing Ca 2+ binding and transmembrane domains after the CALM domain while V589 is an N-terminal truncated variant (V589NT) that is missing the N-terminal domains (N-ter to CALM domain). (E) Western blot showing that RYR3 protein expression decreased in jejunum SM of inducible SMC-specific Srf KO mice as SRF protein was depleted 5, 10, 15, and 20 days following tamoxifen administration. UBE1 was used as an endogenous control.
    Figure Legend Snippet: Identification of an SMC-specific Ryr3 regulated by SRF. (A) A genomic map view of Ryr3 variants expressed in JSMCs and CSMCs. Three variants TCONS_00167498 (V498, blue), TCONS_00152671 (V671, green), and TCONS_00166589 (V589, red) are indicated by arrows. (B) Expression levels of total Ryr3 in SMCs. (C) Expression levels of each Ryr3 vaiant in SMCs. Variants are arranged on the X-axis from longest (left) to shortest (right) in length. The three variants shown on A are also indicated by the color arrows. (D) A topological map of RYR3 variants. Each circle denotes the corresponding amino acid. Colors on amino acid sequence show distinct regions and domains: red, missing or inserted peptides from differentially spliced exons; green, start codons found in differentially spliced variants. Seven transmembrane domains 1–7 and a pore region (magenta) are shown. MR1-5 (blue), SPRY1-3 (dark green), FKBP1A (orange), CALM (purple), and a residue E (black) that is required for Ca 2+ binding (Ca 2+ ) are also indicated. The topology map was drawn based on the longest peptide variant V498. V671 is a C-terminal truncated variant (V671CT) that is missing Ca 2+ binding and transmembrane domains after the CALM domain while V589 is an N-terminal truncated variant (V589NT) that is missing the N-terminal domains (N-ter to CALM domain). (E) Western blot showing that RYR3 protein expression decreased in jejunum SM of inducible SMC-specific Srf KO mice as SRF protein was depleted 5, 10, 15, and 20 days following tamoxifen administration. UBE1 was used as an endogenous control.

    Techniques Used: Expressing, Sequencing, Binding Assay, Variant Assay, Western Blot, Mouse Assay

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    • antibody ryr1  (Alomone Labs)
    93
    Alomone Labs antibody ryr1
    Flow cytometry detects <t>RYR1</t> in freshly isolated LMCs. Scatter plots of LMC suspensions plotted as side scatter (SSC-W) vs. fluorescent signals. Black horizontal lines denote the gate set. Fluorescent signal appearing above gate indicates positive staining. (A) Negative control (Neg) showing background FITC fluorescence of cell population with no <t>antibody</t> staining. Another LMC suspension was used to identify (B, left ) the LMC population stained by α-SMA-FITC ( red box ) and (B, right ) the gate set for non-specific staining of Alexa-Fluor 647 conjugated secondary antibody without primary antibodies within the α-SMA-FITC gated region. (C) Positive detection of RYR1 above the Alexa-Fluor 674 gate in LMCs isolated from rat mesenteric LVs. Data representative of five isolations each from male and female rats ( n = 10).
    Antibody Ryr1, 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
    https://www.bioz.com/result/antibody ryr1/product/Alomone Labs
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    antibody ryr1 - by Bioz Stars, 2022-12
    93/100 stars
    		  Buy from Supplier
    rabbit polyclonal ryr2  (Alomone Labs)
    94
    Alomone Labs rabbit polyclonal ryr2
    Knockdown of <t>RyR1/RyR2</t> downregulated the expression of BK Ca channel β1 subunit in uterine arteries of pregnant animals. Uterine arteries of pregnant sheep were treated with scramble control siRNA or siRNAs for RyR1, RyR2, and RyR3, respectively. Protein abundance of BK Ca channel α and β1 subunits was measured by western blot in uterine arteries 48 h after the treatment. ( A ) RyR1 siRNAs treatment. ( B ) RyR2 siRNAs treatment. ( C ) RyR3 siRNAs treatment. Data are means ± SEM from five animals of each group; independent-samples t -test; * P
    Rabbit Polyclonal Ryr2, 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
    https://www.bioz.com/result/rabbit polyclonal ryr2/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit polyclonal ryr2 - by Bioz Stars, 2022-12
    94/100 stars
    		  Buy from Supplier

    Image Search Results


    Flow cytometry detects RYR1 in freshly isolated LMCs. Scatter plots of LMC suspensions plotted as side scatter (SSC-W) vs. fluorescent signals. Black horizontal lines denote the gate set. Fluorescent signal appearing above gate indicates positive staining. (A) Negative control (Neg) showing background FITC fluorescence of cell population with no antibody staining. Another LMC suspension was used to identify (B, left ) the LMC population stained by α-SMA-FITC ( red box ) and (B, right ) the gate set for non-specific staining of Alexa-Fluor 647 conjugated secondary antibody without primary antibodies within the α-SMA-FITC gated region. (C) Positive detection of RYR1 above the Alexa-Fluor 674 gate in LMCs isolated from rat mesenteric LVs. Data representative of five isolations each from male and female rats ( n = 10).

