cacna1c  (Alomone Labs)


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    Name:
    Guinea pig Anti Cav1 2 CACNA1C Antibody
    Description:
    Guinea pig Anti CaV1 2 CACNA1C Antibody AGP 001 raised in guinea pigs is a highly specific antibody directed against an epitope of the rat protein The antibody can be used in western blot and immunohistochemistry applications It has been designed to recognize CaV1 2 from mouse rat and human samples The antigen used to immunize guinea pigs is the same as Anti CaV1 2 CACNA1C Antibody ACC 003 raised in rabbit Our line of guinea pig antibodies enables more flexibility with our products such as multiplex staining studies immunoprecipitation etc
    Catalog Number:
    AGP-001
    Price:
    397.0
    Category:
    Primary Antibody
    Applications:
    Immunofluorescence, Immunohistochemistry, Western Blot
    Purity:
    Affinity purified on immobilized antigen.
    Immunogen:
    Synthetic peptide
    Size:
    25 mcl
    Antibody Type:
    Polyclonal Primary Antibodies
    Format:
    Lyophilized Powder
    Host:
    Guinea pig
    Isotype:
    Guinea pig total IgG
    Buy from Supplier


    Structured Review

    Alomone Labs cacna1c
    Guinea pig Anti Cav1 2 CACNA1C Antibody
    Guinea pig Anti CaV1 2 CACNA1C Antibody AGP 001 raised in guinea pigs is a highly specific antibody directed against an epitope of the rat protein The antibody can be used in western blot and immunohistochemistry applications It has been designed to recognize CaV1 2 from mouse rat and human samples The antigen used to immunize guinea pigs is the same as Anti CaV1 2 CACNA1C Antibody ACC 003 raised in rabbit Our line of guinea pig antibodies enables more flexibility with our products such as multiplex staining studies immunoprecipitation etc
    https://www.bioz.com/result/cacna1c/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    cacna1c - by Bioz Stars, 2021-09
    94/100 stars

    Images

    1) Product Images from "Serum response factor regulates smooth muscle contractility via myotonic dystrophy protein kinases and L-type calcium channels"

    Article Title: Serum response factor regulates smooth muscle contractility via myotonic dystrophy protein kinases and L-type calcium channels

