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cmlck  (WuXi AppTec)


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    WuXi AppTec cmlck
    Cmlck, supplied by WuXi AppTec, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/cmlck/cmlck+antibody/us11760987-320-7-10
    Average 90 stars, based on 1 article reviews
    cmlck - by Bioz Stars, 2026-10
    90/100 stars

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    Article Title: Cardiac-Directed Expression of Adenylyl Cyclase Catalytic Domain Reverses Cardiac Dysfunction Caused by Sustained Beta-Adrenergic Receptor Stimulation
    Article Snippet: Additional antibodies included GAPDH (1:20,000 dilution; Fitzgerald); cMLCK (1:1,000 dilution; Abgent, San Diego, California); MLC2v (1:1,000 dilution; Synaptic Systems, Gottingen, Germany), PKA catalytic subunit (1:1,000 dilution; BD Transduction, San Jose, California); p-ERK1/2, p38, p-PKARII α and β (1:200 dilution; Santa Cruz Biotechnology); PLB (1:5,000 dilution; Affinity Bioreagents, Rockford, Illinois); phospho-16-PLB (1:3,000 dilution; Badrilla, Leeds, United Kingdom); S100A1 (1:1,000 dilution; Acris); SERCA2a antibody (1:1,000 dilution; Enzo, Exeter, United Kingdom); phospho-αB-crystallin (CryAB) and total CryAB antibodies (1:1,000 dilution; Enzo); P-308-Akt, P-473-Akt, T-Akt, p-GSK3a/b, p-MDM2, P-p70S6K, T-p70S6K, and phospho-S22/23 troponin I (TnI) (1:1,000 dilution each; Cell Signaling, Danvers, Massachusetts); vinculin (1:100,1000 dilution; Sigma, Darmstadt, Germany).

    Article Title: Compositions and methods for the treatment or prevention of heart failure
    Article Snippet: Additional antibodies included GAPDH (1:20,000 dilution; Fitzgerald); cMLCK (1:1,000 dilution; Abgent, San Diego, Calif.); MLC2v (1:1,000 dilution; Synaptic Systems, Gottingen, Germany), PKA catalytic subunit (1:1,000 dilution; BD Transduction, San Jose, Calif.); p-ERK1/2, p38, p-PKARII a and b (1:200 dilution; Santa Cruz Biotechnology); PLB (1:5,000 dilution; Affinity Bioreagents, Rockford, Ill.); phospho-16-PLB (1:3,000 dilution; Badrilla, Leeds, United Kingdom); S100A1 (1:1,000 dilution; Acris); SERCA2a antibody (1:1,000 dilution; Enzo, Exeter, United Kingdom); phospho-aB-crystallin (CryAB) and total CryAB antibodies (1:1,000 dilution; Enzo); P-308-Akt, P-473-Akt, T-Akt, p-GSK3a/b, p-MDM2, P-p70S6K, p70S6K, and phospho-S22/23 troponin I (TnI) (1:1,000 dilution each; Cell Signaling, Danvers, Mass.); vinculin (1:100,1000 dilution; Sigma, Darmstadt, Germany).