    Journal: Frontiers in Pharmacology

    Article Title: Dantrolene Prevents the Lymphostasis Caused by Doxorubicin in the Rat Mesenteric Circulation

    doi: 10.3389/fphar.2021.727526

    Figure Lengend Snippet: Flow cytometry detects RYR1 in freshly isolated LMCs. Scatter plots of LMC suspensions plotted as side scatter (SSC-W) vs. fluorescent signals. Black horizontal lines denote the gate set. Fluorescent signal appearing above gate indicates positive staining. (A) Negative control (Neg) showing background FITC fluorescence of cell population with no antibody staining. Another LMC suspension was used to identify (B, left ) the LMC population stained by α-SMA-FITC ( red box ) and (B, right ) the gate set for non-specific staining of Alexa-Fluor 647 conjugated secondary antibody without primary antibodies within the α-SMA-FITC gated region. (C) Positive detection of RYR1 above the Alexa-Fluor 674 gate in LMCs isolated from rat mesenteric LVs. Data representative of five isolations each from male and female rats ( n = 10).

    Article Snippet: The membrane was first incubated in tris-buffered saline (TBS) containing 0.05% Tween-20 and 5% non-fat dry milk to reduce non-specific antibody binding, then incubated overnight at 4°C with primary antibody RYR1 (1:1,000, Alomone Labs, Jerusalem, Israel) prepared in TBS containing 0.05% Tween-20 and 5% non-fat dry milk.

    Techniques: Flow Cytometry, Isolation, Staining, Negative Control, Fluorescence

    RYR1 antibody selectivity. (A) Western blot shows positive detection of RYR1 (∼565 kD) in rat skeletal muscle lysate and no detection in rat heart or brain lysate. (B,C) Contour plots of RYR1 antibody testing. (B) Red population represents positive detection of RYR1 subtype in male LMCs. Grey population represents the LMC suspension containing no primary antibody. (C) No detection in male LMCs after co-incubation with competing peptide (CP; 1:50 dilution) for the RYR1 antibody. Data representative of three isolations for each sex ( n = 6).

    Journal: Frontiers in Pharmacology

    Article Title: Dantrolene Prevents the Lymphostasis Caused by Doxorubicin in the Rat Mesenteric Circulation

    doi: 10.3389/fphar.2021.727526

    Figure Lengend Snippet: RYR1 antibody selectivity. (A) Western blot shows positive detection of RYR1 (∼565 kD) in rat skeletal muscle lysate and no detection in rat heart or brain lysate. (B,C) Contour plots of RYR1 antibody testing. (B) Red population represents positive detection of RYR1 subtype in male LMCs. Grey population represents the LMC suspension containing no primary antibody. (C) No detection in male LMCs after co-incubation with competing peptide (CP; 1:50 dilution) for the RYR1 antibody. Data representative of three isolations for each sex ( n = 6).

    Article Snippet: The membrane was first incubated in tris-buffered saline (TBS) containing 0.05% Tween-20 and 5% non-fat dry milk to reduce non-specific antibody binding, then incubated overnight at 4°C with primary antibody RYR1 (1:1,000, Alomone Labs, Jerusalem, Israel) prepared in TBS containing 0.05% Tween-20 and 5% non-fat dry milk.

    Techniques: Western Blot, Incubation

    Knockdown of RyR1/RyR2 downregulated the expression of BK Ca channel β1 subunit in uterine arteries of pregnant animals. Uterine arteries of pregnant sheep were treated with scramble control siRNA or siRNAs for RyR1, RyR2, and RyR3, respectively. Protein abundance of BK Ca channel α and β1 subunits was measured by western blot in uterine arteries 48 h after the treatment. ( A ) RyR1 siRNAs treatment. ( B ) RyR2 siRNAs treatment. ( C ) RyR3 siRNAs treatment. Data are means ± SEM from five animals of each group; independent-samples t -test; * P