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0171262

    Alternations of L-type calcium channel transcripts, protein, and action potential in KO smooth muscle. (A) PCR validation of alternatively started and spliced exons of Cacna1c in WT and KO jejunum smooth muscle at KO days 5, 10, and 15. NTC is non template control. Primer sets were designed from variant exons in the regions (e.g. E1-3, forward primer spanning a region on exon 1 and reverse primer on exon 3). (B) qPCR data showing decreased expression of Cacna1c variants starting at exon 1 and exon 2 long and short forms (E1-3, E2L-3, and E2L/S-3) at KO days 5, 10, 15, and 20. E1-3, a region spanning exons 1 and 3; E2L-3, a region spanning exon 2 long (L) form and exon 3; E2L/S-3, a region spanning exon 2 long (L) and short (S) forms and exon 3. (C) Western blot showing decreased levels of CACNA1C protein in Srf KO muscle. (D) Consensus sequence of 5’ splice donor and 3’ splice acceptor sites. (E) A topological map of CACNA1C variants. Amino acid sequence is written in small circles. Four motifs are indicated as I-IV and six transmembrane domains, S1-S6. Four pore regions are also indicated. Colors on amino acid sequence show particular regions and domains: red, missing or inserted peptides from differentially spliced exons; purple, voltage sensors in S4 transmembrane domains; green, start codons found in differentially spliced variants (*, start codons deduced from indicated exons that are differentially spliced; blue, β subunit binding domain; brown, CaM (calmodulin) binding domain; orange, PKA (protein kinase A) phosphorylation site. Alignment of alternatively spliced exons E9/10, E24/25, and E32/33 are shown. (F) Isometric force recordings from antrum and colon of WT and KO mice. Bay K8644 (1 μM) and high potassium (K + ) Krebs (36 mM and 72 mM) were applied to the tissues (indicated by bar and arrows). (G) The graph summarizes the results for 9 antral and 5 colonic WT and KO tissues. The responses to Bay K8644, 36 mM K + , and 72 mM K + were significantly decreased in KO antrums, and the responses to 36 mM K + and 72 mM K + were significantly reduced in KO colons compared to WT. * and ** represent p ≤ 0.05 and p ≤ 0.01 respectively.
    Figure Legend Snippet: Alternations of L-type calcium channel transcripts, protein, and action potential in KO smooth muscle. (A) PCR validation of alternatively started and spliced exons of Cacna1c in WT and KO jejunum smooth muscle at KO days 5, 10, and 15. NTC is non template control. Primer sets were designed from variant exons in the regions (e.g. E1-3, forward primer spanning a region on exon 1 and reverse primer on exon 3). (B) qPCR data showing decreased expression of Cacna1c variants starting at exon 1 and exon 2 long and short forms (E1-3, E2L-3, and E2L/S-3) at KO days 5, 10, 15, and 20. E1-3, a region spanning exons 1 and 3; E2L-3, a region spanning exon 2 long (L) form and exon 3; E2L/S-3, a region spanning exon 2 long (L) and short (S) forms and exon 3. (C) Western blot showing decreased levels of CACNA1C protein in Srf KO muscle. (D) Consensus sequence of 5’ splice donor and 3’ splice acceptor sites. (E) A topological map of CACNA1C variants. Amino acid sequence is written in small circles. Four motifs are indicated as I-IV and six transmembrane domains, S1-S6. Four pore regions are also indicated. Colors on amino acid sequence show particular regions and domains: red, missing or inserted peptides from differentially spliced exons; purple, voltage sensors in S4 transmembrane domains; green, start codons found in differentially spliced variants (*, start codons deduced from indicated exons that are differentially spliced; blue, β subunit binding domain; brown, CaM (calmodulin) binding domain; orange, PKA (protein kinase A) phosphorylation site. Alignment of alternatively spliced exons E9/10, E24/25, and E32/33 are shown. (F) Isometric force recordings from antrum and colon of WT and KO mice. Bay K8644 (1 μM) and high potassium (K + ) Krebs (36 mM and 72 mM) were applied to the tissues (indicated by bar and arrows). (G) The graph summarizes the results for 9 antral and 5 colonic WT and KO tissues. The responses to Bay K8644, 36 mM K + , and 72 mM K + were significantly decreased in KO antrums, and the responses to 36 mM K + and 72 mM K + were significantly reduced in KO colons compared to WT. * and ** represent p ≤ 0.05 and p ≤ 0.01 respectively.

    Techniques Used: Polymerase Chain Reaction, Variant Assay, Real-time Polymerase Chain Reaction, Expressing, Western Blot, Sequencing, Binding Assay, Chick Chorioallantoic Membrane Assay, Mouse Assay

    Model showing the possible molecular pathways by which SRF regulates contractility via DMPK and CACNA1C in SMC.
    Figure Legend Snippet: Model showing the possible molecular pathways by which SRF regulates contractility via DMPK and CACNA1C in SMC.

    Techniques Used:

    Identification of a predominant subtype and alternative transcriptional variants of L-type calcium channels expressed in SMC. (A) Expression levels of L-type calcium channel subtypes in SMC of jejunum and colon. (B) Expression levels of Cacna1c variants in SMC and tissue of jejunum and colon. (C) A genomic map of Cacna1c variants. Five variable regions (V1-5) are indicated. Exons are numbered 1–48. (D) Magnified view of variable regions showing alternatively started or spliced exons (indicated as exon numbers). Seven exons containing alternative transcriptional start sequence are shown by a star (*). Long (L) and short (S) exons that are differentially started or spliced are indicated.
    Figure Legend Snippet: Identification of a predominant subtype and alternative transcriptional variants of L-type calcium channels expressed in SMC. (A) Expression levels of L-type calcium channel subtypes in SMC of jejunum and colon. (B) Expression levels of Cacna1c variants in SMC and tissue of jejunum and colon. (C) A genomic map of Cacna1c variants. Five variable regions (V1-5) are indicated. Exons are numbered 1–48. (D) Magnified view of variable regions showing alternatively started or spliced exons (indicated as exon numbers). Seven exons containing alternative transcriptional start sequence are shown by a star (*). Long (L) and short (S) exons that are differentially started or spliced are indicated.

