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lambda phosphatase 400 units/section  (BioAcademia)

 
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    BioAcademia lambda phosphatase 400 units/section
    Lambda Phosphatase 400 Units/Section, supplied by BioAcademia, 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/lambda+phosphatase/lambda+phosphatase+400+units+section/pm28002815-75-16-20
    Average 90 stars, based on 1 article reviews
    lambda phosphatase 400 units/section - by Bioz Stars, 2026-11
    90/100 stars

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    Staining:

    Article Title: Cortical Actin Alteration at the Matrix-Side Cytoplasm in Lung Adenocarcinoma Cells and Its Significance in Invasion.
    Article Snippet: .. In order to confirm the specificity of the anti-phosphorylated MLC2 antibody, the section was pretreated with lambda phosphatase (400 units/section, BioAcademia, Osaka, Japan) at 30 ° C for 60 min. Phosphorylated MLC was regarded as positive when more than a quarter of the matrix-side circumference of a spheroid was stained. .. For electron microscopy, A549 cells were fixed with 2.5% glutaraldehyde, routinely processed, and observed by a transmission electron microscope (H-7200, Hitachi, Tokyo, Japan).



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    (A) Representative confocal images of axon with growth cones stained for tyrosinated α-tubulin (Tyr, red), F-actin (phalloidin, magenta), and phosphorylated-VASH1 (P[S337]VASH1, gray). Scale bar, 10 µm. ( B ) Quantification of P[S337]VASH1 in growth cones of WT and Vash1 KO neurons. n/N: 67/5 (WT), 111/7 (KO) with n indicating the number of growth cones and N of E13 embryos. Data are expressed as mean ± SD and as fold change over WT. ( C ) Quantification of P[S337]VASH1 in growth cones without treatment or with CNP treatment. n/N: 61/4 (control), 48/3 (CNP) with n indicating the number of growth cones and N the number of E13 embryos. Data are expressed as mean ± SD and as fold change over control. Statistical significance was determined using Mann-Witney test. **** p < 0.0001, ns p > 0.05. ( D, E ) Detection by immunoblot of VASH1 protein and its phosphorylated form in cultured DRG neurons after immunoprecipitation using an anti-SVBP antibody. β-tubulin staining shows similar protein content in the immunoprecipitation inputs. ( D ) Both VASH1 protein and its phosphorylated form are detected in WT but not in Vash1 KO DRGs. Treatment with <t>Lambda</t> protein <t>phosphatase</t> results in the loss of P[S337]VASH1 band. ( E, F ) CNP induces phosphorylation of S337 of VASH1, which is reversed by DT-3, as shown by representative immunoblots from an experiment done with cultured DRG explants ( E ) and quantifications of the P[S337]VASH1/VASH1 ratios from 4 independent experiments ( F ). In F , triangles correspond to data from immunoprecipitation experiments done with cultured DRG dissociated neurons, and circle to immunoprecipitation experiments done with cultured DRG explants.
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    (A) Representative confocal images of axon with growth cones stained for tyrosinated α-tubulin (Tyr, red), F-actin (phalloidin, magenta), and phosphorylated-VASH1 (P[S337]VASH1, gray). Scale bar, 10 µm. ( B ) Quantification of P[S337]VASH1 in growth cones of WT and Vash1 KO neurons. n/N: 67/5 (WT), 111/7 (KO) with n indicating the number of growth cones and N of E13 embryos. Data are expressed as mean ± SD and as fold change over WT. ( C ) Quantification of P[S337]VASH1 in growth cones without treatment or with CNP treatment. n/N: 61/4 (control), 48/3 (CNP) with n indicating the number of growth cones and N the number of E13 embryos. Data are expressed as mean ± SD and as fold change over control. Statistical significance was determined using Mann-Witney test. **** p < 0.0001, ns p > 0.05. ( D, E ) Detection by immunoblot of VASH1 protein and its phosphorylated form in cultured DRG neurons after immunoprecipitation using an anti-SVBP antibody. β-tubulin staining shows similar protein content in the immunoprecipitation inputs. ( D ) Both VASH1 protein and its phosphorylated form are detected in WT but not in Vash1 KO DRGs. Treatment with <t>Lambda</t> protein <t>phosphatase</t> results in the loss of P[S337]VASH1 band. ( E, F ) CNP induces phosphorylation of S337 of VASH1, which is reversed by DT-3, as shown by representative immunoblots from an experiment done with cultured DRG explants ( E ) and quantifications of the P[S337]VASH1/VASH1 ratios from 4 independent experiments ( F ). In F , triangles correspond to data from immunoprecipitation experiments done with cultured DRG dissociated neurons, and circle to immunoprecipitation experiments done with cultured DRG explants.
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    (A) Representative confocal images of axon with growth cones stained for tyrosinated α-tubulin (Tyr, red), F-actin (phalloidin, magenta), and phosphorylated-VASH1 (P[S337]VASH1, gray). Scale bar, 10 µm. ( B ) Quantification of P[S337]VASH1 in growth cones of WT and Vash1 KO neurons. n/N: 67/5 (WT), 111/7 (KO) with n indicating the number of growth cones and N of E13 embryos. Data are expressed as mean ± SD and as fold change over WT. ( C ) Quantification of P[S337]VASH1 in growth cones without treatment or with CNP treatment. n/N: 61/4 (control), 48/3 (CNP) with n indicating the number of growth cones and N the number of E13 embryos. Data are expressed as mean ± SD and as fold change over control. Statistical significance was determined using Mann-Witney test. **** p < 0.0001, ns p > 0.05. ( D, E ) Detection by immunoblot of VASH1 protein and its phosphorylated form in cultured DRG neurons after immunoprecipitation using an anti-SVBP antibody. β-tubulin staining shows similar protein content in the immunoprecipitation inputs. ( D ) Both VASH1 protein and its phosphorylated form are detected in WT but not in Vash1 KO DRGs. Treatment with <t>Lambda</t> protein <t>phosphatase</t> results in the loss of P[S337]VASH1 band. ( E, F ) CNP induces phosphorylation of S337 of VASH1, which is reversed by DT-3, as shown by representative immunoblots from an experiment done with cultured DRG explants ( E ) and quantifications of the P[S337]VASH1/VASH1 ratios from 4 independent experiments ( F ). In F , triangles correspond to data from immunoprecipitation experiments done with cultured DRG dissociated neurons, and circle to immunoprecipitation experiments done with cultured DRG explants.