    Journal: Cardiovascular Research

    Article Title: Ryanodine receptor subtypes regulate Ca2+ sparks/spontaneous transient outward currents and myogenic tone of uterine arteries in pregnancy

    doi: 10.1093/cvr/cvaa089

    Figure Lengend Snippet: Knockdown of RyR1/RyR2 downregulated the expression of BK Ca channel β1 subunit in uterine arteries of pregnant animals. Uterine arteries of pregnant sheep were treated with scramble control siRNA or siRNAs for RyR1, RyR2, and RyR3, respectively. Protein abundance of BK Ca channel α and β1 subunits was measured by western blot in uterine arteries 48 h after the treatment. ( A ) RyR1 siRNAs treatment. ( B ) RyR2 siRNAs treatment. ( C ) RyR3 siRNAs treatment. Data are means ± SEM from five animals of each group; independent-samples t -test; * P

    Article Snippet: After blocking non-specific binding sites by dry milk, membranes were incubated with primary antibodies (1:1000 dilution) against rabbit polyclonal RyR1 (8153, Cell Signaling, Danvers, MA, USA), rabbit polyclonal RyR2 (ARR-002, Alomone Labs, Israel), rabbit polyclonal RyR3 (AB9082, EMD Millipore), mouse monoclonal BKCa channel α, or mouse monoclonal BKCa channel β1 (Santa Cruz Biotechnology, Dallas, TX, USA).

    Techniques: Expressing, Western Blot

    Knockdown of RyR1/RyR2 suppressed STOCs in uterine arteries of pregnant sheep. Uterine arteries of pregnant animals were treated with scramble control siRNAs or siRNAs for RyR1, RyR2, and RyR3, respectively. STOCs were measured in uterine artery vascular smooth muscle cells 48 hours later. ( A ) Representative traces showing STOCs at holding potentials of 10 mV in uterine artery vascular smooth muscle cells. ( B ) STOC frequency. ( C ) STOC amplitude. Data are means ± SEM from five animals of each group; repeated measures ANOVA with the post hoc Bonferroni/Dunn test; * P

    Journal: Cardiovascular Research

    Article Title: Ryanodine receptor subtypes regulate Ca2+ sparks/spontaneous transient outward currents and myogenic tone of uterine arteries in pregnancy

    doi: 10.1093/cvr/cvaa089

    Figure Lengend Snippet: Knockdown of RyR1/RyR2 suppressed STOCs in uterine arteries of pregnant sheep. Uterine arteries of pregnant animals were treated with scramble control siRNAs or siRNAs for RyR1, RyR2, and RyR3, respectively. STOCs were measured in uterine artery vascular smooth muscle cells 48 hours later. ( A ) Representative traces showing STOCs at holding potentials of 10 mV in uterine artery vascular smooth muscle cells. ( B ) STOC frequency. ( C ) STOC amplitude. Data are means ± SEM from five animals of each group; repeated measures ANOVA with the post hoc Bonferroni/Dunn test; * P

    Article Snippet: After blocking non-specific binding sites by dry milk, membranes were incubated with primary antibodies (1:1000 dilution) against rabbit polyclonal RyR1 (8153, Cell Signaling, Danvers, MA, USA), rabbit polyclonal RyR2 (ARR-002, Alomone Labs, Israel), rabbit polyclonal RyR3 (AB9082, EMD Millipore), mouse monoclonal BKCa channel α, or mouse monoclonal BKCa channel β1 (Santa Cruz Biotechnology, Dallas, TX, USA).

    Techniques:

    Knockdown of RyR1/RyR2 increased myogenic tone in uterine arteries of pregnant sheep. Uterine arteries of pregnant animals were treated with scramble control siRNAs or siRNAs for RyR1, RyR2, and RyR3, respectively. Pressure-dependent myogenic tone was measured in uterine arteries 48 h later. ( A–C ) Changes of lumen diameters of uterine arteries in response to increases in intravascular pressure. ( D ) Data summary showing the percentage myogenic tone in RyR siRNA-treated uterine arteries. Data are means ± SEM from five animals of each group; repeated measures ANOVA with the post hoc Bonferroni/Dunn test; * P

    Journal: Cardiovascular Research

    Article Title: Ryanodine receptor subtypes regulate Ca2+ sparks/spontaneous transient outward currents and myogenic tone of uterine arteries in pregnancy

    doi: 10.1093/cvr/cvaa089

    Figure Lengend Snippet: Knockdown of RyR1/RyR2 increased myogenic tone in uterine arteries of pregnant sheep. Uterine arteries of pregnant animals were treated with scramble control siRNAs or siRNAs for RyR1, RyR2, and RyR3, respectively. Pressure-dependent myogenic tone was measured in uterine arteries 48 h later. ( A–C ) Changes of lumen diameters of uterine arteries in response to increases in intravascular pressure. ( D ) Data summary showing the percentage myogenic tone in RyR siRNA-treated uterine arteries. Data are means ± SEM from five animals of each group; repeated measures ANOVA with the post hoc Bonferroni/Dunn test; * P

