heparinase i ii iii  (New England Biolabs)


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    New England Biolabs heparinase i ii iii
    Heparinase I Ii Iii, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    heparinase i ii iii  (New England Biolabs)


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    New England Biolabs heparinase i ii iii
    Heparinase I Ii Iii, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    heparinase i new england biolabs cat  (New England Biolabs)


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    New England Biolabs heparinase i new england biolabs cat
    Heparinase I New England Biolabs Cat, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    heparinase i ii iii  (New England Biolabs)


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    New England Biolabs heparinase i ii iii

    Heparinase I Ii Iii, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Receptor transfer between immune cells by autoantibody-enhanced, CD32-driven trogocytosis is hijacked by HIV-1 to infect resting CD4 T cells"

    Article Title: Receptor transfer between immune cells by autoantibody-enhanced, CD32-driven trogocytosis is hijacked by HIV-1 to infect resting CD4 T cells

    Journal: Cell Reports Medicine

    doi: 10.1016/j.xcrm.2024.101483


    Figure Legend Snippet:

    Techniques Used: Purification, Virus, Recombinant, Staining, Western Blot, Cell Isolation, Isolation, Marker, BIA-KA, Software, Membrane, Cell Culture

    heparinase i  (New England Biolabs)


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    New England Biolabs heparinase i

    Heparinase I, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Receptor transfer between immune cells by autoantibody-enhanced, CD32-driven trogocytosis is hijacked by HIV-1 to infect resting CD4 T cells"

    Article Title: Receptor transfer between immune cells by autoantibody-enhanced, CD32-driven trogocytosis is hijacked by HIV-1 to infect resting CD4 T cells

    Journal: Cell Reports Medicine

    doi: 10.1016/j.xcrm.2024.101483


    Figure Legend Snippet:

    Techniques Used: Purification, Virus, Recombinant, Staining, Western Blot, Cell Isolation, Isolation, Marker, BIA-KA, Software, Membrane, Cell Culture

    heparinase i  (New England Biolabs)


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    New England Biolabs heparinase i
    Heparan sulfate serves as an essential factor during SADS-CoV attachment. (A) Vero cells were pretreated with <t>heparinase</t> <t>I</t> or III at 37°C for 2 h to remove the heparan sulfate (HS) on the cell surface, and then infected with rSADS-GFP at MOI = 0.1. Alternatively, HS (B), glycosaminoglycans (C) such as chondroitin sulfate A (CSA) or hyaluronic acid (Ha), or monosaccharides (D) including galactose (Gal), glucose (Glu), N-acetyl-D-glucosamine (GlcNac), or N-acetyl-D-galactosamine (GalNac) were incubated with rSADS-GFP prior to infection of Vero cells. Supernatants were harvested at 24 h post-infection (hpi) to determine virus titer by qRT-PCR analysis targeting the N gene. **: P ≤ 0.01; ns: not significant. (E) Schematic representation of glycosaminoglycan chains of HS, CSA, and Ha consisting of disaccharide units with various monosaccharides. HS and CSA are connected to proteoglycan via a serine residue, while Ha was found as a free sugar chain in the extracellular matrix.
    Heparinase I, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Functional dissection of the spike glycoprotein S1 subunit and identification of cellular cofactors for regulation of swine acute diarrhea syndrome coronavirus entry"

    Article Title: Functional dissection of the spike glycoprotein S1 subunit and identification of cellular cofactors for regulation of swine acute diarrhea syndrome coronavirus entry

