sodium stibogluconate  (Millipore)


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    Name:
    Sodium gluconate
    Description:

    Catalog Number:
    s2054
    Price:
    None
    Applications:
    Sodium gluconate has been used as a component of recording buffer used in two-electrode voltage-clamp (TEVC) recording in Xenopus laevis oocytes. It has also been used as a control for sodium.
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    Structured Review

    Millipore sodium stibogluconate
    Sodium gluconate

    https://www.bioz.com/result/sodium stibogluconate/product/Millipore
    Average 95 stars, based on 9 article reviews
    Price from $9.99 to $1999.99
    sodium stibogluconate - by Bioz Stars, 2020-08
    95/100 stars

    Images

    1) Product Images from "THEMIS enhances TCR signaling and enables positive selection by selective inhibition of SHP-1"

    Article Title: THEMIS enhances TCR signaling and enables positive selection by selective inhibition of SHP-1

    Journal: Nature immunology

    doi: 10.1038/ni.3692

    Inhibition of SHP-1 PTP activity rescues in vitro maturation of Themis −/− thymocytes Differentiation of DP thymocytes from Themis −/− or Themis +/+ to the CD4 + CD8 − stage in a two step (stimulation-rest) in vitro assay with or without the SHP-1 inhibitor Sodium stibogluconate (SSG). Left, two parameter plots show CD4 versus CD8 staining profiles of thymocytes at the completion of the differentiation assay. Cell recovery and % apoptotic (Annexin V + ) cells were not significantly different in similarly treated Themis −/− or Themis +/+ samples. Right, Summary of results. n=4 for each genotype (t-test 2-tailed type-2, error bars show SD). *** P
    Figure Legend Snippet: Inhibition of SHP-1 PTP activity rescues in vitro maturation of Themis −/− thymocytes Differentiation of DP thymocytes from Themis −/− or Themis +/+ to the CD4 + CD8 − stage in a two step (stimulation-rest) in vitro assay with or without the SHP-1 inhibitor Sodium stibogluconate (SSG). Left, two parameter plots show CD4 versus CD8 staining profiles of thymocytes at the completion of the differentiation assay. Cell recovery and % apoptotic (Annexin V + ) cells were not significantly different in similarly treated Themis −/− or Themis +/+ samples. Right, Summary of results. n=4 for each genotype (t-test 2-tailed type-2, error bars show SD). *** P

    Techniques Used: Inhibition, Activity Assay, In Vitro, Staining, Differentiation Assay, T-Test

    2) Product Images from "Protein tyrosine phosphatase 1B is a mediator of cyclic ADP ribose-induced Ca2+ signaling in ventricular myocytes"

    Article Title: Protein tyrosine phosphatase 1B is a mediator of cyclic ADP ribose-induced Ca2+ signaling in ventricular myocytes

    Journal: Experimental & Molecular Medicine

    doi: 10.1038/emm.2017.68

    Effects of a PTP1B inhibitor, an SHP1/2 inhibitor and stibogluconate on cADPR-induced increase in resting [Ca 2+ ] i in isolated rabbit ventricular myocytes ( a ) and isolated SR vesicles ( b ). ( a ) Fura 2- AM loaded myocytes were incubated with 8 μ M PTP 1B inhibitor, 300 n M SHP1/2 PTPase inhibitor or 11 μ M sodium stibogluconate for 10 min before perfusion with cADPR. Columns with vertical bars represent a quantitative summary of the maximum [Ca 2+ ] i increase after cADPR addition from five experiments. * P
    Figure Legend Snippet: Effects of a PTP1B inhibitor, an SHP1/2 inhibitor and stibogluconate on cADPR-induced increase in resting [Ca 2+ ] i in isolated rabbit ventricular myocytes ( a ) and isolated SR vesicles ( b ). ( a ) Fura 2- AM loaded myocytes were incubated with 8 μ M PTP 1B inhibitor, 300 n M SHP1/2 PTPase inhibitor or 11 μ M sodium stibogluconate for 10 min before perfusion with cADPR. Columns with vertical bars represent a quantitative summary of the maximum [Ca 2+ ] i increase after cADPR addition from five experiments. * P

    Techniques Used: Isolation, Incubation

    3) Product Images from "The Endothelial Tyrosine Phosphatase SHP-1 Plays an Important Role for Vascular Haemostasis in TNFα-Induced Inflammation In Vivo"

    Article Title: The Endothelial Tyrosine Phosphatase SHP-1 Plays an Important Role for Vascular Haemostasis in TNFα-Induced Inflammation In Vivo

    Journal: Mediators of Inflammation

    doi: 10.1155/2013/279781

    Inhibition of SHP-1 increases TNF α -induced upregulation of p-selectin and vWF in endothelial cells in vitro . (a) Incubation of endothelial cells with the pharmacological SHP-1 inhibitor sodium stibogluconate effectively reduces SHP-1 activity as measured by pNPP-dephosphorylation assay. (b) Endothelial p-selectin was not changed by sodium stibogluconate under basal conditions but, significantly upregulated in TNF α -induced endothelial inflammation. (c) vWF was already upregulated by sodium stibogluconate under basal conditions to a similar level as observed in TNF α -induced endothelial inflammation. SG: sodium stibogluconate. *Significantly different at P
    Figure Legend Snippet: Inhibition of SHP-1 increases TNF α -induced upregulation of p-selectin and vWF in endothelial cells in vitro . (a) Incubation of endothelial cells with the pharmacological SHP-1 inhibitor sodium stibogluconate effectively reduces SHP-1 activity as measured by pNPP-dephosphorylation assay. (b) Endothelial p-selectin was not changed by sodium stibogluconate under basal conditions but, significantly upregulated in TNF α -induced endothelial inflammation. (c) vWF was already upregulated by sodium stibogluconate under basal conditions to a similar level as observed in TNF α -induced endothelial inflammation. SG: sodium stibogluconate. *Significantly different at P

    Techniques Used: Inhibition, In Vitro, Incubation, Activity Assay, De-Phosphorylation Assay

