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ltcc α 1c (Alomone Labs)

Name: ltcc α 1c
Brand: Alomone Labs
Rating: 90 (44 reviews)

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Alomone Labs ltcc α 1c

Effects of Flu on the levels of <t>LTCC</t> <t>α</t> <t>1C</t> protein determined by western blot analysis. PDGF time-dependently inhibited LTCC α 1C expression, which could be prevented by fluvastatin. (a) Dose-effect response of PDGF stimulation on the LTCC α 1C expression in VSMCs. (b) Time-effect response of Flu on the LTCC α 1C expression incubated by PDGF. β-actin served as the loading control. Data was represented as means ± SE of 3 separate experiments conducted in triplicate. * P < 0.05 versus blank control and # P < 0.05 versus cells incubation with PDGF. LTCC α 1C : L-type calcium channel α 1C subunit; Flu: fluvastatin; and PDGF: platelet derived growth factor.

Ltcc α 1c, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 90/100, based on 44 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/ltcc α 1c/product/Alomone Labs
Average 90 stars, based on 44 article reviews

ltcc α 1c - by Bioz Stars, 2026-02

90/100 stars

Images

1) Product Images from "Fluvastatin Upregulates the α 1C Subunit of CaV1.2 Channel Expression in Vascular Smooth Muscle Cells via RhoA and ERK/p38 MAPK Pathways"

Article Title: Fluvastatin Upregulates the α 1C Subunit of CaV1.2 Channel Expression in Vascular Smooth Muscle Cells via RhoA and ERK/p38 MAPK Pathways

Journal: Disease Markers

doi: 10.1155/2014/237067

Effects of Flu on the levels of LTCC α 1C protein determined by western blot analysis. PDGF time-dependently inhibited LTCC α 1C expression, which could be prevented by fluvastatin. (a) Dose-effect response of PDGF stimulation on the LTCC α 1C expression in VSMCs. (b) Time-effect response of Flu on the LTCC α 1C expression incubated by PDGF. β-actin served as the loading control. Data was represented as means ± SE of 3 separate experiments conducted in triplicate. * P < 0.05 versus blank control and # P < 0.05 versus cells incubation with PDGF. LTCC α 1C : L-type calcium channel α 1C subunit; Flu: fluvastatin; and PDGF: platelet derived growth factor.

Figure Legend Snippet: Effects of Flu on the levels of LTCC α 1C protein determined by western blot analysis. PDGF time-dependently inhibited LTCC α 1C expression, which could be prevented by fluvastatin. (a) Dose-effect response of PDGF stimulation on the LTCC α 1C expression in VSMCs. (b) Time-effect response of Flu on the LTCC α 1C expression incubated by PDGF. β-actin served as the loading control. Data was represented as means ± SE of 3 separate experiments conducted in triplicate. * P < 0.05 versus blank control and # P < 0.05 versus cells incubation with PDGF. LTCC α 1C : L-type calcium channel α 1C subunit; Flu: fluvastatin; and PDGF: platelet derived growth factor.

Techniques Used: Western Blot, Expressing, Incubation, Derivative Assay

Effects of MAPK or ROCK inhibition on LTCC α 1C expression after PDGF stimulation in VSMCs. LTCC α 1C protein expression was evaluated by western blot analysis. Data was described as means ± SEM from three experiments performed in triplicate. * P < 0.05 versus blank control and # P < 0.05 versus PDGF stimulated cells. MAPK: mitogen activated protein kinase; ROCK: Rho associated protein kinase; LTCC α 1C : L-type calcium channel α 1C subunit; Flu: fluvastatin; and PDGF: platelet derived growth factor.

Figure Legend Snippet: Effects of MAPK or ROCK inhibition on LTCC α 1C expression after PDGF stimulation in VSMCs. LTCC α 1C protein expression was evaluated by western blot analysis. Data was described as means ± SEM from three experiments performed in triplicate. * P < 0.05 versus blank control and # P < 0.05 versus PDGF stimulated cells. MAPK: mitogen activated protein kinase; ROCK: Rho associated protein kinase; LTCC α 1C : L-type calcium channel α 1C subunit; Flu: fluvastatin; and PDGF: platelet derived growth factor.