    Article Snippet: After blocking non-specific binding sites by dry milk, membranes were incubated with primary antibodies (1:1000 dilution) against rabbit polyclonal RyR1 (8153, Cell Signaling, Danvers, MA, USA), rabbit polyclonal RyR2 (ARR-002, Alomone Labs, Israel), rabbit polyclonal RyR3 (AB9082, EMD Millipore), mouse monoclonal BKCa channel α, or mouse monoclonal BKCa channel β1 (Santa Cruz Biotechnology, Dallas, TX, USA).

    Techniques:

    Knockdown of RyR1/RyR2 reduced the interaction of BK Ca channel α and β1 subunits in uterine arteries. ( A ) Representative immunoblots from five replicates show co-immunoprecipitation of BK Ca channel α and β1 subunits in uterine arteries of non-pregnant (NUA) and pregnant (PUA) sheep. Uterine arteries were treated with scramble control siRNA or siRNAs for RyR1, RyR2, and RyR3, respectively, for 48 h. IgG was used as a control to show antibody specificity. ( B ) Representative confocal immunofluorescence images from five replicates show the co-localization of BK Ca channel α and β1 subunits in uterine arteries of pregnant sheep after control siRNAs or RyR siRNAs treatments. The arteries were stained with antibodies against α (green) and β1 (red) subunits. Merged images show in yellow. The nuclear region was stained with DAPI and shows in blue. Scale bar: 100 µm. ( C ) Representative immunoblots from five replicates show co-immunoprecipitation of BK Ca channel α and β1 subunits in uterine arteries of pregnant sheep after control siRNA or RyR siRNAs treatments. β-Actin blots showing equal total protein lysates (input).

    Journal: Cardiovascular Research

    Article Title: Ryanodine receptor subtypes regulate Ca2+ sparks/spontaneous transient outward currents and myogenic tone of uterine arteries in pregnancy

    doi: 10.1093/cvr/cvaa089

    Figure Lengend Snippet: Knockdown of RyR1/RyR2 reduced the interaction of BK Ca channel α and β1 subunits in uterine arteries. ( A ) Representative immunoblots from five replicates show co-immunoprecipitation of BK Ca channel α and β1 subunits in uterine arteries of non-pregnant (NUA) and pregnant (PUA) sheep. Uterine arteries were treated with scramble control siRNA or siRNAs for RyR1, RyR2, and RyR3, respectively, for 48 h. IgG was used as a control to show antibody specificity. ( B ) Representative confocal immunofluorescence images from five replicates show the co-localization of BK Ca channel α and β1 subunits in uterine arteries of pregnant sheep after control siRNAs or RyR siRNAs treatments. The arteries were stained with antibodies against α (green) and β1 (red) subunits. Merged images show in yellow. The nuclear region was stained with DAPI and shows in blue. Scale bar: 100 µm. ( C ) Representative immunoblots from five replicates show co-immunoprecipitation of BK Ca channel α and β1 subunits in uterine arteries of pregnant sheep after control siRNA or RyR siRNAs treatments. β-Actin blots showing equal total protein lysates (input).

    Article Snippet: After blocking non-specific binding sites by dry milk, membranes were incubated with primary antibodies (1:1000 dilution) against rabbit polyclonal RyR1 (8153, Cell Signaling, Danvers, MA, USA), rabbit polyclonal RyR2 (ARR-002, Alomone Labs, Israel), rabbit polyclonal RyR3 (AB9082, EMD Millipore), mouse monoclonal BKCa channel α, or mouse monoclonal BKCa channel β1 (Santa Cruz Biotechnology, Dallas, TX, USA).