    Inhibtion SHP-1 does not affect platelet aggregation in vitro and ex vivo . (a) In platelet-rich plasma (PRP) from healthy human volunteers SHP-1 inhibition by sodium stibogluconate did not increase platelet aggregation neither under basal conditions nor after pretreatment with TNF α (5 ng/mL, 4 h) upon stimulation with the platelet agonists ADP, collagen, or thrombin-receptor activating peptide (TRAP) in different concentrations (low ADP: 0.5–1 μ M; high ADP: 10 μ M; low collagen: 0.5–4 μ g/mL; high collagen: 10 μ g/mL; low TRAP: 1–1.5 μ M; high TRAP: 10–14 μ M; n = 9–12, each). (b) Treatment of animals with the SHP-1 inhibitor sodium stibogluconate (10 μ g/mL, 30 min) did not affect ADP-induced (6.5 μ M) platelet aggregation ex vivo , neither under basal conditions nor in TNF α -induced inflammation (TNF α 5 ng/mL, 4 h, n = 6 animals per group). SG: sodium stibogluconate, AU: arbitrary unite.
    Figure Legend Snippet: Inhibtion SHP-1 does not affect platelet aggregation in vitro and ex vivo . (a) In platelet-rich plasma (PRP) from healthy human volunteers SHP-1 inhibition by sodium stibogluconate did not increase platelet aggregation neither under basal conditions nor after pretreatment with TNF α (5 ng/mL, 4 h) upon stimulation with the platelet agonists ADP, collagen, or thrombin-receptor activating peptide (TRAP) in different concentrations (low ADP: 0.5–1 μ M; high ADP: 10 μ M; low collagen: 0.5–4 μ g/mL; high collagen: 10 μ g/mL; low TRAP: 1–1.5 μ M; high TRAP: 10–14 μ M; n = 9–12, each). (b) Treatment of animals with the SHP-1 inhibitor sodium stibogluconate (10 μ g/mL, 30 min) did not affect ADP-induced (6.5 μ M) platelet aggregation ex vivo , neither under basal conditions nor in TNF α -induced inflammation (TNF α 5 ng/mL, 4 h, n = 6 animals per group). SG: sodium stibogluconate, AU: arbitrary unite.

    Techniques Used: In Vitro, Ex Vivo, Inhibition

    Inhibition of SHP-1 leads to increased platelet rolling in vivo in TNF α -induced systemic inflammation. (a) In vivo the amount of rolling platelets (defined as platelets with a velocity of less than 5% of maximal velocity) as analyzed by intravital microscopy in the dorsal skinfold chamber was slightly enhanced in vivo after treatment with the SHP-1 inhibitor sodium stibogluconate (10 μ g/mL, 30 min) under basal conditions but significantly increased in TNF α -induced inflammation (TNF α 5 ng/mL, 4 h). (b) Inhibition of SHP-1 by sodium stibogluconate in TNF α -induced inflammation resulted in a leftward shift in platelet velocity distribution pattern (i.e., towards lower platelet velocities) in the frequency histogram, indicating increased transient platelet interaction with the endothelium. The histograms display all platelet velocities from 5 different animals per group. SG: sodium stibogluconate. *Significantly different at P
    Figure Legend Snippet: Inhibition of SHP-1 leads to increased platelet rolling in vivo in TNF α -induced systemic inflammation. (a) In vivo the amount of rolling platelets (defined as platelets with a velocity of less than 5% of maximal velocity) as analyzed by intravital microscopy in the dorsal skinfold chamber was slightly enhanced in vivo after treatment with the SHP-1 inhibitor sodium stibogluconate (10 μ g/mL, 30 min) under basal conditions but significantly increased in TNF α -induced inflammation (TNF α 5 ng/mL, 4 h). (b) Inhibition of SHP-1 by sodium stibogluconate in TNF α -induced inflammation resulted in a leftward shift in platelet velocity distribution pattern (i.e., towards lower platelet velocities) in the frequency histogram, indicating increased transient platelet interaction with the endothelium. The histograms display all platelet velocities from 5 different animals per group. SG: sodium stibogluconate. *Significantly different at P

    Techniques Used: Inhibition, In Vivo, Intravital Microscopy

    Inhibition of SHP-1 leads to accelerated arteriolar thrombus formation in vivo . Time to thrombotic arteriolar vessel occlusion in vivo , as measured in the ferric chloride superfusion model in the dorsal skinfold chamber in mice, was significantly accelerated when animals were treated with the SHP-1 inhibitor sodium stibogluconate (10 μ g/mL, 30 min) under basal conditions. TNF α -induced inflammation itself (TNF α 5 ng/mL, 4 h) led to accelerated thrombus formation, but the effect was further increased by SHP-1 inhibition. SG: sodium stibogluconate. *Significantly different at P
    Figure Legend Snippet: Inhibition of SHP-1 leads to accelerated arteriolar thrombus formation in vivo . Time to thrombotic arteriolar vessel occlusion in vivo , as measured in the ferric chloride superfusion model in the dorsal skinfold chamber in mice, was significantly accelerated when animals were treated with the SHP-1 inhibitor sodium stibogluconate (10 μ g/mL, 30 min) under basal conditions. TNF α -induced inflammation itself (TNF α 5 ng/mL, 4 h) led to accelerated thrombus formation, but the effect was further increased by SHP-1 inhibition. SG: sodium stibogluconate. *Significantly different at P

    Techniques Used: Inhibition, In Vivo, Mouse Assay

    4) Product Images from "Early T Cell Signalling Is Reversibly Altered in PD-1+ T Lymphocytes Infiltrating Human Tumors"

    Article Title: Early T Cell Signalling Is Reversibly Altered in PD-1+ T Lymphocytes Infiltrating Human Tumors

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0017621

    PD-1 expression delivers an inhibitory signal attenuated by sodium stibogluconate. ( A ) Typical average Ca responses elicited by anti-CD3 (arrow) in melanoma TIL, treated or not for 20 min with SSG. ( B ) Average Ca responses in TIL treated or not with SSG (n = 12 tumors). ( C ) Top: fluorescence images of PD-1 and YFP-transfected PBT. Bottom: typical average Ca responses triggered by anti-CD3 (arrows) in YFP + and PD-1 + transfectants (left) and in PD1 + transfectants treated or not with SSG (right). ( D ) Average Ca response (in % of the response in YFP + cells) in YFP + and PD-1 + transfectants treated or not with SSG (n = 7 independent experiments). Data represent mean +/− SEM * p
    Figure Legend Snippet: PD-1 expression delivers an inhibitory signal attenuated by sodium stibogluconate. ( A ) Typical average Ca responses elicited by anti-CD3 (arrow) in melanoma TIL, treated or not for 20 min with SSG. ( B ) Average Ca responses in TIL treated or not with SSG (n = 12 tumors). ( C ) Top: fluorescence images of PD-1 and YFP-transfected PBT. Bottom: typical average Ca responses triggered by anti-CD3 (arrows) in YFP + and PD-1 + transfectants (left) and in PD1 + transfectants treated or not with SSG (right). ( D ) Average Ca response (in % of the response in YFP + cells) in YFP + and PD-1 + transfectants treated or not with SSG (n = 7 independent experiments). Data represent mean +/− SEM * p

    Techniques Used: Expressing, Fluorescence, Transfection

    5) Product Images from "FcεRI γ-Chain Negatively Modulates Dectin-1 Responses in Dendritic Cells"

    Article Title: FcεRI γ-Chain Negatively Modulates Dectin-1 Responses in Dendritic Cells