Techniques Used: Inhibition, Expressing, Western Blot, Derivative Assay

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Journal: Disease Markers

Article Title: Fluvastatin Upregulates the α 1C Subunit of CaV1.2 Channel Expression in Vascular Smooth Muscle Cells via RhoA and ERK/p38 MAPK Pathways

doi: 10.1155/2014/237067

Figure Lengend Snippet: Effects of Flu on the levels of LTCC α 1C protein determined by western blot analysis. PDGF time-dependently inhibited LTCC α 1C expression, which could be prevented by fluvastatin. (a) Dose-effect response of PDGF stimulation on the LTCC α 1C expression in VSMCs. (b) Time-effect response of Flu on the LTCC α 1C expression incubated by PDGF. β-actin served as the loading control. Data was represented as means ± SE of 3 separate experiments conducted in triplicate. * P < 0.05 versus blank control and # P < 0.05 versus cells incubation with PDGF. LTCC α 1C : L-type calcium channel α 1C subunit; Flu: fluvastatin; and PDGF: platelet derived growth factor.

Article Snippet: Primary antibodies were used at the indicated dilutions as follows: LTCC α 1C , 1 : 200 (Alomone); β -actin, 1 : 1000; anti-p-p38 MAPK, 1 : 1000; anti-total-p38 MAPK, 1 : 1000; anti-p-JNK, 1 : 1000; anti-total-JNK 1 : 1000; anti-p-ERK1/2 (1 : 1000); and anti-total-ERK1/2 (1 : 1000); all were from Cell Signalling Technology (Danvers, MA).

Techniques: Western Blot, Expressing, Incubation, Derivative Assay

Journal: Disease Markers

Article Title: Fluvastatin Upregulates the α 1C Subunit of CaV1.2 Channel Expression in Vascular Smooth Muscle Cells via RhoA and ERK/p38 MAPK Pathways

doi: 10.1155/2014/237067

Figure Lengend Snippet: Effects of MAPK or ROCK inhibition on LTCC α 1C expression after PDGF stimulation in VSMCs. LTCC α 1C protein expression was evaluated by western blot analysis. Data was described as means ± SEM from three experiments performed in triplicate. * P < 0.05 versus blank control and # P < 0.05 versus PDGF stimulated cells. MAPK: mitogen activated protein kinase; ROCK: Rho associated protein kinase; LTCC α 1C : L-type calcium channel α 1C subunit; Flu: fluvastatin; and PDGF: platelet derived growth factor.

Techniques: Inhibition, Expressing, Western Blot, Derivative Assay

MβCD decreases the phosphorylation level of the β 2 subunit of L-type calcium channels (LTCCs). The phosphorylation level of the β 2 subunit of LTCCs was measured by Western blotting, as indicated below, after the incubation of CGNs in MLocke’s K25 plus 1 or 5 mM of MβCD for 15 min at 37 °C in a 5% CO 2 culture chamber. After SDS-PAGE (7.5% acrylamide), the proteins were transferred to PVDF membranes for Western blotting, as indicated in the Materials and Methods. The positions of the molecular weight marker bands closest to the target proteins of the primary antibodies, i.e., β 2 subunit of LTCCs, LTCC α 1C subunit, and β-actin, are shown at the left or right side of the corresponding PVDF membrane images. The phosphorylation levels of the β 2 subunit of LTCCs, (p)β 2 LTCC/LTCC, were measured using the ratio between the intensities of the ~73 and ~174 kDa bands obtained with rabbit antibodies: PCCb2-140AP (FabGennix Inc., Frisco, TX, USA)—dilution 1:100 [(p)β 2 LTCC]—and anti-LTCC-α 1C -subunit (Santa Cruz Biotechnology, Heidelberg, Germany, sc-25686)—dilution 1:100 [LTCC], respectively. For quantification of the ratio (p)β 2 LTCC/LTCC, the intensities of the bands were normalized first to the intensities of their corresponding ~42 kDa anti-β-actin bands (mouse anti-β-actin A1978, 0.75 µg/mL) as the internal control of protein loading. See Materials and Methods for other experimental details. Images shown are representative of the results obtained in experiments done with at least three different CGN preparations. The average results ± S.E. of triplicate experiments are presented as a bar plot. (*) p < 0.05.