    Journal: Journal of Virology

    doi: 10.1128/jvi.00139-24

    Heparan sulfate serves as an essential factor during SADS-CoV attachment. (A) Vero cells were pretreated with heparinase I or III at 37°C for 2 h to remove the heparan sulfate (HS) on the cell surface, and then infected with rSADS-GFP at MOI = 0.1. Alternatively, HS (B), glycosaminoglycans (C) such as chondroitin sulfate A (CSA) or hyaluronic acid (Ha), or monosaccharides (D) including galactose (Gal), glucose (Glu), N-acetyl-D-glucosamine (GlcNac), or N-acetyl-D-galactosamine (GalNac) were incubated with rSADS-GFP prior to infection of Vero cells. Supernatants were harvested at 24 h post-infection (hpi) to determine virus titer by qRT-PCR analysis targeting the N gene. **: P ≤ 0.01; ns: not significant. (E) Schematic representation of glycosaminoglycan chains of HS, CSA, and Ha consisting of disaccharide units with various monosaccharides. HS and CSA are connected to proteoglycan via a serine residue, while Ha was found as a free sugar chain in the extracellular matrix.
    Figure Legend Snippet: Heparan sulfate serves as an essential factor during SADS-CoV attachment. (A) Vero cells were pretreated with heparinase I or III at 37°C for 2 h to remove the heparan sulfate (HS) on the cell surface, and then infected with rSADS-GFP at MOI = 0.1. Alternatively, HS (B), glycosaminoglycans (C) such as chondroitin sulfate A (CSA) or hyaluronic acid (Ha), or monosaccharides (D) including galactose (Gal), glucose (Glu), N-acetyl-D-glucosamine (GlcNac), or N-acetyl-D-galactosamine (GalNac) were incubated with rSADS-GFP prior to infection of Vero cells. Supernatants were harvested at 24 h post-infection (hpi) to determine virus titer by qRT-PCR analysis targeting the N gene. **: P ≤ 0.01; ns: not significant. (E) Schematic representation of glycosaminoglycan chains of HS, CSA, and Ha consisting of disaccharide units with various monosaccharides. HS and CSA are connected to proteoglycan via a serine residue, while Ha was found as a free sugar chain in the extracellular matrix.

    Techniques Used: Infection, Incubation, Virus, Quantitative RT-PCR, Residue

    heparinase i  (New England Biolabs)


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    New England Biolabs heparinase i
    Heparan sulfate serves as an essential factor during SADS-CoV attachment. (A) Vero cells were pretreated with <t>heparinase</t> <t>I</t> or III at 37°C for 2 h to remove the heparan sulfate (HS) on the cell surface, and then infected with rSADS-GFP at MOI = 0.1. Alternatively, HS (B), glycosaminoglycans (C) such as chondroitin sulfate A (CSA) or hyaluronic acid (Ha), or monosaccharides (D) including galactose (Gal), glucose (Glu), N-acetyl-D-glucosamine (GlcNac), or N-acetyl-D-galactosamine (GalNac) were incubated with rSADS-GFP prior to infection of Vero cells. Supernatants were harvested at 24 h post-infection (hpi) to determine virus titer by qRT-PCR analysis targeting the N gene. **: P ≤ 0.01; ns: not significant. (E) Schematic representation of glycosaminoglycan chains of HS, CSA, and Ha consisting of disaccharide units with various monosaccharides. HS and CSA are connected to proteoglycan via a serine residue, while Ha was found as a free sugar chain in the extracellular matrix.
    Heparinase I, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Functional dissection of the spike glycoprotein S1 subunit and identification of cellular cofactors for regulation of swine acute diarrhea syndrome coronavirus entry"

    Article Title: Functional dissection of the spike glycoprotein S1 subunit and identification of cellular cofactors for regulation of swine acute diarrhea syndrome coronavirus entry