    Journal: Frontiers in Immunology

    doi: 10.3389/fimmu.2017.01424

    Phosphatases were recruited by FcRγ and negatively regulated Dectin-1 responses in DCs. Six-day-cultured BMDCs derived from WT mice were collected and treated with dZym. (A) Cell lysates were collected at indicated time points and incubated with anti-FcRγ Ab. After 16 h, protein A/G beads were added for precipitation. The phosphatases SHIP-1, SHP-1, SHP-2, and PTEN in whole cell lysate or associated proteins with FcRγ were detected by SDS-PAGE and Western blot. Quantification was determined by densitometry using ImageJ software. (B) BMDCs were incubated with sodium stibogluconate (SS) (SHP-1 inhibitor) or SF1670 (PTEN inhibitor) for 1 h before dZym treatment. After 16 h, the expressions of CD80, CD86, and MHC-II were detected by flow cytometry. The changes of MFIs from control to treatment are indicated in each histogram. Gray areas represented the isotype-matched Ig controls. All data shown were representative from three to five independent experiments.
    Figure Legend Snippet: Phosphatases were recruited by FcRγ and negatively regulated Dectin-1 responses in DCs. Six-day-cultured BMDCs derived from WT mice were collected and treated with dZym. (A) Cell lysates were collected at indicated time points and incubated with anti-FcRγ Ab. After 16 h, protein A/G beads were added for precipitation. The phosphatases SHIP-1, SHP-1, SHP-2, and PTEN in whole cell lysate or associated proteins with FcRγ were detected by SDS-PAGE and Western blot. Quantification was determined by densitometry using ImageJ software. (B) BMDCs were incubated with sodium stibogluconate (SS) (SHP-1 inhibitor) or SF1670 (PTEN inhibitor) for 1 h before dZym treatment. After 16 h, the expressions of CD80, CD86, and MHC-II were detected by flow cytometry. The changes of MFIs from control to treatment are indicated in each histogram. Gray areas represented the isotype-matched Ig controls. All data shown were representative from three to five independent experiments.

    Techniques Used: Cell Culture, Derivative Assay, Mouse Assay, Incubation, SDS Page, Western Blot, Software, Flow Cytometry, Cytometry

    6) Product Images from "A Telomeric Cluster of Antimony Resistance Genes on Chromosome 34 of Leishmania infantum"

    Article Title: A Telomeric Cluster of Antimony Resistance Genes on Chromosome 34 of Leishmania infantum

    Journal: Antimicrobial Agents and Chemotherapy

    doi: 10.1128/AAC.00544-16

    (A) In vitro infection of bone marrow-derived macrophages and treatment with sodium stibogluconate. L. donovani parasites transfected with the vector, ARM58, ARM56, HSP23, or the ARM58-ARM56 transgene were used to infect BMMs at an MOI of 5:1. After 24
    Figure Legend Snippet: (A) In vitro infection of bone marrow-derived macrophages and treatment with sodium stibogluconate. L. donovani parasites transfected with the vector, ARM58, ARM56, HSP23, or the ARM58-ARM56 transgene were used to infect BMMs at an MOI of 5:1. After 24

    Techniques Used: In Vitro, Infection, Derivative Assay, Transfection, Plasmid Preparation

    7) Product Images from "Protein tyrosine phosphatase 1B is a mediator of cyclic ADP ribose-induced Ca2+ signaling in ventricular myocytes"

    Article Title: Protein tyrosine phosphatase 1B is a mediator of cyclic ADP ribose-induced Ca2+ signaling in ventricular myocytes

    Journal: Experimental & Molecular Medicine

    doi: 10.1038/emm.2017.68

    Effects of a PTP1B inhibitor, an SHP1/2 inhibitor and stibogluconate on cADPR-induced increase in resting [Ca 2+ ] i in isolated rabbit ventricular myocytes ( a ) and isolated SR vesicles ( b ). ( a ) Fura 2- AM loaded myocytes were incubated with 8 μ M PTP 1B inhibitor, 300 n M SHP1/2 PTPase inhibitor or 11 μ M sodium stibogluconate for 10 min before perfusion with cADPR. Columns with vertical bars represent a quantitative summary of the maximum [Ca 2+ ] i increase after cADPR addition from five experiments. * P
    Figure Legend Snippet: Effects of a PTP1B inhibitor, an SHP1/2 inhibitor and stibogluconate on cADPR-induced increase in resting [Ca 2+ ] i in isolated rabbit ventricular myocytes ( a ) and isolated SR vesicles ( b ). ( a ) Fura 2- AM loaded myocytes were incubated with 8 μ M PTP 1B inhibitor, 300 n M SHP1/2 PTPase inhibitor or 11 μ M sodium stibogluconate for 10 min before perfusion with cADPR. Columns with vertical bars represent a quantitative summary of the maximum [Ca 2+ ] i increase after cADPR addition from five experiments. * P

    Techniques Used: Isolation, Incubation

    8) Product Images from "Inhibition of Src homology 2 domain‐containing phosphatase 1 increases insulin sensitivity in high‐fat diet‐induced insulin‐resistant mice"

    Article Title: Inhibition of Src homology 2 domain‐containing phosphatase 1 increases insulin sensitivity in high‐fat diet‐induced insulin‐resistant mice

    Journal: FEBS Open Bio

    doi: 10.1002/2211-5463.12000

    PTP inhibition resulted in enhanced glucose uptake accompanied by increased insulin receptor phosphorylation. (A‐B) Differentiated C2C12 cells were treated with sodium stibogluconate (A), BMOV (B) and transfected with SHP ‐1 si RNA (C) followed by measurement of insulin‐induced glucose uptake. Expression of mRNA was analysed to confirm efficient SHP ‐1 downregulation and to rule out compensatory regulation of the insulin receptor and other PTP s (D). (* P
    Figure Legend Snippet: PTP inhibition resulted in enhanced glucose uptake accompanied by increased insulin receptor phosphorylation. (A‐B) Differentiated C2C12 cells were treated with sodium stibogluconate (A), BMOV (B) and transfected with SHP ‐1 si RNA (C) followed by measurement of insulin‐induced glucose uptake. Expression of mRNA was analysed to confirm efficient SHP ‐1 downregulation and to rule out compensatory regulation of the insulin receptor and other PTP s (D). (* P

    Techniques Used: Inhibition, Transfection, Expressing

    SHP ‐1 inhibition with sodium stibogluconate increased insulin receptor phosphorylation. AML 12 cells were treated with or without sodium stibogluconate followed by insulin stimulation [3 n m ] for immunoblotting. Site‐specific phosphorylation levels of the insulin receptor and insulin signalling downstream kinases Akt and Erk were analysed. Shown is one representative immunoblot of n = 3 independent experiments.
    Figure Legend Snippet: SHP ‐1 inhibition with sodium stibogluconate increased insulin receptor phosphorylation. AML 12 cells were treated with or without sodium stibogluconate followed by insulin stimulation [3 n m ] for immunoblotting. Site‐specific phosphorylation levels of the insulin receptor and insulin signalling downstream kinases Akt and Erk were analysed. Shown is one representative immunoblot of n = 3 independent experiments.