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    In situ phosphorylation of cTnI and cRLC by <t>cMLCK</t> in troponin-exchanged rat ventricular trabeculae. A , recombinant cardiac troponin exchange efficiency in ventricular trabeculae, determined by Western blotting against cTnT. Endogenous native rat cTnT ( left ) migrates faster in SDS-PAGE than recombinant human cTnT ( right ), allowing estimation of the cTn exchange efficiency into rat ventricular trabeculae ( center ). Mean ± S.E., n = 3. B , low-molecular-weight portion of SDS-PAGE of ventricular trabeculae treated without (−) and with (+) protein kinase inhibitors (H-89 and staurosporine). Gels were stained with phospho-specific Pro-Q Diamond or SYPRO total protein stain. Densitometric analysis for cTnI is shown on the right . Means ± S.E., n = 6. C and D , rat cTn-exchanged ( C ) or human cTn-exchanged ( D ) demembranated ventricular trabeculae were incubated without (− cMLCK , time-matched control) or with cMLCK (+ cMLCK ), and phosphorylation levels were determined by Phos-tag TM SDS-PAGE, followed by Western blotting against cTnI ( top ) and cRLC ( bottom ). Unphosphorylated human cTnI (indicated by 0P' ) migrates faster than unphosphorylated rat cTnI ( 0P ). TnI degradation products are labeled accordingly ( Deg ). Ponceau stains for endogenous rat ( rcTnT ) and exogenous human cardiac troponin T ( hcTnT ) are shown in the center panels. E , densitometric analysis of cTnI ( top ) and cRLC phosphorylation ( bottom ) levels before (−) and after cMLCK (+) incubation in C and D . Means ± S.E., n = 3–6. Statistical significance of differences was assessed with an unpaired, two-tailed Student's t test. ns , not significant; *, p < 0.05; ***, p < 0.001.
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    In situ phosphorylation of cTnI and cRLC by <t>cMLCK</t> in troponin-exchanged rat ventricular trabeculae. A , recombinant cardiac troponin exchange efficiency in ventricular trabeculae, determined by Western blotting against cTnT. Endogenous native rat cTnT ( left ) migrates faster in SDS-PAGE than recombinant human cTnT ( right ), allowing estimation of the cTn exchange efficiency into rat ventricular trabeculae ( center ). Mean ± S.E., n = 3. B , low-molecular-weight portion of SDS-PAGE of ventricular trabeculae treated without (−) and with (+) protein kinase inhibitors (H-89 and staurosporine). Gels were stained with phospho-specific Pro-Q Diamond or SYPRO total protein stain. Densitometric analysis for cTnI is shown on the right . Means ± S.E., n = 6. C and D , rat cTn-exchanged ( C ) or human cTn-exchanged ( D ) demembranated ventricular trabeculae were incubated without (− cMLCK , time-matched control) or with cMLCK (+ cMLCK ), and phosphorylation levels were determined by Phos-tag TM SDS-PAGE, followed by Western blotting against cTnI ( top ) and cRLC ( bottom ). Unphosphorylated human cTnI (indicated by 0P' ) migrates faster than unphosphorylated rat cTnI ( 0P ). TnI degradation products are labeled accordingly ( Deg ). Ponceau stains for endogenous rat ( rcTnT ) and exogenous human cardiac troponin T ( hcTnT ) are shown in the center panels. E , densitometric analysis of cTnI ( top ) and cRLC phosphorylation ( bottom ) levels before (−) and after cMLCK (+) incubation in C and D . Means ± S.E., n = 3–6. Statistical significance of differences was assessed with an unpaired, two-tailed Student's t test. ns , not significant; *, p < 0.05; ***, p < 0.001.
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    In situ phosphorylation of cTnI and cRLC by <t>cMLCK</t> in troponin-exchanged rat ventricular trabeculae. A , recombinant cardiac troponin exchange efficiency in ventricular trabeculae, determined by Western blotting against cTnT. Endogenous native rat cTnT ( left ) migrates faster in SDS-PAGE than recombinant human cTnT ( right ), allowing estimation of the cTn exchange efficiency into rat ventricular trabeculae ( center ). Mean ± S.E., n = 3. B , low-molecular-weight portion of SDS-PAGE of ventricular trabeculae treated without (−) and with (+) protein kinase inhibitors (H-89 and staurosporine). Gels were stained with phospho-specific Pro-Q Diamond or SYPRO total protein stain. Densitometric analysis for cTnI is shown on the right . Means ± S.E., n = 6. C and D , rat cTn-exchanged ( C ) or human cTn-exchanged ( D ) demembranated ventricular trabeculae were incubated without (− cMLCK , time-matched control) or with cMLCK (+ cMLCK ), and phosphorylation levels were determined by Phos-tag TM SDS-PAGE, followed by Western blotting against cTnI ( top ) and cRLC ( bottom ). Unphosphorylated human cTnI (indicated by 0P' ) migrates faster than unphosphorylated rat cTnI ( 0P ). TnI degradation products are labeled accordingly ( Deg ). Ponceau stains for endogenous rat ( rcTnT ) and exogenous human cardiac troponin T ( hcTnT ) are shown in the center panels. E , densitometric analysis of cTnI ( top ) and cRLC phosphorylation ( bottom ) levels before (−) and after cMLCK (+) incubation in C and D . Means ± S.E., n = 3–6. Statistical significance of differences was assessed with an unpaired, two-tailed Student's t test. ns , not significant; *, p < 0.05; ***, p < 0.001.