    Techniques Used: Expressing, Sequencing

    2) Product Images from "Severe T-System Remodeling in Pediatric Viral Myocarditis"

    Article Title: Severe T-System Remodeling in Pediatric Viral Myocarditis

    Journal: Frontiers in Cardiovascular Medicine

    doi: 10.3389/fcvm.2020.624776

    Structural integrity of excitation-contraction (EC) coupling junctions before and after VAD therapy of a myocarditis patient. (A,B) Raw confocal images of fixed isolated cardiomyocytes from pre- and post-VAD of the patient presented in Figures 6 , 7 , co-stained for LTCC (red), RyR (green), and JPH2 (blue) and with DAPI (not shown). (C,D) Overlay of binary images for the EC coupling proteins shown in (A,B) , with magnifications of boxed regions. The cell surface, obtained from autofluorescence, is shown white, nuclei are shown white with black asterisk. Co-localizations of LTCC, JPH2, and RyR appear cyan, magenta, yellow, or white (see color legend). (E) Cardiomyocyte JPH2 cluster density (JPH2 density) of AVSD as reference and the Pre- and Post-VAD sample. (F) Fraction of LTCC clusters that were co-localized with both RyR and JPH2, as a measure of intact EC coupling junctions ( n = 10/9 cells for Pre/Post-VAD). * p
    Figure Legend Snippet: Structural integrity of excitation-contraction (EC) coupling junctions before and after VAD therapy of a myocarditis patient. (A,B) Raw confocal images of fixed isolated cardiomyocytes from pre- and post-VAD of the patient presented in Figures 6 , 7 , co-stained for LTCC (red), RyR (green), and JPH2 (blue) and with DAPI (not shown). (C,D) Overlay of binary images for the EC coupling proteins shown in (A,B) , with magnifications of boxed regions. The cell surface, obtained from autofluorescence, is shown white, nuclei are shown white with black asterisk. Co-localizations of LTCC, JPH2, and RyR appear cyan, magenta, yellow, or white (see color legend). (E) Cardiomyocyte JPH2 cluster density (JPH2 density) of AVSD as reference and the Pre- and Post-VAD sample. (F) Fraction of LTCC clusters that were co-localized with both RyR and JPH2, as a measure of intact EC coupling junctions ( n = 10/9 cells for Pre/Post-VAD). * p

    Techniques Used: Isolation, Staining

    Related Articles

    Immunofluorescence:

    Article Title: The Na+/H+-Exchanger NHE1 Regulates Extra- and Intracellular pH and Nimodipine-sensitive [Ca2+]i in the Suprachiasmatic Nucleus
    Article Snippet: .. For immunofluorescence staining, sections (20 µm) were washed for 20–30 min in PBS and then incubated overnight at 4 °C in PBS containing 2% serum, 0.3% Triton X-100, and primary antibodies against NHE1 (rabbit anti-NHE1; 1:100; ab67314, RRID:AB_1141782; Abcam, Cambridge, MA, USA), neurophysin II (NP2) (goat anti-NP2; 1:500; sc-27093, RRID:AB_2061964; Santa Cruz, CA, USA), vasoactive intestinal peptide (VIP) (guinea pig anti-VIP; 1:500; T-5030, RRID:AB_518690; Peninsula Laboratories, San Carlos, CA, USA), gastrin-releasing peptide (GRP) (goat anti-GRP; 1:100; sc-7788, RRID:AB_2232721; Santa Cruz, CA, USA), vesicular glutamate transporter type 2 (vGluT2) (guinea pig anti-vGluT2; 1:300; AB2251, RRID:AB_1587626; Millipore, Temecula, CA, USA), serotonin transporter (SERT) (mouse anti-SERT; 1:200; MAB1564, RRID:AB_94220; Millipore, Temecula, CA, USA), neuropeptide Y (NPY) (goat anti-NPY; 1:300; NBP1-46535, RRID:AB_10009813; Novus, Littleton, CO, USA), CaV1.2 (guinea pig anti-CaV1.2; 1:100; AGP-001; RRID:AB_11219156; Alomone Labs, Jerusalem, Israel), NCX1 (mouse anti-NCX1, against epitope between amino acid 371 and 525 on intracellular side of plasma membrane; 1:100; AB2869, RRID:AB_2191134; Abcam, MA, USA), and Bassoon (mouse anti-Bassoon; 1:200; ADI-VAM-PS003-D, RRID:AB_2038857; Enzo Life Sciences, Farmingdale, NY, USA). ..

