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λ phosphatase  (New England Biolabs)


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    Structured Review

    New England Biolabs λ phosphatase
    λ Phosphatase, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 2943 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/lambda+phosphatase/Lambda+Protein+Phosphatase/pmc10041653-322-22-23
    Average 99 stars, based on 2943 article reviews
    λ phosphatase - by Bioz Stars, 2026-11
    99/100 stars

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    Related Articles

    Incubation:

    Article Title: Multi-omics and biochemical reconstitution reveal CDK7-dependent mechanisms controlling RNA polymerase II function at gene 5’- and 3’-ends
    Article Snippet: SuperSignal West Pico PLUS Chemiluminescent Substrate (Thermo Fisher Scientific, cat. #34579) was used for protein visualization following 1h secondary antibody incubation and TBS-T washes. .. After NTP addition and incubation (described above), IMT samples were placed on a magnetic strip, washed with 100μL wash buffer, and resuspended in 5μL 10× NEBuffer for Protein MetalloPhosphatases, 5μL 10 mM MnCl 2 , 35μL water, and 5μL Lambda Protein Phosphatase (New England Biolabs, cat. #P0753). ..

    Article Title: KaiC family ATPases in the nonheterocystous nitrogen-fixing cyanobacterium Leptolyngbya boryana
    Article Snippet: .. Moreover, 2 μg of the proteins purified in NEBuffer for phosphatase treatment with 1 mM MnCl 2 was added to 400 U of lambda protein phosphatase (NEB, MA, USA) and incubated at 30°C for 1 h. The reaction was stopped by adding SDS sample buffer, which was then boiled for 5 min. An aliquot of the sample was subjected to SDS–PAGE, followed by Coomassie Brilliant blue (CBB) staining. ..

    Article Title: KaiC family ATPases in the nonheterocystous nitrogen-fixing cyanobacterium Leptolyngbya boryana.
    Article Snippet: .. Moreover, 2 μg of the proteins purified in NEBuffer for phosphatase treatment with 1 mM MnCl2 was added to 400 U of lambda protein phosphatase (NEB, MA, USA) and incubated at 30°C for 1 h. The reaction was stopped by adding SDS sample buffer, which was then boiled for 5 min. An aliquot of the sample was subjected to SDS–PAGE, followed by Coomassie Brilliant blue (CBB) staining. ..

    Stripping Membranes:

    Article Title: Multi-omics and biochemical reconstitution reveal CDK7-dependent mechanisms controlling RNA polymerase II function at gene 5’- and 3’-ends
    Article Snippet: SuperSignal West Pico PLUS Chemiluminescent Substrate (Thermo Fisher Scientific, cat. #34579) was used for protein visualization following 1h secondary antibody incubation and TBS-T washes. .. After NTP addition and incubation (described above), IMT samples were placed on a magnetic strip, washed with 100μL wash buffer, and resuspended in 5μL 10× NEBuffer for Protein MetalloPhosphatases, 5μL 10 mM MnCl 2 , 35μL water, and 5μL Lambda Protein Phosphatase (New England Biolabs, cat. #P0753). ..

    Western Blot:

    Article Title: FUBP3 mediates the amyloid-β-induced neuronal NLRP3 expression
    Article Snippet: .. To confirm the specificity of the phospho-tau antibodies, brain lysates from C57BL/6J mice were treated with 400 units of λ-protein phosphatase (CatP0753S, New England Biolabd, Beijing, China), following the manufacturer’s instructions, before being subjected to western blotting. ..

    Purification:

    Article Title: KaiC family ATPases in the nonheterocystous nitrogen-fixing cyanobacterium Leptolyngbya boryana
    Article Snippet: .. Moreover, 2 μg of the proteins purified in NEBuffer for phosphatase treatment with 1 mM MnCl 2 was added to 400 U of lambda protein phosphatase (NEB, MA, USA) and incubated at 30°C for 1 h. The reaction was stopped by adding SDS sample buffer, which was then boiled for 5 min. An aliquot of the sample was subjected to SDS–PAGE, followed by Coomassie Brilliant blue (CBB) staining. ..

    Article Title: KaiC family ATPases in the nonheterocystous nitrogen-fixing cyanobacterium Leptolyngbya boryana.
    Article Snippet: .. Moreover, 2 μg of the proteins purified in NEBuffer for phosphatase treatment with 1 mM MnCl2 was added to 400 U of lambda protein phosphatase (NEB, MA, USA) and incubated at 30°C for 1 h. The reaction was stopped by adding SDS sample buffer, which was then boiled for 5 min. An aliquot of the sample was subjected to SDS–PAGE, followed by Coomassie Brilliant blue (CBB) staining. ..

    Staining:

    Article Title: KaiC family ATPases in the nonheterocystous nitrogen-fixing cyanobacterium Leptolyngbya boryana
    Article Snippet: .. Moreover, 2 μg of the proteins purified in NEBuffer for phosphatase treatment with 1 mM MnCl 2 was added to 400 U of lambda protein phosphatase (NEB, MA, USA) and incubated at 30°C for 1 h. The reaction was stopped by adding SDS sample buffer, which was then boiled for 5 min. An aliquot of the sample was subjected to SDS–PAGE, followed by Coomassie Brilliant blue (CBB) staining. ..

    Article Title: KaiC family ATPases in the nonheterocystous nitrogen-fixing cyanobacterium Leptolyngbya boryana.
    Article Snippet: .. Moreover, 2 μg of the proteins purified in NEBuffer for phosphatase treatment with 1 mM MnCl2 was added to 400 U of lambda protein phosphatase (NEB, MA, USA) and incubated at 30°C for 1 h. The reaction was stopped by adding SDS sample buffer, which was then boiled for 5 min. An aliquot of the sample was subjected to SDS–PAGE, followed by Coomassie Brilliant blue (CBB) staining. ..



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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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    (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