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    In situ phosphorylation of cTnI and cRLC by <t>cMLCK</t> in troponin-exchanged rat ventricular trabeculae. A , recombinant cardiac troponin exchange efficiency in ventricular trabeculae, determined by Western blotting against cTnT. Endogenous native rat cTnT ( left ) migrates faster in SDS-PAGE than recombinant human cTnT ( right ), allowing estimation of the cTn exchange efficiency into rat ventricular trabeculae ( center ). Mean ± S.E., n = 3. B , low-molecular-weight portion of SDS-PAGE of ventricular trabeculae treated without (−) and with (+) protein kinase inhibitors (H-89 and staurosporine). Gels were stained with phospho-specific Pro-Q Diamond or SYPRO total protein stain. Densitometric analysis for cTnI is shown on the right . Means ± S.E., n = 6. C and D , rat cTn-exchanged ( C ) or human cTn-exchanged ( D ) demembranated ventricular trabeculae were incubated without (− cMLCK , time-matched control) or with cMLCK (+ cMLCK ), and phosphorylation levels were determined by Phos-tag TM SDS-PAGE, followed by Western blotting against cTnI ( top ) and cRLC ( bottom ). Unphosphorylated human cTnI (indicated by 0P' ) migrates faster than unphosphorylated rat cTnI ( 0P ). TnI degradation products are labeled accordingly ( Deg ). Ponceau stains for endogenous rat ( rcTnT ) and exogenous human cardiac troponin T ( hcTnT ) are shown in the center panels. E , densitometric analysis of cTnI ( top ) and cRLC phosphorylation ( bottom ) levels before (−) and after cMLCK (+) incubation in C and D . Means ± S.E., n = 3–6. Statistical significance of differences was assessed with an unpaired, two-tailed Student's t test. ns , not significant; *, p < 0.05; ***, p < 0.001.
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    In situ phosphorylation of cTnI and cRLC by <t>cMLCK</t> in troponin-exchanged rat ventricular trabeculae. A , recombinant cardiac troponin exchange efficiency in ventricular trabeculae, determined by Western blotting against cTnT. Endogenous native rat cTnT ( left ) migrates faster in SDS-PAGE than recombinant human cTnT ( right ), allowing estimation of the cTn exchange efficiency into rat ventricular trabeculae ( center ). Mean ± S.E., n = 3. B , low-molecular-weight portion of SDS-PAGE of ventricular trabeculae treated without (−) and with (+) protein kinase inhibitors (H-89 and staurosporine). Gels were stained with phospho-specific Pro-Q Diamond or SYPRO total protein stain. Densitometric analysis for cTnI is shown on the right . Means ± S.E., n = 6. C and D , rat cTn-exchanged ( C ) or human cTn-exchanged ( D ) demembranated ventricular trabeculae were incubated without (− cMLCK , time-matched control) or with cMLCK (+ cMLCK ), and phosphorylation levels were determined by Phos-tag TM SDS-PAGE, followed by Western blotting against cTnI ( top ) and cRLC ( bottom ). Unphosphorylated human cTnI (indicated by 0P' ) migrates faster than unphosphorylated rat cTnI ( 0P ). TnI degradation products are labeled accordingly ( Deg ). Ponceau stains for endogenous rat ( rcTnT ) and exogenous human cardiac troponin T ( hcTnT ) are shown in the center panels. E , densitometric analysis of cTnI ( top ) and cRLC phosphorylation ( bottom ) levels before (−) and after cMLCK (+) incubation in C and D . Means ± S.E., n = 3–6. Statistical significance of differences was assessed with an unpaired, two-tailed Student's t test. ns , not significant; *, p < 0.05; ***, p < 0.001.
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    In situ phosphorylation of cTnI and cRLC by cMLCK in troponin-exchanged rat ventricular trabeculae. A , recombinant cardiac troponin exchange efficiency in ventricular trabeculae, determined by Western blotting against cTnT. Endogenous native rat cTnT ( left ) migrates faster in SDS-PAGE than recombinant human cTnT ( right ), allowing estimation of the cTn exchange efficiency into rat ventricular trabeculae ( center ). Mean ± S.E., n = 3. B , low-molecular-weight portion of SDS-PAGE of ventricular trabeculae treated without (−) and with (+) protein kinase inhibitors (H-89 and staurosporine). Gels were stained with phospho-specific Pro-Q Diamond or SYPRO total protein stain. Densitometric analysis for cTnI is shown on the right . Means ± S.E., n = 6. C and D , rat cTn-exchanged ( C ) or human cTn-exchanged ( D ) demembranated ventricular trabeculae were incubated without (− cMLCK , time-matched control) or with cMLCK (+ cMLCK ), and phosphorylation levels were determined by Phos-tag TM SDS-PAGE, followed by Western blotting against cTnI ( top ) and cRLC ( bottom ). Unphosphorylated human cTnI (indicated by 0P' ) migrates faster than unphosphorylated rat cTnI ( 0P ). TnI degradation products are labeled accordingly ( Deg ). Ponceau stains for endogenous rat ( rcTnT ) and exogenous human cardiac troponin T ( hcTnT ) are shown in the center panels. E , densitometric analysis of cTnI ( top ) and cRLC phosphorylation ( bottom ) levels before (−) and after cMLCK (+) incubation in C and D . Means ± S.E., n = 3–6. Statistical significance of differences was assessed with an unpaired, two-tailed Student's t test. ns , not significant; *, p < 0.05; ***, p < 0.001.