    Staining:

    Article Title: The Na+/H+-Exchanger NHE1 Regulates Extra- and Intracellular pH and Nimodipine-sensitive [Ca2+]i in the Suprachiasmatic Nucleus
    Article Snippet: .. For immunofluorescence staining, sections (20 µm) were washed for 20–30 min in PBS and then incubated overnight at 4 °C in PBS containing 2% serum, 0.3% Triton X-100, and primary antibodies against NHE1 (rabbit anti-NHE1; 1:100; ab67314, RRID:AB_1141782; Abcam, Cambridge, MA, USA), neurophysin II (NP2) (goat anti-NP2; 1:500; sc-27093, RRID:AB_2061964; Santa Cruz, CA, USA), vasoactive intestinal peptide (VIP) (guinea pig anti-VIP; 1:500; T-5030, RRID:AB_518690; Peninsula Laboratories, San Carlos, CA, USA), gastrin-releasing peptide (GRP) (goat anti-GRP; 1:100; sc-7788, RRID:AB_2232721; Santa Cruz, CA, USA), vesicular glutamate transporter type 2 (vGluT2) (guinea pig anti-vGluT2; 1:300; AB2251, RRID:AB_1587626; Millipore, Temecula, CA, USA), serotonin transporter (SERT) (mouse anti-SERT; 1:200; MAB1564, RRID:AB_94220; Millipore, Temecula, CA, USA), neuropeptide Y (NPY) (goat anti-NPY; 1:300; NBP1-46535, RRID:AB_10009813; Novus, Littleton, CO, USA), CaV1.2 (guinea pig anti-CaV1.2; 1:100; AGP-001; RRID:AB_11219156; Alomone Labs, Jerusalem, Israel), NCX1 (mouse anti-NCX1, against epitope between amino acid 371 and 525 on intracellular side of plasma membrane; 1:100; AB2869, RRID:AB_2191134; Abcam, MA, USA), and Bassoon (mouse anti-Bassoon; 1:200; ADI-VAM-PS003-D, RRID:AB_2038857; Enzo Life Sciences, Farmingdale, NY, USA). ..

    Article Title: Severe T-System Remodeling in Pediatric Viral Myocarditis
    Article Snippet: .. Primary antibodies against JPH2 (Thermo Fisher, 40-5300), LTCC (Alomone, AGP-001), and RyR (Thermo Fisher, MA3 916) were diluted 1:200 in staining solution (phosphate buffered saline, PBS, supplemented with 1% BSA, 5% normal goat serum, 0.25% TritonX-100) and incubated for a minimum of 16h in the dark at 4°C. ..