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    (A) Representative confocal images of axon with growth cones stained for tyrosinated α-tubulin (Tyr, red), F-actin (phalloidin, magenta), and phosphorylated-VASH1 (P[S337]VASH1, gray). Scale bar, 10 µm. ( B ) Quantification of P[S337]VASH1 in growth cones of WT and Vash1 KO neurons. n/N: 67/5 (WT), 111/7 (KO) with n indicating the number of growth cones and N of E13 embryos. Data are expressed as mean ± SD and as fold change over WT. ( C ) Quantification of P[S337]VASH1 in growth cones without treatment or with CNP treatment. n/N: 61/4 (control), 48/3 (CNP) with n indicating the number of growth cones and N the number of E13 embryos. Data are expressed as mean ± SD and as fold change over control. Statistical significance was determined using Mann-Witney test. **** p < 0.0001, ns p > 0.05. ( D, E ) Detection by immunoblot of VASH1 protein and its phosphorylated form in cultured DRG neurons after immunoprecipitation using an anti-SVBP antibody. β-tubulin staining shows similar protein content in the immunoprecipitation inputs. ( D ) Both VASH1 protein and its phosphorylated form are detected in WT but not in Vash1 KO DRGs. Treatment with <t>Lambda</t> protein <t>phosphatase</t> results in the loss of P[S337]VASH1 band. ( E, F ) CNP induces phosphorylation of S337 of VASH1, which is reversed by DT-3, as shown by representative immunoblots from an experiment done with cultured DRG explants ( E ) and quantifications of the P[S337]VASH1/VASH1 ratios from 4 independent experiments ( F ). In F , triangles correspond to data from immunoprecipitation experiments done with cultured DRG dissociated neurons, and circle to immunoprecipitation experiments done with cultured DRG explants.
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    (A) Representative confocal images of axon with growth cones stained for tyrosinated α-tubulin (Tyr, red), F-actin (phalloidin, magenta), and phosphorylated-VASH1 (P[S337]VASH1, gray). Scale bar, 10 µm. ( B ) Quantification of P[S337]VASH1 in growth cones of WT and Vash1 KO neurons. n/N: 67/5 (WT), 111/7 (KO) with n indicating the number of growth cones and N of E13 embryos. Data are expressed as mean ± SD and as fold change over WT. ( C ) Quantification of P[S337]VASH1 in growth cones without treatment or with CNP treatment. n/N: 61/4 (control), 48/3 (CNP) with n indicating the number of growth cones and N the number of E13 embryos. Data are expressed as mean ± SD and as fold change over control. Statistical significance was determined using Mann-Witney test. **** p < 0.0001, ns p > 0.05. ( D, E ) Detection by immunoblot of VASH1 protein and its phosphorylated form in cultured DRG neurons after immunoprecipitation using an anti-SVBP antibody. β-tubulin staining shows similar protein content in the immunoprecipitation inputs. ( D ) Both VASH1 protein and its phosphorylated form are detected in WT but not in Vash1 KO DRGs. Treatment with <t>Lambda</t> protein <t>phosphatase</t> results in the loss of P[S337]VASH1 band. ( E, F ) CNP induces phosphorylation of S337 of VASH1, which is reversed by DT-3, as shown by representative immunoblots from an experiment done with cultured DRG explants ( E ) and quantifications of the P[S337]VASH1/VASH1 ratios from 4 independent experiments ( F ). In F , triangles correspond to data from immunoprecipitation experiments done with cultured DRG dissociated neurons, and circle to immunoprecipitation experiments done with cultured DRG explants.
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    (A) Representative confocal images of axon with growth cones stained for tyrosinated α-tubulin (Tyr, red), F-actin (phalloidin, magenta), and phosphorylated-VASH1 (P[S337]VASH1, gray). Scale bar, 10 µm. ( B ) Quantification of P[S337]VASH1 in growth cones of WT and Vash1 KO neurons. n/N: 67/5 (WT), 111/7 (KO) with n indicating the number of growth cones and N of E13 embryos. Data are expressed as mean ± SD and as fold change over WT. ( C ) Quantification of P[S337]VASH1 in growth cones without treatment or with CNP treatment. n/N: 61/4 (control), 48/3 (CNP) with n indicating the number of growth cones and N the number of E13 embryos. Data are expressed as mean ± SD and as fold change over control. Statistical significance was determined using Mann-Witney test. **** p < 0.0001, ns p > 0.05. ( D, E ) Detection by immunoblot of VASH1 protein and its phosphorylated form in cultured DRG neurons after immunoprecipitation using an anti-SVBP antibody. β-tubulin staining shows similar protein content in the immunoprecipitation inputs. ( D ) Both VASH1 protein and its phosphorylated form are detected in WT but not in Vash1 KO DRGs. Treatment with <t>Lambda</t> protein <t>phosphatase</t> results in the loss of P[S337]VASH1 band. ( E, F ) CNP induces phosphorylation of S337 of VASH1, which is reversed by DT-3, as shown by representative immunoblots from an experiment done with cultured DRG explants ( E ) and quantifications of the P[S337]VASH1/VASH1 ratios from 4 independent experiments ( F ). In F , triangles correspond to data from immunoprecipitation experiments done with cultured DRG dissociated neurons, and circle to immunoprecipitation experiments done with cultured DRG explants.
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    (A) Representative confocal images of axon with growth cones stained for tyrosinated α-tubulin (Tyr, red), F-actin (phalloidin, magenta), and phosphorylated-VASH1 (P[S337]VASH1, gray). Scale bar, 10 µm. ( B ) Quantification of P[S337]VASH1 in growth cones of WT and Vash1 KO neurons. n/N: 67/5 (WT), 111/7 (KO) with n indicating the number of growth cones and N of E13 embryos. Data are expressed as mean ± SD and as fold change over WT. ( C ) Quantification of P[S337]VASH1 in growth cones without treatment or with CNP treatment. n/N: 61/4 (control), 48/3 (CNP) with n indicating the number of growth cones and N the number of E13 embryos. Data are expressed as mean ± SD and as fold change over control. Statistical significance was determined using Mann-Witney test. **** p < 0.0001, ns p > 0.05. ( D, E ) Detection by immunoblot of VASH1 protein and its phosphorylated form in cultured DRG neurons after immunoprecipitation using an anti-SVBP antibody. β-tubulin staining shows similar protein content in the immunoprecipitation inputs. ( D ) Both VASH1 protein and its phosphorylated form are detected in WT but not in Vash1 KO DRGs. Treatment with <t>Lambda</t> protein <t>phosphatase</t> results in the loss of P[S337]VASH1 band. ( E, F ) CNP induces phosphorylation of S337 of VASH1, which is reversed by DT-3, as shown by representative immunoblots from an experiment done with cultured DRG explants ( E ) and quantifications of the P[S337]VASH1/VASH1 ratios from 4 independent experiments ( F ). In F , triangles correspond to data from immunoprecipitation experiments done with cultured DRG dissociated neurons, and circle to immunoprecipitation experiments done with cultured DRG explants.
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    Image Search Results