    Journal: The Journal of Biological Chemistry

    Article Title: Cardiac myosin regulatory light chain kinase modulates cardiac contractility by phosphorylating both myosin regulatory light chain and troponin I

    doi: 10.1074/jbc.RA119.011945

    Figure Lengend Snippet: In situ phosphorylation of cTnI and cRLC by cMLCK in troponin-exchanged rat ventricular trabeculae. A , recombinant cardiac troponin exchange efficiency in ventricular trabeculae, determined by Western blotting against cTnT. Endogenous native rat cTnT ( left ) migrates faster in SDS-PAGE than recombinant human cTnT ( right ), allowing estimation of the cTn exchange efficiency into rat ventricular trabeculae ( center ). Mean ± S.E., n = 3. B , low-molecular-weight portion of SDS-PAGE of ventricular trabeculae treated without (−) and with (+) protein kinase inhibitors (H-89 and staurosporine). Gels were stained with phospho-specific Pro-Q Diamond or SYPRO total protein stain. Densitometric analysis for cTnI is shown on the right . Means ± S.E., n = 6. C and D , rat cTn-exchanged ( C ) or human cTn-exchanged ( D ) demembranated ventricular trabeculae were incubated without (− cMLCK , time-matched control) or with cMLCK (+ cMLCK ), and phosphorylation levels were determined by Phos-tag TM SDS-PAGE, followed by Western blotting against cTnI ( top ) and cRLC ( bottom ). Unphosphorylated human cTnI (indicated by 0P' ) migrates faster than unphosphorylated rat cTnI ( 0P ). TnI degradation products are labeled accordingly ( Deg ). Ponceau stains for endogenous rat ( rcTnT ) and exogenous human cardiac troponin T ( hcTnT ) are shown in the center panels. E , densitometric analysis of cTnI ( top ) and cRLC phosphorylation ( bottom ) levels before (−) and after cMLCK (+) incubation in C and D . Means ± S.E., n = 3–6. Statistical significance of differences was assessed with an unpaired, two-tailed Student's t test. ns , not significant; *, p < 0.05; ***, p < 0.001.

    Article Snippet: Cardiac troponins were gel-filtered into cMLCK assay buffer (50 mmol/liter HEPES, 50 mmol/liter NaCl, 2 mmol/liter MgCl 2 , 1 mmol/liter CaCl 2 , and 1 mmol/liter DTT) via NAP5 columns (GE Healthcare).

    Techniques: In Situ, Recombinant, Western Blot, SDS Page, Molecular Weight, Staining, Incubation, Labeling, Two Tailed Test