    Incubation:

    Article Title: The Na+/H+-Exchanger NHE1 Regulates Extra- and Intracellular pH and Nimodipine-sensitive [Ca2+]i in the Suprachiasmatic Nucleus
    Article Snippet: .. For immunofluorescence staining, sections (20 µm) were washed for 20–30 min in PBS and then incubated overnight at 4 °C in PBS containing 2% serum, 0.3% Triton X-100, and primary antibodies against NHE1 (rabbit anti-NHE1; 1:100; ab67314, RRID:AB_1141782; Abcam, Cambridge, MA, USA), neurophysin II (NP2) (goat anti-NP2; 1:500; sc-27093, RRID:AB_2061964; Santa Cruz, CA, USA), vasoactive intestinal peptide (VIP) (guinea pig anti-VIP; 1:500; T-5030, RRID:AB_518690; Peninsula Laboratories, San Carlos, CA, USA), gastrin-releasing peptide (GRP) (goat anti-GRP; 1:100; sc-7788, RRID:AB_2232721; Santa Cruz, CA, USA), vesicular glutamate transporter type 2 (vGluT2) (guinea pig anti-vGluT2; 1:300; AB2251, RRID:AB_1587626; Millipore, Temecula, CA, USA), serotonin transporter (SERT) (mouse anti-SERT; 1:200; MAB1564, RRID:AB_94220; Millipore, Temecula, CA, USA), neuropeptide Y (NPY) (goat anti-NPY; 1:300; NBP1-46535, RRID:AB_10009813; Novus, Littleton, CO, USA), CaV1.2 (guinea pig anti-CaV1.2; 1:100; AGP-001; RRID:AB_11219156; Alomone Labs, Jerusalem, Israel), NCX1 (mouse anti-NCX1, against epitope between amino acid 371 and 525 on intracellular side of plasma membrane; 1:100; AB2869, RRID:AB_2191134; Abcam, MA, USA), and Bassoon (mouse anti-Bassoon; 1:200; ADI-VAM-PS003-D, RRID:AB_2038857; Enzo Life Sciences, Farmingdale, NY, USA). ..

    Article Title: Severe T-System Remodeling in Pediatric Viral Myocarditis
    Article Snippet: .. Primary antibodies against JPH2 (Thermo Fisher, 40-5300), LTCC (Alomone, AGP-001), and RyR (Thermo Fisher, MA3 916) were diluted 1:200 in staining solution (phosphate buffered saline, PBS, supplemented with 1% BSA, 5% normal goat serum, 0.25% TritonX-100) and incubated for a minimum of 16h in the dark at 4°C. ..

    Article Title: Cardiovascular phenotype of the Dmdmdx rat – a suitable animal model for Duchenne muscular dystrophy
    Article Snippet: .. This was followed by blocking with 10% horse serum and 0.01% azide in PBS for 2 h. Thereafter, the cells were incubated with a selective anti-Cav 1.2 antibody (#AGP-001, Alomone Labs; 1:500 in PBS) at 4°C overnight. ..

    Blocking Assay:

    Article Title: Cardiovascular phenotype of the Dmdmdx rat – a suitable animal model for Duchenne muscular dystrophy
    Article Snippet: .. This was followed by blocking with 10% horse serum and 0.01% azide in PBS for 2 h. Thereafter, the cells were incubated with a selective anti-Cav 1.2 antibody (#AGP-001, Alomone Labs; 1:500 in PBS) at 4°C overnight. ..