    Techniques Used: Inhibition

    PTP s are not differentially expressed after PTP inhibition in metabolic tissues. Measurements of PTP expression on mRNA level were performed in liver (A), skeletal muscle (B) and adipose tissue (C) of BMOV and sodium stibogluconate treated mice compared to HFD mice.
    Figure Legend Snippet: PTP s are not differentially expressed after PTP inhibition in metabolic tissues. Measurements of PTP expression on mRNA level were performed in liver (A), skeletal muscle (B) and adipose tissue (C) of BMOV and sodium stibogluconate treated mice compared to HFD mice.

    Techniques Used: Inhibition, Expressing, Mouse Assay

    Related Articles

    High Performance Liquid Chromatography:

    Article Title: FAD roles in glucose catalytic oxidation studied by multiphase flow of extractive electrospray ionization (MF-EESI) mass spectrometry roles in glucose catalytic oxidation studied by multiphase flow of extractive electrospray ionization (MF-EESI) mass spectrometry †Electronic supplementary information (ESI) available
    Article Snippet: .. HPLC grade methanol was purchased from Fisher Chemical (USA) while gluconic acid, glucose oxidase, and glucose were obtained from Sigma-Aldrich (USA). .. Phosphate buffered saline (PBS) (0.01 M, pH = 7.2–7.4) was purchased from Solarbio (Beijing Solarbio Science & Technology Co., Ltd.).

    Article Title: Simultaneous untargeted and targeted metabolomics profiling of underivatized primary metabolites in sulfur-deficient barley by ultra-high performance liquid chromatography-quadrupole/time-of-flight mass spectrometry
    Article Snippet: .. Chemicals and reagents Amino acids, and organic acids HPLC quality standards proline (Pro), isoleucine (Ile), leucine (Leu), asparagine (Asn), aspartic acid (Asp), glutamine (Gln), glutamic acid (Glu), lysine (Lys), methionine (Met), histidine (His), phenylalanine (Phe), arginine (Arg), tyrosine (Tyr), tryptophan (Trp), 5 amino acid derivatives: O-acetyl-serine, thiamine, glutathione reduced (GSH), S-adenosyl-methionine (SAM), glutathione oxidized (GSSG), fumaric acid, succinic acid, malic acid, phospho(enol)pyruvic acid, cis-aconitic acid, shikimic acid, citric acid, isocitric acid, gluconic acid, 2 phosphorylated sugars: d -glucose 6-phosphate, trehalose 6-Phosphate, 4 secondary metabolites: gallic acid, azelaic acid, kaempferol, chlorogenic acid, and two internal standards: Lactitol and Taurine, were purchased from Sigma-Aldrich (Saint Quentin, France). .. Ultra-pure water was prepared by a Milli-Q Advantage A10 system (Darmstadt, Germany), Acetonitrile (ACN) and Methanol (MeOH) Optima LC–MS grade were purchased from Fisher (Leicester, UK), Formic Acid (FA) LC–MS grade and perchloric acid (PCA) were purchased from Merck (Darmstadt, Germany).

    Article Title: Production and effect of aldonic acids during enzymatic hydrolysis of lignocellulose at high dry matter content
    Article Snippet: .. Analysis of carbohydrates and oxidized products The quantification of D-glucose, D-cellobiose, gluconic acid (Sigma Aldrich, USA) and cellobionic acid (synthesized in this work), was done on two different HPLC instruments: i) UltiMate 3000 HPLC (Dionex, Germering, Germany) equipped with refractive index detector (Shodex, Japan) and UV detector at 200 nm (Dionex). .. The separation was performed in a Phenomenex Rezex ROA column at 80°C with 5 mM H2 SO4 as eluent at a flow rate of 0.6 ml/min.

    Synthesized:

    Article Title: Production and effect of aldonic acids during enzymatic hydrolysis of lignocellulose at high dry matter content
    Article Snippet: .. Analysis of carbohydrates and oxidized products The quantification of D-glucose, D-cellobiose, gluconic acid (Sigma Aldrich, USA) and cellobionic acid (synthesized in this work), was done on two different HPLC instruments: i) UltiMate 3000 HPLC (Dionex, Germering, Germany) equipped with refractive index detector (Shodex, Japan) and UV detector at 200 nm (Dionex). .. The separation was performed in a Phenomenex Rezex ROA column at 80°C with 5 mM H2 SO4 as eluent at a flow rate of 0.6 ml/min.

    Growth Assay:

    Article Title: Cellobionic acid utilization: from Neurospora crassa to Saccharomyces cerevisiae
    Article Snippet: .. N. crassa growth assay Conidia were inoculated at a concentration equal to 106 conidia per milliliter in 3 mL Vogel’s salts [ ] with 1 % wt/vol Avicel PH 101 (Sigma), glucose (Sigma), cellobiose (Sigma), gluconic acid (Sigma), cellobionic acid prepared as described above, or with no carbon, in a 24-well deep-well plate. .. The plate was sealed with Corning™ breathable sealing tape and incubated at 25 °C in constant light and shaking (200 rpm).

    Concentration Assay:

    Article Title: Cellobionic acid utilization: from Neurospora crassa to Saccharomyces cerevisiae
    Article Snippet: .. N. crassa growth assay Conidia were inoculated at a concentration equal to 106 conidia per milliliter in 3 mL Vogel’s salts [ ] with 1 % wt/vol Avicel PH 101 (Sigma), glucose (Sigma), cellobiose (Sigma), gluconic acid (Sigma), cellobionic acid prepared as described above, or with no carbon, in a 24-well deep-well plate. .. The plate was sealed with Corning™ breathable sealing tape and incubated at 25 °C in constant light and shaking (200 rpm).

    Expressing:

    Article Title: Two-electrode Voltage-clamp Recordings in Xenopus laevis Oocytes: Reconstitution of Abscisic Acid Activation of SLAC1 Anion Channel via PYL9 ABA Receptor
    Article Snippet: .. Borosilicate glass capillaries (World Precision Instruments, catalog number: 1B100F-4) Parafilm (Sigma-Aldrich, catalog number: P7793-1EA) Xenopus laevis oocytes (Ecocyte Bioscience, catalog number: 0-100-2) Vector: pNB1 oocyte expression vector harboring the cDNA of interest using the USER method ( ). or other oocytes expression vector like mMESSAGE mMACHINE® T7 Kit (Thermo Fisher Scientific, Ambion™, catalog number: AM1344) Collagenase D (Roche Diagnostics, catalog number: 11088882001) Mineral oil (Sigma-Aldrich, catalog number: M5904) MES hydrate (Sigma-Aldrich, catalog number: M2933) Tris-base (Thermo Fisher Scientific, Fisher Scientific, catalog number: BP152-5) Calcium chloride (CaCl2 ) (Sigma-Aldrich, catalog number: C5670) Magnesium chloride (MgCl2 ) (Sigma-Aldrich, catalog number: M8266) Sodium chloride (NaCl) (Thermo Fisher Scientific, Fisher Scientific, catalog number: S271-10) Potassium chloride (KCl) (Sigma-Aldrich, catalog number: P9333) Na-gluconate (Sigma-Aldrich, catalog number: S2054) D-sorbitol (Sigma-Aldrich, catalog number: S1876) Gentamicin solution (Sigma-Aldrich, catalog number: G1272) ND96 buffer (see Recipes) Recording buffer (see Recipes) .. Two-electrode voltage clamp amplifier ( e.g., Warner Instrument, model: Oocyte Clamp OC-725C) Digidata 1440A low-noise data acquisition system (Molecular Devices, model: Digidata 1440A) P-87 flaming/brown microelectrode micropipette puller (Sutter Instrument, model: P-87) Osmometer ( e.g., Wescor, model: Vapor Pressure Osmometer 5500) Microdispenser (Drummond Scientific, catalog number: 3-000-510) Custom glass tubing (Drummond Scientific, catalog number: 3-000-210-G8)

