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    New England Biolabs phosphatase
    (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.
    Phosphatase, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 2929 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/lambda+phosphatase/Lambda+Protein+Phosphatase/bio_rxiv__64898__2026__10__14__759141-247-9-13
    Average 99 stars, based on 2929 article reviews
    phosphatase - by Bioz Stars, 2026-11
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    Images

    1) Product Images from "VASH1 phosphorylation regulates tubulin detyrosination via CNP/PRKG1α signaling in DRG neurons"

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

    Journal: bioRxiv

    doi: 10.64898/2026.10.14.759141

    (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.
    Figure Legend 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.

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

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    Incubation:

    Article Title: Large Library Docking for Polypharmacology
    Article Snippet: .. Elution was incubated with 5 μL lambda phosphatase (supplemented with 1 mM MnCl2 for activity), 1 μL CIP (NEB), 1 uL Antarctic phosphatase, and incubated at 4 °C for 30 min with gentle rocking. ..

    Activity Assay:

    Article Title: Large Library Docking for Polypharmacology
    Article Snippet: .. Elution was incubated with 5 μL lambda phosphatase (supplemented with 1 mM MnCl2 for activity), 1 μL CIP (NEB), 1 uL Antarctic phosphatase, and incubated at 4 °C for 30 min with gentle rocking. ..

    Gentle:

    Article Title: Large Library Docking for Polypharmacology
    Article Snippet: .. Elution was incubated with 5 μL lambda phosphatase (supplemented with 1 mM MnCl2 for activity), 1 μL CIP (NEB), 1 uL Antarctic phosphatase, and incubated at 4 °C for 30 min with gentle rocking. ..

    Recombinant:

    Article Title: GCN2 and perk kinase inhibitors and methods of use thereof
    Article Snippet: .. Recombinant GCN2 (EIF2AK4) (Carna Biosciences, Japan) was dephosphorylated by incubating with 16,000 units of lambda phosphatase (New England Biolabs, Ipswich, MA) for 3 h at 30° C. in 1× phosphatase reaction buffer. .. To measure Compound 2-mediated GCN2 modulation, 12.5 nM dephosphorylated GCN2 diluted in Kinase buffer (Invitrogen, Carlsbad, CA) was incubated with Compound 2 titer for 30 min at RT.

    De-Phosphorylation Assay:

    Article Title: Phosphorylation by CDK1 switches the function of the human SLX4 SAP domain from DNA binding to MUS81 binding
    Article Snippet: The protocol described in Ref [ ] was used to phosphorylate with CDK1-CycB1 (Lifetechnology) and purify the rSAP and rSAP4TA proteins. .. Dephosphorylation was achieved by incubating samples for 1 h at 30°C with 1 μl of lambda phosphatase (NEB) for 9 μM of SAP, 1X phosphatase buffer, and 1 mM MgCl 2 , in a final volume of 10 μl. ..

    Article Title: Ser423-phosphorylated MECP2 (MECP2-pS423) accumulates in human brain, cerebrospinal fluid and serum in sporadic Alzheimer's disease.
    Article Snippet: Methyl-CpG-binding protein 2 (MECP2) is a nuclear protein that serves as a global epigenetic repressor.. Activity-dependent Ser421-phosphorylation is permissive to translocation of mouse Mecp2 to the cytoplasm, thereby reducing the repressor functions and activating neurotrophins.. Mecp2-pS421 levels increase in neuron soma of AD (APP/PS1) mouse model and ablating Mecp2 increases activity of glycogen synthase kinase 3 beta, implying a link between MECP2 phosphorylation and Tau pathology in Alzheimer’s disease (AD).

    Sample Prep:

    Article Title: Microtubules guide Aurora B substrate geometries for accurate chromosome segregation
    Article Snippet: .. For sample preparation, freshly purified CeCPC or HsCPC proteins at 5.6 μM were first dephosphorylated using lambda phosphatase (NEB) at 30°C for 30 min and then desalted into binding buffer using a Zeba spin desalting column (Thermo Fisher Scientific). .. Freshly purified Hec1-Nuf2 complex, MCAK, or Ndc80C bonsai was diluted to 5.6 μM in binding buffer and then clarified by centrifugation at 17,000 g for 8 min at R.T. Cryo-EM grids (Quantifoil R 1.2/1.3 400 Mesh, Au) were prepared on a Vitrobot IV (Thermo Fisher Scientific) set to 100% humidity at 22°C.

    Purification:

    Article Title: Microtubules guide Aurora B substrate geometries for accurate chromosome segregation
    Article Snippet: .. For sample preparation, freshly purified CeCPC or HsCPC proteins at 5.6 μM were first dephosphorylated using lambda phosphatase (NEB) at 30°C for 30 min and then desalted into binding buffer using a Zeba spin desalting column (Thermo Fisher Scientific). .. Freshly purified Hec1-Nuf2 complex, MCAK, or Ndc80C bonsai was diluted to 5.6 μM in binding buffer and then clarified by centrifugation at 17,000 g for 8 min at R.T. Cryo-EM grids (Quantifoil R 1.2/1.3 400 Mesh, Au) were prepared on a Vitrobot IV (Thermo Fisher Scientific) set to 100% humidity at 22°C.

    Article Title: A pathological phosphorylation pattern enhances tau cooperativity on microtubules and facilitates tau filament assembly
    Article Snippet: Briefly, differentially phosphorylated StrepII-SNAP- Communications Biology Article in Press tau proteins were diluted to ~ 25 μM by purification buffer (50mM Tris–HCl pH 8.0, 150mM KCH3COO, 2mM MgSO4, 1mM EGTA, 5% glycerol), then incubated with 50 μM of SNAP-Surface 649 on ice for 2 h. Excess SNAP-Surface 649 was removed by 5mLHiTrap Desalting column (Cytiva) equilibrated with PB buffer. .. Purified SF9 expressed sfGFP-Tau was diluted to 2uM in a 25ul solution containing 1x Protein Metallophosphatase buffer (NEB), 1 mM MnCl2 (NEB), and 400 units of Lambda Phosphatase (NEB). ..

    Binding Assay:

    Article Title: Microtubules guide Aurora B substrate geometries for accurate chromosome segregation
    Article Snippet: .. For sample preparation, freshly purified CeCPC or HsCPC proteins at 5.6 μM were first dephosphorylated using lambda phosphatase (NEB) at 30°C for 30 min and then desalted into binding buffer using a Zeba spin desalting column (Thermo Fisher Scientific). .. Freshly purified Hec1-Nuf2 complex, MCAK, or Ndc80C bonsai was diluted to 5.6 μM in binding buffer and then clarified by centrifugation at 17,000 g for 8 min at R.T. Cryo-EM grids (Quantifoil R 1.2/1.3 400 Mesh, Au) were prepared on a Vitrobot IV (Thermo Fisher Scientific) set to 100% humidity at 22°C.



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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 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