    Journal: Journal of Virology

    doi: 10.1128/jvi.00139-24

    Heparan sulfate serves as an essential factor during SADS-CoV attachment. (A) Vero cells were pretreated with heparinase I or III at 37°C for 2 h to remove the heparan sulfate (HS) on the cell surface, and then infected with rSADS-GFP at MOI = 0.1. Alternatively, HS (B), glycosaminoglycans (C) such as chondroitin sulfate A (CSA) or hyaluronic acid (Ha), or monosaccharides (D) including galactose (Gal), glucose (Glu), N-acetyl-D-glucosamine (GlcNac), or N-acetyl-D-galactosamine (GalNac) were incubated with rSADS-GFP prior to infection of Vero cells. Supernatants were harvested at 24 h post-infection (hpi) to determine virus titer by qRT-PCR analysis targeting the N gene. **: P ≤ 0.01; ns: not significant. (E) Schematic representation of glycosaminoglycan chains of HS, CSA, and Ha consisting of disaccharide units with various monosaccharides. HS and CSA are connected to proteoglycan via a serine residue, while Ha was found as a free sugar chain in the extracellular matrix.
    Figure Legend Snippet: Heparan sulfate serves as an essential factor during SADS-CoV attachment. (A) Vero cells were pretreated with heparinase I or III at 37°C for 2 h to remove the heparan sulfate (HS) on the cell surface, and then infected with rSADS-GFP at MOI = 0.1. Alternatively, HS (B), glycosaminoglycans (C) such as chondroitin sulfate A (CSA) or hyaluronic acid (Ha), or monosaccharides (D) including galactose (Gal), glucose (Glu), N-acetyl-D-glucosamine (GlcNac), or N-acetyl-D-galactosamine (GalNac) were incubated with rSADS-GFP prior to infection of Vero cells. Supernatants were harvested at 24 h post-infection (hpi) to determine virus titer by qRT-PCR analysis targeting the N gene. **: P ≤ 0.01; ns: not significant. (E) Schematic representation of glycosaminoglycan chains of HS, CSA, and Ha consisting of disaccharide units with various monosaccharides. HS and CSA are connected to proteoglycan via a serine residue, while Ha was found as a free sugar chain in the extracellular matrix.

    Techniques Used: Infection, Incubation, Virus, Quantitative RT-PCR, Residue

    l protein phosphatase  (New England Biolabs)


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    New England Biolabs l protein phosphatase
    Increased phosphorylation of Liprin-α1 in cells overexpressing DYRK3 (A) COS7 cells co-expressing either GFP or GFP-DYRK3 with FLAG-LL5α, -Liprin-α1 or -ERC1 were lysed and analyzed by immunoblotting. A clear shift of part of the band corresponding to lower mobility (red arrowhead) induced by co-expression of DYRK3 was observed only for Liprin-α1. RACK1 used as loading control. (B) Incubation with the λ <t>phosphatase</t> to eliminate phosphorylation increases the mobility of Liprin-α1. (C) COS7 cells co-expressing GFP, GFP-DYRK3 or GFP-DYRK3 K218M with FLAG-Liprin-α1. A clear shift of part of the Liprin-α1 band was observed only in the presence of wild type DYRK3 (left). Immunoprecipitation (right) with anti-Liprin-α1 antibody of FLAG-Liprin-α1 from COS7 cells co-expressing either GFP or GFP-DYRK3. Immunoprecipitates (150 μg protein lysate/lane) and lysates (20 μg protein lysate/lane) were blotted with anti-FLAG (to detect FLAG-Liprin-α1), DYRK3, and GFP Abs. (D) Phosphorylation of endogenous Liprin-α in COS7 and HEK293 cells expressing either GFP or GFP-DYRK3. Cells lysates analyzed by immunoblotting after PhosTag gel (10 μg protein lysate/lane loaded on 6% acrylamide gel with 25 μM PhosTag). Smear for lower mobility (red arrows) was enhanced by GFP-DYRK3 overexpression. (E) MDA-MB-231 cells expressing either GFP or GFP-DYRK3 were incubated for 2 h with 1 μM of the DYRK3 inhibitor GSK-626616 (GSK +) or with control serum-free medium with DMSO (GSK –). Lysates were run on PhosTag SDS-PAGE (top filter: 10 μg protein lysate/lane loaded on 6% acrylamide gel with 25 μM PhosTag), or SDS-PAGE (middle and bottom filters: 30 μg protein lysate/lane loaded on 4–15% acrylamide gradient gels), and blotted to reveal endogenous Liprin-α1 (eLiprin-α1), GFP-DYRK3 and GFP.
    L Protein Phosphatase, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Dual specificity kinase DYRK3 regulates cell migration by influencing the stability of protrusions"