Journal: International Journal of Molecular Sciences

Article Title: Methyl-β-Cyclodextrin Impairs the Phosphorylation of the β 2 Subunit of L-Type Calcium Channels and Cytosolic Calcium Homeostasis in Mature Cerebellar Granule Neurons

doi: 10.3390/ijms19113667

Figure Lengend Snippet: MβCD decreases the phosphorylation level of the β 2 subunit of L-type calcium channels (LTCCs). The phosphorylation level of the β 2 subunit of LTCCs was measured by Western blotting, as indicated below, after the incubation of CGNs in MLocke’s K25 plus 1 or 5 mM of MβCD for 15 min at 37 °C in a 5% CO 2 culture chamber. After SDS-PAGE (7.5% acrylamide), the proteins were transferred to PVDF membranes for Western blotting, as indicated in the Materials and Methods. The positions of the molecular weight marker bands closest to the target proteins of the primary antibodies, i.e., β 2 subunit of LTCCs, LTCC α 1C subunit, and β-actin, are shown at the left or right side of the corresponding PVDF membrane images. The phosphorylation levels of the β 2 subunit of LTCCs, (p)β 2 LTCC/LTCC, were measured using the ratio between the intensities of the ~73 and ~174 kDa bands obtained with rabbit antibodies: PCCb2-140AP (FabGennix Inc., Frisco, TX, USA)—dilution 1:100 [(p)β 2 LTCC]—and anti-LTCC-α 1C -subunit (Santa Cruz Biotechnology, Heidelberg, Germany, sc-25686)—dilution 1:100 [LTCC], respectively. For quantification of the ratio (p)β 2 LTCC/LTCC, the intensities of the bands were normalized first to the intensities of their corresponding ~42 kDa anti-β-actin bands (mouse anti-β-actin A1978, 0.75 µg/mL) as the internal control of protein loading. See Materials and Methods for other experimental details. Images shown are representative of the results obtained in experiments done with at least three different CGN preparations. The average results ± S.E. of triplicate experiments are presented as a bar plot. (*) p < 0.05.

Article Snippet: Primary antibodies: rabbit anti-LTCC α 1C subunit (sc-25686), rabbit anti-rabbit PKA (sc-28892), rabbit anti-CaMK-II (sc-9035), and rabbit anti-caveolin-1 (sc-894) were supplied by Santa Cruz Biotechnology (Santa Cruz, CA, USA);. rabbit anti-p-β 2 subunit of LTCCs (PCCb2-140AP) was supplied by FabGennix Inc. (Frisco, TX, USA); and mouse anti-β-actin (A1978) was supplied by Sigma-Aldrich (Spain office).

Techniques: Phospho-proteomics, Western Blot, Incubation, SDS Page, Molecular Weight, Marker, Membrane, Control

H-89 and KN-93 decrease the phosphorylation of the β 2 subunit of LTCCs to values measured in proapoptotic MLocke’s K5. ( A ) CGNs in MLocke’s K25 were incubated for 15 min at 37 °C in a 5% CO 2 culture chamber with 20 µM H-89, 30 µM KN-93, or in the absence of these inhibitors (K25 control), or after CGN incubation for 1 h at 37 °C in the 5% CO 2 culture chamber in the proapoptosis MLocke’s K5 condition (K5). ( B ) CGNs in MLocke’s K25 were incubated for 15 min at 37 °C in the 5% CO 2 culture chamber with 30 µM KN-92, 30 µM KN-93, or in the absence of these inhibitors (K25 control). After SDS-PAGE (7.5% acrylamide), the proteins were transferred to PVDF membranes for Western blotting as indicated in Materials and Methods. For panel B, the PVDF membrane was stripped twice to remove primary antibodies—anti-β 2 subunit of LTCCs and anti-LTCC α 1C subunit—and used afterward for β-actin detection. The results shown in these panels are representative of the results obtained in triplicate experiments with different CGN preparations. The position of the molecular weight marker bands closest to the target proteins of the primary antibodies, i.e., β 2 subunit of LTCC, LTCC α 1C subunit, and β-actin, are shown at the left or right side of the corresponding PVDF membrane images. Western blots were revealed by exposure to autoradiography films for ( A ) and with ChemiDoc TM XRS+ from Bio-Rad for ( B ). The phosphorylation levels of the β 2 subunit of LTCCs, (p)β 2 LTCC/LTCC, shown in the bar graphs of panels A and B, were measured as indicated in the legend for and are average results ± S.E. of triplicate experiments. (*) p < 0.05. ( C ) Time dependence of population averages of the 340/380 ratio in neuronal somas before and after the addition of 30 µM KN-93 (black-filled squares) or 30 µM KN-92 (white-filled squares) at the point indicated by the first arrow. At the point indicated by the second arrow, 10 µM nifedipine was added. Mature CGNs in culture were loaded with Fura-2, as indicated in the Materials and Methods section, and then changed to MLocke’s K25 buffer (37 °C) to start serial 340 and 380 image acquisition. Data acquisition was done as indicated in the Materials and Methods section, with exposure times lower than 0.4 s at time intervals of 30 s. The 340/380 ratio of neuronal somas was measured using the region of interest (ROI) tool of the HCImage software. The 340/380 ratio values shown are the average ± S.E. of experiments done with three different preparations of CGNs (n > 300 neuronal somas of fields taken from six plates for each experimental condition).