    Plasmid Preparation:

    Article Title: Two-electrode Voltage-clamp Recordings in Xenopus laevis Oocytes: Reconstitution of Abscisic Acid Activation of SLAC1 Anion Channel via PYL9 ABA Receptor
    Article Snippet: .. Borosilicate glass capillaries (World Precision Instruments, catalog number: 1B100F-4) Parafilm (Sigma-Aldrich, catalog number: P7793-1EA) Xenopus laevis oocytes (Ecocyte Bioscience, catalog number: 0-100-2) Vector: pNB1 oocyte expression vector harboring the cDNA of interest using the USER method ( ). or other oocytes expression vector like mMESSAGE mMACHINE® T7 Kit (Thermo Fisher Scientific, Ambion™, catalog number: AM1344) Collagenase D (Roche Diagnostics, catalog number: 11088882001) Mineral oil (Sigma-Aldrich, catalog number: M5904) MES hydrate (Sigma-Aldrich, catalog number: M2933) Tris-base (Thermo Fisher Scientific, Fisher Scientific, catalog number: BP152-5) Calcium chloride (CaCl2 ) (Sigma-Aldrich, catalog number: C5670) Magnesium chloride (MgCl2 ) (Sigma-Aldrich, catalog number: M8266) Sodium chloride (NaCl) (Thermo Fisher Scientific, Fisher Scientific, catalog number: S271-10) Potassium chloride (KCl) (Sigma-Aldrich, catalog number: P9333) Na-gluconate (Sigma-Aldrich, catalog number: S2054) D-sorbitol (Sigma-Aldrich, catalog number: S1876) Gentamicin solution (Sigma-Aldrich, catalog number: G1272) ND96 buffer (see Recipes) Recording buffer (see Recipes) .. Two-electrode voltage clamp amplifier ( e.g., Warner Instrument, model: Oocyte Clamp OC-725C) Digidata 1440A low-noise data acquisition system (Molecular Devices, model: Digidata 1440A) P-87 flaming/brown microelectrode micropipette puller (Sutter Instrument, model: P-87) Osmometer ( e.g., Wescor, model: Vapor Pressure Osmometer 5500) Microdispenser (Drummond Scientific, catalog number: 3-000-510) Custom glass tubing (Drummond Scientific, catalog number: 3-000-210-G8)

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    Millipore myostatin
    Chronic systemic administration of formoterol alters the expression of genes associated with skeletal muscle hypertrophy and myogenesis at multiple timepoints . Quantitative RT-PCR was used to assay the expression of A . Stat3 , B . Idb1 , C . Smad1 , D . Acvr2b , E . Smad3 , and F . <t>Myostatin</t> mRNAs in tibialis anterior over chronic timepoints. Muscles were removed at 1, 7 and 28 days following daily intraperitoneal injection of formoterol or saline vehicle (NT = no treatment). Results were normalized against 36B4 at each timepoint. Data are expressed as mean ± SEM (n = 5). Statistical significance was assessed using a one-way ANOVA with Bonferroni's post-test where p
    Myostatin, supplied by Millipore, used in various techniques. Bioz Stars score: 86/100, based on 15 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore myostatin protein
    <t>Myostatin</t> protein expression is increased in Tcap KO mouse muscles. Immunoblots were performed on muscle lysates from WT and Tcap KO gastrocnemius muscles probed with an anti-myostatin antibody. ( A ) To evaluate the myostatin antibody, recombinant purified human myostatin protein was subjected to both non-reducing (−) and reducing (+) conditions as indicated. One hundred and twenty-five, 250 and 500 ng purified myostatin protein were loaded in each condition. Bands at ∼26 and ∼13 kDa were clearly seen, indicating the sensitivity of the antibody to detect intact and cleaved C-terminal dimer myostatin proteins, respectively. ( B ) Both the 45-kDa precursor and 26-kDa processed myostatin bands were observed, but only in Tcap KO muscle lysates and not in WT muscles. ( C ) To assess the sensitivity of myostatin antibody in skeletal muscle tissue, female rats ( n = 3) were suspended by their tails (HLU) for four weeks, SOL muscles were subsequently removed and muscle lysates were probed with anti-myostatin antibody. Intensity of myostatin bands (∼26 kDa) increased relative to GAPDH bands (∼36 kDa) during HLU compared with non-HLU controls. Densitometry analysis ( D ) of MSTN bands demonstrated significantly greater intensity ( P
    Myostatin Protein, supplied by Millipore, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Millipore anti myostatin antibody
    <t>Myostatin</t> protein expression is increased in Tcap KO mouse muscles. Immunoblots were performed on muscle lysates from WT and Tcap KO gastrocnemius muscles probed with an anti-myostatin antibody. ( A ) To evaluate the myostatin antibody, recombinant purified human myostatin protein was subjected to both non-reducing (−) and reducing (+) conditions as indicated. One hundred and twenty-five, 250 and 500 ng purified myostatin protein were loaded in each condition. Bands at ∼26 and ∼13 kDa were clearly seen, indicating the sensitivity of the antibody to detect intact and cleaved C-terminal dimer myostatin proteins, respectively. ( B ) Both the 45-kDa precursor and 26-kDa processed myostatin bands were observed, but only in Tcap KO muscle lysates and not in WT muscles. ( C ) To assess the sensitivity of myostatin antibody in skeletal muscle tissue, female rats ( n = 3) were suspended by their tails (HLU) for four weeks, SOL muscles were subsequently removed and muscle lysates were probed with anti-myostatin antibody. Intensity of myostatin bands (∼26 kDa) increased relative to GAPDH bands (∼36 kDa) during HLU compared with non-HLU controls. Densitometry analysis ( D ) of MSTN bands demonstrated significantly greater intensity ( P
    Anti Myostatin Antibody, supplied by Millipore, 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/result/anti myostatin antibody/product/Millipore
    Average 90 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti myostatin antibody - by Bioz Stars, 2020-08
    90/100 stars
      Buy from Supplier