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    Alomone Labs cacna1c
    Alternations of L-type calcium channel transcripts, protein, and action potential in KO smooth muscle. (A) PCR validation of alternatively started and spliced exons of <t>Cacna1c</t> in WT and KO jejunum smooth muscle at KO days 5, 10, and 15. NTC is non template control. Primer sets were designed from variant exons in the regions (e.g. E1-3, forward primer spanning a region on exon 1 and reverse primer on exon 3). (B) qPCR data showing decreased expression of Cacna1c variants starting at exon 1 and exon 2 long and short forms (E1-3, E2L-3, and E2L/S-3) at KO days 5, 10, 15, and 20. E1-3, a region spanning exons 1 and 3; E2L-3, a region spanning exon 2 long (L) form and exon 3; E2L/S-3, a region spanning exon 2 long (L) and short (S) forms and exon 3. (C) Western blot showing decreased levels of CACNA1C protein in Srf KO muscle. (D) Consensus sequence of 5’ splice donor and 3’ splice acceptor sites. (E) A topological map of CACNA1C variants. Amino acid sequence is written in small circles. Four motifs are indicated as I-IV and six transmembrane domains, S1-S6. Four pore regions are also indicated. Colors on amino acid sequence show particular regions and domains: red, missing or inserted peptides from differentially spliced exons; purple, voltage sensors in S4 transmembrane domains; green, start codons found in differentially spliced variants (*, start codons deduced from indicated exons that are differentially spliced; blue, β subunit binding domain; brown, CaM (calmodulin) binding domain; orange, PKA (protein kinase A) phosphorylation site. Alignment of alternatively spliced exons E9/10, E24/25, and E32/33 are shown. (F) Isometric force recordings from antrum and colon of WT and KO mice. Bay K8644 (1 μM) and high potassium (K + ) Krebs (36 mM and 72 mM) were applied to the tissues (indicated by bar and arrows). (G) The graph summarizes the results for 9 antral and 5 colonic WT and KO tissues. The responses to Bay K8644, 36 mM K + , and 72 mM K + were significantly decreased in KO antrums, and the responses to 36 mM K + and 72 mM K + were significantly reduced in KO colons compared to WT. * and ** represent p ≤ 0.05 and p ≤ 0.01 respectively.
    Cacna1c, 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/cacna1c/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    cacna1c - by Bioz Stars, 2021-09
    94/100 stars
      Buy from Supplier

    Image Search Results


    Alternations of L-type calcium channel transcripts, protein, and action potential in KO smooth muscle. (A) PCR validation of alternatively started and spliced exons of Cacna1c in WT and KO jejunum smooth muscle at KO days 5, 10, and 15. NTC is non template control. Primer sets were designed from variant exons in the regions (e.g. E1-3, forward primer spanning a region on exon 1 and reverse primer on exon 3). (B) qPCR data showing decreased expression of Cacna1c variants starting at exon 1 and exon 2 long and short forms (E1-3, E2L-3, and E2L/S-3) at KO days 5, 10, 15, and 20. E1-3, a region spanning exons 1 and 3; E2L-3, a region spanning exon 2 long (L) form and exon 3; E2L/S-3, a region spanning exon 2 long (L) and short (S) forms and exon 3. (C) Western blot showing decreased levels of CACNA1C protein in Srf KO muscle. (D) Consensus sequence of 5’ splice donor and 3’ splice acceptor sites. (E) A topological map of CACNA1C variants. Amino acid sequence is written in small circles. Four motifs are indicated as I-IV and six transmembrane domains, S1-S6. Four pore regions are also indicated. Colors on amino acid sequence show particular regions and domains: red, missing or inserted peptides from differentially spliced exons; purple, voltage sensors in S4 transmembrane domains; green, start codons found in differentially spliced variants (*, start codons deduced from indicated exons that are differentially spliced; blue, β subunit binding domain; brown, CaM (calmodulin) binding domain; orange, PKA (protein kinase A) phosphorylation site. Alignment of alternatively spliced exons E9/10, E24/25, and E32/33 are shown. (F) Isometric force recordings from antrum and colon of WT and KO mice. Bay K8644 (1 μM) and high potassium (K + ) Krebs (36 mM and 72 mM) were applied to the tissues (indicated by bar and arrows). (G) The graph summarizes the results for 9 antral and 5 colonic WT and KO tissues. The responses to Bay K8644, 36 mM K + , and 72 mM K + were significantly decreased in KO antrums, and the responses to 36 mM K + and 72 mM K + were significantly reduced in KO colons compared to WT. * and ** represent p ≤ 0.05 and p ≤ 0.01 respectively.