Journal: International Journal of Molecular Sciences

Article Title: Methyl-β-Cyclodextrin Impairs the Phosphorylation of the β 2 Subunit of L-Type Calcium Channels and Cytosolic Calcium Homeostasis in Mature Cerebellar Granule Neurons

doi: 10.3390/ijms19113667

Figure Lengend Snippet: H-89 and KN-93 decrease the phosphorylation of the β 2 subunit of LTCCs to values measured in proapoptotic MLocke’s K5. ( A ) CGNs in MLocke’s K25 were incubated for 15 min at 37 °C in a 5% CO 2 culture chamber with 20 µM H-89, 30 µM KN-93, or in the absence of these inhibitors (K25 control), or after CGN incubation for 1 h at 37 °C in the 5% CO 2 culture chamber in the proapoptosis MLocke’s K5 condition (K5). ( B ) CGNs in MLocke’s K25 were incubated for 15 min at 37 °C in the 5% CO 2 culture chamber with 30 µM KN-92, 30 µM KN-93, or in the absence of these inhibitors (K25 control). After SDS-PAGE (7.5% acrylamide), the proteins were transferred to PVDF membranes for Western blotting as indicated in Materials and Methods. For panel B, the PVDF membrane was stripped twice to remove primary antibodies—anti-β 2 subunit of LTCCs and anti-LTCC α 1C subunit—and used afterward for β-actin detection. The results shown in these panels are representative of the results obtained in triplicate experiments with different CGN preparations. The position of the molecular weight marker bands closest to the target proteins of the primary antibodies, i.e., β 2 subunit of LTCC, LTCC α 1C subunit, and β-actin, are shown at the left or right side of the corresponding PVDF membrane images. Western blots were revealed by exposure to autoradiography films for ( A ) and with ChemiDoc TM XRS+ from Bio-Rad for ( B ). The phosphorylation levels of the β 2 subunit of LTCCs, (p)β 2 LTCC/LTCC, shown in the bar graphs of panels A and B, were measured as indicated in the legend for and are average results ± S.E. of triplicate experiments. (*) p < 0.05. ( C ) Time dependence of population averages of the 340/380 ratio in neuronal somas before and after the addition of 30 µM KN-93 (black-filled squares) or 30 µM KN-92 (white-filled squares) at the point indicated by the first arrow. At the point indicated by the second arrow, 10 µM nifedipine was added. Mature CGNs in culture were loaded with Fura-2, as indicated in the Materials and Methods section, and then changed to MLocke’s K25 buffer (37 °C) to start serial 340 and 380 image acquisition. Data acquisition was done as indicated in the Materials and Methods section, with exposure times lower than 0.4 s at time intervals of 30 s. The 340/380 ratio of neuronal somas was measured using the region of interest (ROI) tool of the HCImage software. The 340/380 ratio values shown are the average ± S.E. of experiments done with three different preparations of CGNs (n > 300 neuronal somas of fields taken from six plates for each experimental condition).

Techniques: Phospho-proteomics, Incubation, Control, SDS Page, Western Blot, Membrane, Molecular Weight, Marker, Autoradiography, Software

a, b Regulatory LTCC α 2 subunit was significantly downregulated in AF animals, whereas the pore forming α 1c subunit was not affected. c AF lead to significant upregulation of the NCX1 transporter. Representative Western blots and mean (± SEM) optical density data normalized to GAPDH are displayed (n = 5 animals per group). * P < 0.05; *** P < 0.001.