    Image Search Results


    Chronic systemic administration of formoterol alters the expression of genes associated with skeletal muscle hypertrophy and myogenesis at multiple timepoints . Quantitative RT-PCR was used to assay the expression of A . Stat3 , B . Idb1 , C . Smad1 , D . Acvr2b , E . Smad3 , and F . Myostatin mRNAs in tibialis anterior over chronic timepoints. Muscles were removed at 1, 7 and 28 days following daily intraperitoneal injection of formoterol or saline vehicle (NT = no treatment). Results were normalized against 36B4 at each timepoint. Data are expressed as mean ± SEM (n = 5). Statistical significance was assessed using a one-way ANOVA with Bonferroni's post-test where p

    Journal: BMC Genomics

    Article Title: Expression profiling of skeletal muscle following acute and chronic ?2-adrenergic stimulation: implications for hypertrophy, metabolism and circadian rhythm

    doi: 10.1186/1471-2164-10-448

    Figure Lengend Snippet: Chronic systemic administration of formoterol alters the expression of genes associated with skeletal muscle hypertrophy and myogenesis at multiple timepoints . Quantitative RT-PCR was used to assay the expression of A . Stat3 , B . Idb1 , C . Smad1 , D . Acvr2b , E . Smad3 , and F . Myostatin mRNAs in tibialis anterior over chronic timepoints. Muscles were removed at 1, 7 and 28 days following daily intraperitoneal injection of formoterol or saline vehicle (NT = no treatment). Results were normalized against 36B4 at each timepoint. Data are expressed as mean ± SEM (n = 5). Statistical significance was assessed using a one-way ANOVA with Bonferroni's post-test where p

    Article Snippet: Secondary anti-rabbit-horseradish peroxidase conjugate (Pierce Biotechnology) in blocking buffer was used at 1:10000 for Gapdh , Smad3 , and phospho-Smad3 for 1 h. Secondary anti-goat-horseradish peroxidase conjugate (Pierce Biotechnology) in blocking buffer was used at 1:10000 for Myostatin for 1 h. Horseradish peroxidase localization was detected with Immobilon Western Chemiluminescent HRP Substrate (Millipore) according to the manufacturer's instructions and visualized by X-ray film.

    Techniques: Expressing, Quantitative RT-PCR, Injection

    Acute systemic administration of formoterol alters the expression of genes associated with muscle growth and differentiation at multiple timepoints . Quantitative RT-PCR was used to assay the expression of A . Stat3 , B . Idb1 , C . Smad1 , D . Acvr2b , E . Smad3 , and F . Myostatin mRNAs in tibialis anterior over acute timepoints. Muscles were removed at 1, 4, 8 and 24 hours following a single intraperitoneal injection of formoterol or saline vehicle (NT = no treatment). Results were normalized against 36B4 at each timepoint. Statistical significance was assessed using a one-way ANOVA with Bonferroni's post-test where p

    Journal: BMC Genomics

    Article Title: Expression profiling of skeletal muscle following acute and chronic ?2-adrenergic stimulation: implications for hypertrophy, metabolism and circadian rhythm

    doi: 10.1186/1471-2164-10-448

    Figure Lengend Snippet: Acute systemic administration of formoterol alters the expression of genes associated with muscle growth and differentiation at multiple timepoints . Quantitative RT-PCR was used to assay the expression of A . Stat3 , B . Idb1 , C . Smad1 , D . Acvr2b , E . Smad3 , and F . Myostatin mRNAs in tibialis anterior over acute timepoints. Muscles were removed at 1, 4, 8 and 24 hours following a single intraperitoneal injection of formoterol or saline vehicle (NT = no treatment). Results were normalized against 36B4 at each timepoint. Statistical significance was assessed using a one-way ANOVA with Bonferroni's post-test where p

    Article Snippet: Secondary anti-rabbit-horseradish peroxidase conjugate (Pierce Biotechnology) in blocking buffer was used at 1:10000 for Gapdh , Smad3 , and phospho-Smad3 for 1 h. Secondary anti-goat-horseradish peroxidase conjugate (Pierce Biotechnology) in blocking buffer was used at 1:10000 for Myostatin for 1 h. Horseradish peroxidase localization was detected with Immobilon Western Chemiluminescent HRP Substrate (Millipore) according to the manufacturer's instructions and visualized by X-ray film.

    Techniques: Expressing, Quantitative RT-PCR, Injection

    Myostatin to IGF-1 Ratio. The relationship of myostatin/IGF-1 (left axis) and ventricular dysfunction (right axis) has been plotted for Adult Normal (n = 5), pediatric right ventricular outflow tract (RVOT) (n = 3), pediatric orthotopic heart transplant (OHT) (n = 7 paired LV and RV), and pediatric biventricular assist device (BiVAD) myocardial tissue samples (n = 3 paired LV and RV). A strong association between increased myostatin/IGF-1 ratios and worsening ventricular dysfunction exists: Adult Normal samples had low myostatin/IGF-1 levels, while BiVAD samples displayed high myostatin/IGF-1 levels.

    Journal: PLoS ONE

    Article Title: Myostatin Is Elevated in Congenital Heart Disease and After Mechanical Unloading

    doi: 10.1371/journal.pone.0023818

    Figure Lengend Snippet: Myostatin to IGF-1 Ratio. The relationship of myostatin/IGF-1 (left axis) and ventricular dysfunction (right axis) has been plotted for Adult Normal (n = 5), pediatric right ventricular outflow tract (RVOT) (n = 3), pediatric orthotopic heart transplant (OHT) (n = 7 paired LV and RV), and pediatric biventricular assist device (BiVAD) myocardial tissue samples (n = 3 paired LV and RV). A strong association between increased myostatin/IGF-1 ratios and worsening ventricular dysfunction exists: Adult Normal samples had low myostatin/IGF-1 levels, while BiVAD samples displayed high myostatin/IGF-1 levels.

    Article Snippet: The following antibodies were used: myostatin (1∶500, Millipore, Temecula, CA), IGF-1 (1∶500, R & D Systems, Minneapolis, MN), MEF-2 (1∶1000, Santa Cruz Biotechnology, Santa Cruz, CA), and GAPDH (1∶4000, Santa Cruz Biotechnology, Santa Cruz, CA).