    Article Title: Dual specificity kinase DYRK3 regulates cell migration by influencing the stability of protrusions

    Journal: iScience

    doi: 10.1016/j.isci.2024.109440

    Increased phosphorylation of Liprin-α1 in cells overexpressing DYRK3 (A) COS7 cells co-expressing either GFP or GFP-DYRK3 with FLAG-LL5α, -Liprin-α1 or -ERC1 were lysed and analyzed by immunoblotting. A clear shift of part of the band corresponding to lower mobility (red arrowhead) induced by co-expression of DYRK3 was observed only for Liprin-α1. RACK1 used as loading control. (B) Incubation with the λ phosphatase to eliminate phosphorylation increases the mobility of Liprin-α1. (C) COS7 cells co-expressing GFP, GFP-DYRK3 or GFP-DYRK3 K218M with FLAG-Liprin-α1. A clear shift of part of the Liprin-α1 band was observed only in the presence of wild type DYRK3 (left). Immunoprecipitation (right) with anti-Liprin-α1 antibody of FLAG-Liprin-α1 from COS7 cells co-expressing either GFP or GFP-DYRK3. Immunoprecipitates (150 μg protein lysate/lane) and lysates (20 μg protein lysate/lane) were blotted with anti-FLAG (to detect FLAG-Liprin-α1), DYRK3, and GFP Abs. (D) Phosphorylation of endogenous Liprin-α in COS7 and HEK293 cells expressing either GFP or GFP-DYRK3. Cells lysates analyzed by immunoblotting after PhosTag gel (10 μg protein lysate/lane loaded on 6% acrylamide gel with 25 μM PhosTag). Smear for lower mobility (red arrows) was enhanced by GFP-DYRK3 overexpression. (E) MDA-MB-231 cells expressing either GFP or GFP-DYRK3 were incubated for 2 h with 1 μM of the DYRK3 inhibitor GSK-626616 (GSK +) or with control serum-free medium with DMSO (GSK –). Lysates were run on PhosTag SDS-PAGE (top filter: 10 μg protein lysate/lane loaded on 6% acrylamide gel with 25 μM PhosTag), or SDS-PAGE (middle and bottom filters: 30 μg protein lysate/lane loaded on 4–15% acrylamide gradient gels), and blotted to reveal endogenous Liprin-α1 (eLiprin-α1), GFP-DYRK3 and GFP.
    Figure Legend Snippet: Increased phosphorylation of Liprin-α1 in cells overexpressing DYRK3 (A) COS7 cells co-expressing either GFP or GFP-DYRK3 with FLAG-LL5α, -Liprin-α1 or -ERC1 were lysed and analyzed by immunoblotting. A clear shift of part of the band corresponding to lower mobility (red arrowhead) induced by co-expression of DYRK3 was observed only for Liprin-α1. RACK1 used as loading control. (B) Incubation with the λ phosphatase to eliminate phosphorylation increases the mobility of Liprin-α1. (C) COS7 cells co-expressing GFP, GFP-DYRK3 or GFP-DYRK3 K218M with FLAG-Liprin-α1. A clear shift of part of the Liprin-α1 band was observed only in the presence of wild type DYRK3 (left). Immunoprecipitation (right) with anti-Liprin-α1 antibody of FLAG-Liprin-α1 from COS7 cells co-expressing either GFP or GFP-DYRK3. Immunoprecipitates (150 μg protein lysate/lane) and lysates (20 μg protein lysate/lane) were blotted with anti-FLAG (to detect FLAG-Liprin-α1), DYRK3, and GFP Abs. (D) Phosphorylation of endogenous Liprin-α in COS7 and HEK293 cells expressing either GFP or GFP-DYRK3. Cells lysates analyzed by immunoblotting after PhosTag gel (10 μg protein lysate/lane loaded on 6% acrylamide gel with 25 μM PhosTag). Smear for lower mobility (red arrows) was enhanced by GFP-DYRK3 overexpression. (E) MDA-MB-231 cells expressing either GFP or GFP-DYRK3 were incubated for 2 h with 1 μM of the DYRK3 inhibitor GSK-626616 (GSK +) or with control serum-free medium with DMSO (GSK –). Lysates were run on PhosTag SDS-PAGE (top filter: 10 μg protein lysate/lane loaded on 6% acrylamide gel with 25 μM PhosTag), or SDS-PAGE (middle and bottom filters: 30 μg protein lysate/lane loaded on 4–15% acrylamide gradient gels), and blotted to reveal endogenous Liprin-α1 (eLiprin-α1), GFP-DYRK3 and GFP.