Journal: PLoS ONE

Article Title: Atrial Fibrillation Complicated by Heart Failure Induces Distinct Remodeling of Calcium Cycling Proteins

doi: 10.1371/journal.pone.0116395

Figure Lengend Snippet: a, b Regulatory LTCC α 2 subunit was significantly downregulated in AF animals, whereas the pore forming α 1c subunit was not affected. c AF lead to significant upregulation of the NCX1 transporter. Representative Western blots and mean (± SEM) optical density data normalized to GAPDH are displayed (n = 5 animals per group). * P < 0.05; *** P < 0.001.

Article Snippet: Equal amounts of protein were separated on 6–20% SDS polyacrylamide gels, transferred to polyvinylidene difluoride membranes, and developed using primary antibodies directed against L-type calcium channel (LTCC) α 1c subunit (sc-25686; Santa Cruz Biotechnology, Heidelberg, Germany), LTCC α 2 subunit (ab62814; Abcam), Na + -Ca 2+ exchanger (NCX) 1 (ab2869; Abcam), catalytic protein kinase A (PKA) subunits Cα/β (ab26322; Abcam), phosphorylated regulatory PKA subunit RIIα (Ser99) (ab32390; Abcam), phospholamban (PLN) (MA3-922; Thermo Scientific, Dreieich, Germany), phosphorylated PLN (Ser16) (07-052; Upstate (Merck Millipore), Billerica, MA, USA), phosphorylated PLN (Thr17) (sc-17024-R; Santa Cruz Biotechnology, Heidelberg, Germany), Ca 2+ -calmodulin-dependent protein kinase II (CaMKII) δ (C1035-04E; Biomol, Hamburg, Germany), autophosphorylated CaMKIIδ (Thr286) (V1111; Promega, Madison, WI, USA), ryanodine receptor type 2 (RyR2) (ab2868; Abcam), phosphorylated RyR2 (Ser2808) (A010-30; Badrilla, Leeds, UK), phosphorylated RyR2 (Ser2814) (A010-31AP; Badrilla), and sarcoplasmic reticulum Ca 2+ -ATPase (Serca) 2a (sc-8095; Santa Cruz Biotechnology).

Techniques: Western Blot

Changes in protein expression are indicated by arrows (orange color). Solid black arrows indicate transport directions of Ca 2+ or Na + ions, respectively. Decreased levels of Ca 2+ -calmodulin-dependent protein kinase (CaMK) IIδ and protein kinase A (PKA) causes hypophosphorylation of phospholamban (PLN) and ryanodine receptor (RyR) 2, leading to reduced Ca 2+ uptake into the sarcoplasmic reticulum through sarcoplasmic reticulum Ca 2+ -ATPase (Serca) 2a. Increased intracellular Ca 2+ levels and upregulation of Na + -Ca 2+ exchanger (NCX) 1 expression enhance electrogenic Na + -Ca 2+ exchange. This mechanism is attenuated by reduced L-type calcium channel (LTCC) expression that limits systolic Ca 2+ influx.

Journal: PLoS ONE

Article Title: Atrial Fibrillation Complicated by Heart Failure Induces Distinct Remodeling of Calcium Cycling Proteins

doi: 10.1371/journal.pone.0116395

Figure Lengend Snippet: Changes in protein expression are indicated by arrows (orange color). Solid black arrows indicate transport directions of Ca 2+ or Na + ions, respectively. Decreased levels of Ca 2+ -calmodulin-dependent protein kinase (CaMK) IIδ and protein kinase A (PKA) causes hypophosphorylation of phospholamban (PLN) and ryanodine receptor (RyR) 2, leading to reduced Ca 2+ uptake into the sarcoplasmic reticulum through sarcoplasmic reticulum Ca 2+ -ATPase (Serca) 2a. Increased intracellular Ca 2+ levels and upregulation of Na + -Ca 2+ exchanger (NCX) 1 expression enhance electrogenic Na + -Ca 2+ exchange. This mechanism is attenuated by reduced L-type calcium channel (LTCC) expression that limits systolic Ca 2+ influx.

Techniques: Expressing

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Images

1) Product Images from "Fluvastatin Upregulates the α 1C Subunit of CaV1.2 Channel Expression in Vascular Smooth Muscle Cells via RhoA and ERK/p38 MAPK Pathways"

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