    Techniques:

    MEF-2 Expression. A.) Representative Western blot for MEF-2, a transcriptional factor for myostatin, in Adult Normal (n = 5), pediatric right ventricular outflow tract (RVOT) (n = 3), pediatric orthotopic heart transplant (OHT) (n = 7 paired LV and RV), and pediatric biventricular assist device (BiVAD) myocardial tissue samples (n = 3 paired LV and RV). B.) MEF-2 was significantly increased in LV-OHT compared to Adult Normal control (# p

    Journal: PLoS ONE

    Article Title: Myostatin Is Elevated in Congenital Heart Disease and After Mechanical Unloading

    doi: 10.1371/journal.pone.0023818

    Figure Lengend Snippet: MEF-2 Expression. A.) Representative Western blot for MEF-2, a transcriptional factor for myostatin, in Adult Normal (n = 5), pediatric right ventricular outflow tract (RVOT) (n = 3), pediatric orthotopic heart transplant (OHT) (n = 7 paired LV and RV), and pediatric biventricular assist device (BiVAD) myocardial tissue samples (n = 3 paired LV and RV). B.) MEF-2 was significantly increased in LV-OHT compared to Adult Normal control (# p

    Article Snippet: The following antibodies were used: myostatin (1∶500, Millipore, Temecula, CA), IGF-1 (1∶500, R & D Systems, Minneapolis, MN), MEF-2 (1∶1000, Santa Cruz Biotechnology, Santa Cruz, CA), and GAPDH (1∶4000, Santa Cruz Biotechnology, Santa Cruz, CA).

    Techniques: Expressing, Western Blot

    Myostatin Expression. A.) Representative Western blot for the myostatin peptide (∼50 kDa) in Adult Normal (n = 5), pediatric right ventricular outflow tract (RVOT) (n = 3), pediatric orthotopic heart transplant (OHT) (n = 7 paired LV and RV), and pediatric biventricular assist device (BiVAD) myocardial tissue samples (n = 3 paired LV and RV). B.) No significant differences were found between Adult Normal and RVOT, while LV-OHT were significantly higher than RV-OHT samples ( p

    Journal: PLoS ONE

    Article Title: Myostatin Is Elevated in Congenital Heart Disease and After Mechanical Unloading

    doi: 10.1371/journal.pone.0023818

    Figure Lengend Snippet: Myostatin Expression. A.) Representative Western blot for the myostatin peptide (∼50 kDa) in Adult Normal (n = 5), pediatric right ventricular outflow tract (RVOT) (n = 3), pediatric orthotopic heart transplant (OHT) (n = 7 paired LV and RV), and pediatric biventricular assist device (BiVAD) myocardial tissue samples (n = 3 paired LV and RV). B.) No significant differences were found between Adult Normal and RVOT, while LV-OHT were significantly higher than RV-OHT samples ( p

    Article Snippet: The following antibodies were used: myostatin (1∶500, Millipore, Temecula, CA), IGF-1 (1∶500, R & D Systems, Minneapolis, MN), MEF-2 (1∶1000, Santa Cruz Biotechnology, Santa Cruz, CA), and GAPDH (1∶4000, Santa Cruz Biotechnology, Santa Cruz, CA).

    Techniques: Expressing, Western Blot

    Myostatin protein expression is increased in Tcap KO mouse muscles. Immunoblots were performed on muscle lysates from WT and Tcap KO gastrocnemius muscles probed with an anti-myostatin antibody. ( A ) To evaluate the myostatin antibody, recombinant purified human myostatin protein was subjected to both non-reducing (−) and reducing (+) conditions as indicated. One hundred and twenty-five, 250 and 500 ng purified myostatin protein were loaded in each condition. Bands at ∼26 and ∼13 kDa were clearly seen, indicating the sensitivity of the antibody to detect intact and cleaved C-terminal dimer myostatin proteins, respectively. ( B ) Both the 45-kDa precursor and 26-kDa processed myostatin bands were observed, but only in Tcap KO muscle lysates and not in WT muscles. ( C ) To assess the sensitivity of myostatin antibody in skeletal muscle tissue, female rats ( n = 3) were suspended by their tails (HLU) for four weeks, SOL muscles were subsequently removed and muscle lysates were probed with anti-myostatin antibody. Intensity of myostatin bands (∼26 kDa) increased relative to GAPDH bands (∼36 kDa) during HLU compared with non-HLU controls. Densitometry analysis ( D ) of MSTN bands demonstrated significantly greater intensity ( P

    Journal: Human Molecular Genetics

    Article Title: Functional muscle analysis of the Tcap knockout mouse

    doi: 10.1093/hmg/ddq105

    Figure Lengend Snippet: Myostatin protein expression is increased in Tcap KO mouse muscles. Immunoblots were performed on muscle lysates from WT and Tcap KO gastrocnemius muscles probed with an anti-myostatin antibody. ( A ) To evaluate the myostatin antibody, recombinant purified human myostatin protein was subjected to both non-reducing (−) and reducing (+) conditions as indicated. One hundred and twenty-five, 250 and 500 ng purified myostatin protein were loaded in each condition. Bands at ∼26 and ∼13 kDa were clearly seen, indicating the sensitivity of the antibody to detect intact and cleaved C-terminal dimer myostatin proteins, respectively. ( B ) Both the 45-kDa precursor and 26-kDa processed myostatin bands were observed, but only in Tcap KO muscle lysates and not in WT muscles. ( C ) To assess the sensitivity of myostatin antibody in skeletal muscle tissue, female rats ( n = 3) were suspended by their tails (HLU) for four weeks, SOL muscles were subsequently removed and muscle lysates were probed with anti-myostatin antibody. Intensity of myostatin bands (∼26 kDa) increased relative to GAPDH bands (∼36 kDa) during HLU compared with non-HLU controls. Densitometry analysis ( D ) of MSTN bands demonstrated significantly greater intensity ( P

    Article Snippet: Anti-myostatin antibody and purified myostatin protein were obtained from Millipore Corporation (Bedford, MA, USA; Cat# ab3239) and ProSpec (Rehovot, Israel; Cat# CYT-418), respectively.

    Techniques: Expressing, Western Blot, Recombinant, Purification

    Tcap and myostatin associate in mouse skeletal muscle tissue. HLU was used to increase myostatin expression in skeletal muscle. Adult female mice ( n = 2) were suspended by their tails (HLU) for 2 weeks. ( A ) Three independent thin sections of SOL muscles were stained with primary antibodies directed against either Tcap or myostatin and conjugated to red or green fluorescent secondary antibodies, respectively, as indicated. In merged images (second column from the right) the relative amount of color overlap was determined with computer software. The mean (±SD) percent overlap between Tcap and myostatin was 20.5 ± 0.9%, suggesting a biological association between the two proteins. The far-right column shows detail of the area indicated by the box. ( B ) Representative line-scan analysis of fluorescent intensity. Points along the line drawn on the image connecting two points, labeled ‘a’ and ‘b’, were sampled to generate an intensity profile of two fluorescent colors, red (Tcap) and green (myostatin). Peak intensity for both Tcap and myostatin line scans correlate with the regular repeating z-disc striations observed in longitudinal thin sections of muscle.