    Journal: PLoS ONE

    Article Title: Serum response factor regulates smooth muscle contractility via myotonic dystrophy protein kinases and L-type calcium channels

    doi: 10.1371/journal.pone.0171262

    Figure Lengend Snippet: Alternations of L-type calcium channel transcripts, protein, and action potential in KO smooth muscle. (A) PCR validation of alternatively started and spliced exons of Cacna1c in WT and KO jejunum smooth muscle at KO days 5, 10, and 15. NTC is non template control. Primer sets were designed from variant exons in the regions (e.g. E1-3, forward primer spanning a region on exon 1 and reverse primer on exon 3). (B) qPCR data showing decreased expression of Cacna1c variants starting at exon 1 and exon 2 long and short forms (E1-3, E2L-3, and E2L/S-3) at KO days 5, 10, 15, and 20. E1-3, a region spanning exons 1 and 3; E2L-3, a region spanning exon 2 long (L) form and exon 3; E2L/S-3, a region spanning exon 2 long (L) and short (S) forms and exon 3. (C) Western blot showing decreased levels of CACNA1C protein in Srf KO muscle. (D) Consensus sequence of 5’ splice donor and 3’ splice acceptor sites. (E) A topological map of CACNA1C variants. Amino acid sequence is written in small circles. Four motifs are indicated as I-IV and six transmembrane domains, S1-S6. Four pore regions are also indicated. Colors on amino acid sequence show particular regions and domains: red, missing or inserted peptides from differentially spliced exons; purple, voltage sensors in S4 transmembrane domains; green, start codons found in differentially spliced variants (*, start codons deduced from indicated exons that are differentially spliced; blue, β subunit binding domain; brown, CaM (calmodulin) binding domain; orange, PKA (protein kinase A) phosphorylation site. Alignment of alternatively spliced exons E9/10, E24/25, and E32/33 are shown. (F) Isometric force recordings from antrum and colon of WT and KO mice. Bay K8644 (1 μM) and high potassium (K + ) Krebs (36 mM and 72 mM) were applied to the tissues (indicated by bar and arrows). (G) The graph summarizes the results for 9 antral and 5 colonic WT and KO tissues. The responses to Bay K8644, 36 mM K + , and 72 mM K + were significantly decreased in KO antrums, and the responses to 36 mM K + and 72 mM K + were significantly reduced in KO colons compared to WT. * and ** represent p ≤ 0.05 and p ≤ 0.01 respectively.

    Article Snippet: Primary antibodies against the following antigens were used: CACNA1C (guinea pig, 1:1000, Alomone Labs, Jerusalem, Israel), SRF (rabbit, 1:500, Santa Cruz Biotechnology, Dallas, TX), or GAPDH (rabbit, 1:1500, Cell Signaling Technology, Danvers, MA).

    Techniques: Polymerase Chain Reaction, Variant Assay, Real-time Polymerase Chain Reaction, Expressing, Western Blot, Sequencing, Binding Assay, Chick Chorioallantoic Membrane Assay, Mouse Assay

    Model showing the possible molecular pathways by which SRF regulates contractility via DMPK and CACNA1C in SMC.

    Journal: PLoS ONE

    Article Title: Serum response factor regulates smooth muscle contractility via myotonic dystrophy protein kinases and L-type calcium channels

    doi: 10.1371/journal.pone.0171262

    Figure Lengend Snippet: Model showing the possible molecular pathways by which SRF regulates contractility via DMPK and CACNA1C in SMC.

    Article Snippet: Primary antibodies against the following antigens were used: CACNA1C (guinea pig, 1:1000, Alomone Labs, Jerusalem, Israel), SRF (rabbit, 1:500, Santa Cruz Biotechnology, Dallas, TX), or GAPDH (rabbit, 1:1500, Cell Signaling Technology, Danvers, MA).

    Techniques:

    Identification of a predominant subtype and alternative transcriptional variants of L-type calcium channels expressed in SMC. (A) Expression levels of L-type calcium channel subtypes in SMC of jejunum and colon. (B) Expression levels of Cacna1c variants in SMC and tissue of jejunum and colon. (C) A genomic map of Cacna1c variants. Five variable regions (V1-5) are indicated. Exons are numbered 1–48. (D) Magnified view of variable regions showing alternatively started or spliced exons (indicated as exon numbers). Seven exons containing alternative transcriptional start sequence are shown by a star (*). Long (L) and short (S) exons that are differentially started or spliced are indicated.