    (A) Representative confocal images of axon with growth cones stained for tyrosinated α-tubulin (Tyr, red), F-actin (phalloidin, magenta), and phosphorylated-VASH1 (P[S337]VASH1, gray). Scale bar, 10 µm. ( B ) Quantification of P[S337]VASH1 in growth cones of WT and Vash1 KO neurons. n/N: 67/5 (WT), 111/7 (KO) with n indicating the number of growth cones and N of E13 embryos. Data are expressed as mean ± SD and as fold change over WT. ( C ) Quantification of P[S337]VASH1 in growth cones without treatment or with CNP treatment. n/N: 61/4 (control), 48/3 (CNP) with n indicating the number of growth cones and N the number of E13 embryos. Data are expressed as mean ± SD and as fold change over control. Statistical significance was determined using Mann-Witney test. **** p < 0.0001, ns p > 0.05. ( D, E ) Detection by immunoblot of VASH1 protein and its phosphorylated form in cultured DRG neurons after immunoprecipitation using an anti-SVBP antibody. β-tubulin staining shows similar protein content in the immunoprecipitation inputs. ( D ) Both VASH1 protein and its phosphorylated form are detected in WT but not in Vash1 KO DRGs. Treatment with Lambda protein phosphatase results in the loss of P[S337]VASH1 band. ( E, F ) CNP induces phosphorylation of S337 of VASH1, which is reversed by DT-3, as shown by representative immunoblots from an experiment done with cultured DRG explants ( E ) and quantifications of the P[S337]VASH1/VASH1 ratios from 4 independent experiments ( F ). In F , triangles correspond to data from immunoprecipitation experiments done with cultured DRG dissociated neurons, and circle to immunoprecipitation experiments done with cultured DRG explants.