    Journal: Human Molecular Genetics

    Article Title: Functional muscle analysis of the Tcap knockout mouse

    doi: 10.1093/hmg/ddq105

    Figure Lengend Snippet: Tcap and myostatin associate in mouse skeletal muscle tissue. HLU was used to increase myostatin expression in skeletal muscle. Adult female mice ( n = 2) were suspended by their tails (HLU) for 2 weeks. ( A ) Three independent thin sections of SOL muscles were stained with primary antibodies directed against either Tcap or myostatin and conjugated to red or green fluorescent secondary antibodies, respectively, as indicated. In merged images (second column from the right) the relative amount of color overlap was determined with computer software. The mean (±SD) percent overlap between Tcap and myostatin was 20.5 ± 0.9%, suggesting a biological association between the two proteins. The far-right column shows detail of the area indicated by the box. ( B ) Representative line-scan analysis of fluorescent intensity. Points along the line drawn on the image connecting two points, labeled ‘a’ and ‘b’, were sampled to generate an intensity profile of two fluorescent colors, red (Tcap) and green (myostatin). Peak intensity for both Tcap and myostatin line scans correlate with the regular repeating z-disc striations observed in longitudinal thin sections of muscle.

    Article Snippet: Anti-myostatin antibody and purified myostatin protein were obtained from Millipore Corporation (Bedford, MA, USA; Cat# ab3239) and ProSpec (Rehovot, Israel; Cat# CYT-418), respectively.

    Techniques: Expressing, Mouse Assay, Staining, Software, Labeling

    Myostatin protein expression is increased in Tcap KO mouse muscles. Immunoblots were performed on muscle lysates from WT and Tcap KO gastrocnemius muscles probed with an anti-myostatin antibody. ( A ) To evaluate the myostatin antibody, recombinant purified human myostatin protein was subjected to both non-reducing (−) and reducing (+) conditions as indicated. One hundred and twenty-five, 250 and 500 ng purified myostatin protein were loaded in each condition. Bands at ∼26 and ∼13 kDa were clearly seen, indicating the sensitivity of the antibody to detect intact and cleaved C-terminal dimer myostatin proteins, respectively. ( B ) Both the 45-kDa precursor and 26-kDa processed myostatin bands were observed, but only in Tcap KO muscle lysates and not in WT muscles. ( C ) To assess the sensitivity of myostatin antibody in skeletal muscle tissue, female rats ( n = 3) were suspended by their tails (HLU) for four weeks, SOL muscles were subsequently removed and muscle lysates were probed with anti-myostatin antibody. Intensity of myostatin bands (∼26 kDa) increased relative to GAPDH bands (∼36 kDa) during HLU compared with non-HLU controls. Densitometry analysis ( D ) of MSTN bands demonstrated significantly greater intensity ( P

    Journal: Human Molecular Genetics

    Article Title: Functional muscle analysis of the Tcap knockout mouse

    doi: 10.1093/hmg/ddq105

    Figure Lengend Snippet: Myostatin protein expression is increased in Tcap KO mouse muscles. Immunoblots were performed on muscle lysates from WT and Tcap KO gastrocnemius muscles probed with an anti-myostatin antibody. ( A ) To evaluate the myostatin antibody, recombinant purified human myostatin protein was subjected to both non-reducing (−) and reducing (+) conditions as indicated. One hundred and twenty-five, 250 and 500 ng purified myostatin protein were loaded in each condition. Bands at ∼26 and ∼13 kDa were clearly seen, indicating the sensitivity of the antibody to detect intact and cleaved C-terminal dimer myostatin proteins, respectively. ( B ) Both the 45-kDa precursor and 26-kDa processed myostatin bands were observed, but only in Tcap KO muscle lysates and not in WT muscles. ( C ) To assess the sensitivity of myostatin antibody in skeletal muscle tissue, female rats ( n = 3) were suspended by their tails (HLU) for four weeks, SOL muscles were subsequently removed and muscle lysates were probed with anti-myostatin antibody. Intensity of myostatin bands (∼26 kDa) increased relative to GAPDH bands (∼36 kDa) during HLU compared with non-HLU controls. Densitometry analysis ( D ) of MSTN bands demonstrated significantly greater intensity ( P

    Article Snippet: Anti-myostatin antibody and purified myostatin protein were obtained from Millipore Corporation (Bedford, MA, USA; Cat# ab3239) and ProSpec (Rehovot, Israel; Cat# CYT-418), respectively.

    Techniques: Expressing, Western Blot, Recombinant, Purification

    Tcap and myostatin associate in mouse skeletal muscle tissue. HLU was used to increase myostatin expression in skeletal muscle. Adult female mice ( n = 2) were suspended by their tails (HLU) for 2 weeks. ( A ) Three independent thin sections of SOL muscles were stained with primary antibodies directed against either Tcap or myostatin and conjugated to red or green fluorescent secondary antibodies, respectively, as indicated. In merged images (second column from the right) the relative amount of color overlap was determined with computer software. The mean (±SD) percent overlap between Tcap and myostatin was 20.5 ± 0.9%, suggesting a biological association between the two proteins. The far-right column shows detail of the area indicated by the box. ( B ) Representative line-scan analysis of fluorescent intensity. Points along the line drawn on the image connecting two points, labeled ‘a’ and ‘b’, were sampled to generate an intensity profile of two fluorescent colors, red (Tcap) and green (myostatin). Peak intensity for both Tcap and myostatin line scans correlate with the regular repeating z-disc striations observed in longitudinal thin sections of muscle.

    Journal: Human Molecular Genetics

    Article Title: Functional muscle analysis of the Tcap knockout mouse

    doi: 10.1093/hmg/ddq105

    Figure Lengend Snippet: Tcap and myostatin associate in mouse skeletal muscle tissue. HLU was used to increase myostatin expression in skeletal muscle. Adult female mice ( n = 2) were suspended by their tails (HLU) for 2 weeks. ( A ) Three independent thin sections of SOL muscles were stained with primary antibodies directed against either Tcap or myostatin and conjugated to red or green fluorescent secondary antibodies, respectively, as indicated. In merged images (second column from the right) the relative amount of color overlap was determined with computer software. The mean (±SD) percent overlap between Tcap and myostatin was 20.5 ± 0.9%, suggesting a biological association between the two proteins. The far-right column shows detail of the area indicated by the box. ( B ) Representative line-scan analysis of fluorescent intensity. Points along the line drawn on the image connecting two points, labeled ‘a’ and ‘b’, were sampled to generate an intensity profile of two fluorescent colors, red (Tcap) and green (myostatin). Peak intensity for both Tcap and myostatin line scans correlate with the regular repeating z-disc striations observed in longitudinal thin sections of muscle.

    Article Snippet: Anti-myostatin antibody and purified myostatin protein were obtained from Millipore Corporation (Bedford, MA, USA; Cat# ab3239) and ProSpec (Rehovot, Israel; Cat# CYT-418), respectively.

    Techniques: Expressing, Mouse Assay, Staining, Software, Labeling