    Techniques: Western Blot, Immunoprecipitation, Immunofluorescence, Staining

    Knockdown of RyR1/RyR2 decreased Ca 2+ sparks in uterine arteries of pregnant sheep. Uterine arteries of pregnant animals were treated with scramble control siRNA or siRNAs for RyR1, RyR2, and RyR3, respectively. Ca 2+ sparks in uterine arteries were measured 48 h later. ( A ) Representative line-scan images of Fluo-4AM loaded uterine arteries showing Ca 2+ sparks recorded before and after the sequential application of 30 mmol/L K + (30 K) following siRNA treatments. ( B ) Percentage of Ca 2+ spark-firing vascular smooth muscle cells. ( C ) Ca 2+ spark frequency. Data are means ± SEM from five animals of each group; independent-samples t -test; * P

    Journal: Cardiovascular Research

    Article Title: Ryanodine receptor subtypes regulate Ca2+ sparks/spontaneous transient outward currents and myogenic tone of uterine arteries in pregnancy

    doi: 10.1093/cvr/cvaa089

    Figure Lengend Snippet: Knockdown of RyR1/RyR2 decreased Ca 2+ sparks in uterine arteries of pregnant sheep. Uterine arteries of pregnant animals were treated with scramble control siRNA or siRNAs for RyR1, RyR2, and RyR3, respectively. Ca 2+ sparks in uterine arteries were measured 48 h later. ( A ) Representative line-scan images of Fluo-4AM loaded uterine arteries showing Ca 2+ sparks recorded before and after the sequential application of 30 mmol/L K + (30 K) following siRNA treatments. ( B ) Percentage of Ca 2+ spark-firing vascular smooth muscle cells. ( C ) Ca 2+ spark frequency. Data are means ± SEM from five animals of each group; independent-samples t -test; * P

    Article Snippet: After blocking non-specific binding sites by dry milk, membranes were incubated with primary antibodies (1:1000 dilution) against rabbit polyclonal RyR1 (8153, Cell Signaling, Danvers, MA, USA), rabbit polyclonal RyR2 (ARR-002, Alomone Labs, Israel), rabbit polyclonal RyR3 (AB9082, EMD Millipore), mouse monoclonal BKCa channel α, or mouse monoclonal BKCa channel β1 (Santa Cruz Biotechnology, Dallas, TX, USA).

    Techniques:

    Pregnancy increased co-localization of RyR1/RyR2 with BKCa channel in uterine arteries. ( A ) Representative confocal immunofluorescence images from five replicates show the co-localization of RyRs and BK Ca channels in uterine arteries. Uterine arteries of non-pregnant (NUA) and pregnant (PUA) animals were stained with antibodies against the β1 subunit of BK Ca channel (BK Ca β1, red) and RyR1, RyR2, or RyR3 (green). Merged images show the co-localization of RyR1 or RyR2 with BK Ca β1 (in yellow). The nuclear region was stained with DAPI and shows in blue. Scale bar: 100 µm. ( B ) PLA assay to confirm the co-localization of RyR1/RyR2 and BK Ca β1 in uterine arteries. ( C ) Quantification of the PLA signals. Images from five independent replicates were analysed. The nuclear region was stained with DAPI and shown in blue. Scale bar: 50 µm. Data are means ± SEM from five animals of each group; independent-samples t -test; * P

    Journal: Cardiovascular Research

    Article Title: Ryanodine receptor subtypes regulate Ca2+ sparks/spontaneous transient outward currents and myogenic tone of uterine arteries in pregnancy

    doi: 10.1093/cvr/cvaa089

    Figure Lengend Snippet: Pregnancy increased co-localization of RyR1/RyR2 with BKCa channel in uterine arteries. ( A ) Representative confocal immunofluorescence images from five replicates show the co-localization of RyRs and BK Ca channels in uterine arteries. Uterine arteries of non-pregnant (NUA) and pregnant (PUA) animals were stained with antibodies against the β1 subunit of BK Ca channel (BK Ca β1, red) and RyR1, RyR2, or RyR3 (green). Merged images show the co-localization of RyR1 or RyR2 with BK Ca β1 (in yellow). The nuclear region was stained with DAPI and shows in blue. Scale bar: 100 µm. ( B ) PLA assay to confirm the co-localization of RyR1/RyR2 and BK Ca β1 in uterine arteries. ( C ) Quantification of the PLA signals. Images from five independent replicates were analysed. The nuclear region was stained with DAPI and shown in blue. Scale bar: 50 µm. Data are means ± SEM from five animals of each group; independent-samples t -test; * P

    Article Snippet: After blocking non-specific binding sites by dry milk, membranes were incubated with primary antibodies (1:1000 dilution) against rabbit polyclonal RyR1 (8153, Cell Signaling, Danvers, MA, USA), rabbit polyclonal RyR2 (ARR-002, Alomone Labs, Israel), rabbit polyclonal RyR3 (AB9082, EMD Millipore), mouse monoclonal BKCa channel α, or mouse monoclonal BKCa channel β1 (Santa Cruz Biotechnology, Dallas, TX, USA).

    Techniques: Immunofluorescence, Staining, Proximity Ligation Assay