    Journal: bioRxiv

    Article Title: VASH1 phosphorylation regulates tubulin detyrosination via CNP/PRKG1α signaling in DRG neurons

    doi: 10.64898/2026.10.14.759141

    Figure Lengend Snippet: (A) Representative confocal images of axon with growth cones stained for tyrosinated α-tubulin (Tyr, red), F-actin (phalloidin, magenta), and phosphorylated-VASH1 (P[S337]VASH1, gray). Scale bar, 10 µm. ( B ) Quantification of P[S337]VASH1 in growth cones of WT and Vash1 KO neurons. n/N: 67/5 (WT), 111/7 (KO) with n indicating the number of growth cones and N of E13 embryos. Data are expressed as mean ± SD and as fold change over WT. ( C ) Quantification of P[S337]VASH1 in growth cones without treatment or with CNP treatment. n/N: 61/4 (control), 48/3 (CNP) with n indicating the number of growth cones and N the number of E13 embryos. Data are expressed as mean ± SD and as fold change over control. Statistical significance was determined using Mann-Witney test. **** p < 0.0001, ns p > 0.05. ( D, E ) Detection by immunoblot of VASH1 protein and its phosphorylated form in cultured DRG neurons after immunoprecipitation using an anti-SVBP antibody. β-tubulin staining shows similar protein content in the immunoprecipitation inputs. ( D ) Both VASH1 protein and its phosphorylated form are detected in WT but not in Vash1 KO DRGs. Treatment with Lambda protein phosphatase results in the loss of P[S337]VASH1 band. ( E, F ) CNP induces phosphorylation of S337 of VASH1, which is reversed by DT-3, as shown by representative immunoblots from an experiment done with cultured DRG explants ( E ) and quantifications of the P[S337]VASH1/VASH1 ratios from 4 independent experiments ( F ). In F , triangles correspond to data from immunoprecipitation experiments done with cultured DRG dissociated neurons, and circle to immunoprecipitation experiments done with cultured DRG explants.

    Article Snippet: For phosphatase treatment experiments, bead-bound complexes were incubated with phosphatase (Lambda protein phosphatase, New England Biolabs) for 30 min at 30°C according to the manufacturer’s protocol before elution.

    Techniques: Confocal, Staining, Control, Western Blot, Cell Culture, Immunoprecipitation, Phospho-proteomics