    Journal: PLoS ONE

    Article Title: Serum response factor regulates smooth muscle contractility via myotonic dystrophy protein kinases and L-type calcium channels

    doi: 10.1371/journal.pone.0171262

    Figure Lengend Snippet: Identification of a predominant subtype and alternative transcriptional variants of L-type calcium channels expressed in SMC. (A) Expression levels of L-type calcium channel subtypes in SMC of jejunum and colon. (B) Expression levels of Cacna1c variants in SMC and tissue of jejunum and colon. (C) A genomic map of Cacna1c variants. Five variable regions (V1-5) are indicated. Exons are numbered 1–48. (D) Magnified view of variable regions showing alternatively started or spliced exons (indicated as exon numbers). Seven exons containing alternative transcriptional start sequence are shown by a star (*). Long (L) and short (S) exons that are differentially started or spliced are indicated.

    Article Snippet: Primary antibodies against the following antigens were used: CACNA1C (guinea pig, 1:1000, Alomone Labs, Jerusalem, Israel), SRF (rabbit, 1:500, Santa Cruz Biotechnology, Dallas, TX), or GAPDH (rabbit, 1:1500, Cell Signaling Technology, Danvers, MA).

    Techniques: Expressing, Sequencing

    Structural integrity of excitation-contraction (EC) coupling junctions before and after VAD therapy of a myocarditis patient. (A,B) Raw confocal images of fixed isolated cardiomyocytes from pre- and post-VAD of the patient presented in Figures 6 , 7 , co-stained for LTCC (red), RyR (green), and JPH2 (blue) and with DAPI (not shown). (C,D) Overlay of binary images for the EC coupling proteins shown in (A,B) , with magnifications of boxed regions. The cell surface, obtained from autofluorescence, is shown white, nuclei are shown white with black asterisk. Co-localizations of LTCC, JPH2, and RyR appear cyan, magenta, yellow, or white (see color legend). (E) Cardiomyocyte JPH2 cluster density (JPH2 density) of AVSD as reference and the Pre- and Post-VAD sample. (F) Fraction of LTCC clusters that were co-localized with both RyR and JPH2, as a measure of intact EC coupling junctions ( n = 10/9 cells for Pre/Post-VAD). * p

    Journal: Frontiers in Cardiovascular Medicine

    Article Title: Severe T-System Remodeling in Pediatric Viral Myocarditis

    doi: 10.3389/fcvm.2020.624776

    Figure Lengend Snippet: Structural integrity of excitation-contraction (EC) coupling junctions before and after VAD therapy of a myocarditis patient. (A,B) Raw confocal images of fixed isolated cardiomyocytes from pre- and post-VAD of the patient presented in Figures 6 , 7 , co-stained for LTCC (red), RyR (green), and JPH2 (blue) and with DAPI (not shown). (C,D) Overlay of binary images for the EC coupling proteins shown in (A,B) , with magnifications of boxed regions. The cell surface, obtained from autofluorescence, is shown white, nuclei are shown white with black asterisk. Co-localizations of LTCC, JPH2, and RyR appear cyan, magenta, yellow, or white (see color legend). (E) Cardiomyocyte JPH2 cluster density (JPH2 density) of AVSD as reference and the Pre- and Post-VAD sample. (F) Fraction of LTCC clusters that were co-localized with both RyR and JPH2, as a measure of intact EC coupling junctions ( n = 10/9 cells for Pre/Post-VAD). * p

    Article Snippet: Primary antibodies against JPH2 (Thermo Fisher, 40-5300), LTCC (Alomone, AGP-001), and RyR (Thermo Fisher, MA3 916) were diluted 1:200 in staining solution (phosphate buffered saline, PBS, supplemented with 1% BSA, 5% normal goat serum, 0.25% TritonX-100) and incubated for a minimum of 16h in the dark at 4°C.

    Techniques: Isolation, Staining