    Techniques Used: Expressing, Western Blot, Incubation, Immunoprecipitation, Acrylamide Gel Assay, Over Expression, SDS Page

    N-terminal region of Liprin-α1 contains phosphorylation sites regulated by DYRK3 enzymatic activity (A) Scheme of Liprin-α1 and its N-terminal region Liprin(1–675). (B) Lysates from COS7 cells co-transfected with either GFP or GFP-DYRK3 together with the N-terminal Liprin(1–675) fragment. Smear of the Liprin(1–675) band (red arrowhead) was observed only in lysates from cells co-expressing GFP-DYRK3, and was abolished by incubation with λ phosphatase. (C) Left filters: phosphorylation of N-terminal Liprin(1–675) was detected by immunoblotting from PhosTag gels (7% acrylamide with 50 μM PhosTag) loaded with lysates from cells co-expressing Liprin(1–675) with either GFP (lane 1) or GFP-DYRK3 (lanes 2, 3). Sample in lane 3 was loaded after incubation with λ phosphatase. Right filters: enhanced resolution of DYRK3-induced phosphorylation of Liprin(1–675) after SDS-PAGE on 7% acrylamide gels supplemented with 25 μM PhosTag. (D) Cotransfected COS7 cells analyzed by immunoblotting from 7% acrylamide gels supplemented with 25 μM PhosTag. Incubation for 2 h with 1 μM of the DYRK3 inhibitor GSK-626616 abolished phosphorylation of Liprin(1–675) induced by DYRK3 co-expression (asterisk). (E) Quantification of the increased phosphorylation of Liprin(1–675) induced by DYRK3 (asterisk in panel D); mean ± SEM; n = 3 experiments. Brown-Forsythe and Welch ANOVA test with Dunnett’s T3 posthoc.
    Figure Legend Snippet: N-terminal region of Liprin-α1 contains phosphorylation sites regulated by DYRK3 enzymatic activity (A) Scheme of Liprin-α1 and its N-terminal region Liprin(1–675). (B) Lysates from COS7 cells co-transfected with either GFP or GFP-DYRK3 together with the N-terminal Liprin(1–675) fragment. Smear of the Liprin(1–675) band (red arrowhead) was observed only in lysates from cells co-expressing GFP-DYRK3, and was abolished by incubation with λ phosphatase. (C) Left filters: phosphorylation of N-terminal Liprin(1–675) was detected by immunoblotting from PhosTag gels (7% acrylamide with 50 μM PhosTag) loaded with lysates from cells co-expressing Liprin(1–675) with either GFP (lane 1) or GFP-DYRK3 (lanes 2, 3). Sample in lane 3 was loaded after incubation with λ phosphatase. Right filters: enhanced resolution of DYRK3-induced phosphorylation of Liprin(1–675) after SDS-PAGE on 7% acrylamide gels supplemented with 25 μM PhosTag. (D) Cotransfected COS7 cells analyzed by immunoblotting from 7% acrylamide gels supplemented with 25 μM PhosTag. Incubation for 2 h with 1 μM of the DYRK3 inhibitor GSK-626616 abolished phosphorylation of Liprin(1–675) induced by DYRK3 co-expression (asterisk). (E) Quantification of the increased phosphorylation of Liprin(1–675) induced by DYRK3 (asterisk in panel D); mean ± SEM; n = 3 experiments. Brown-Forsythe and Welch ANOVA test with Dunnett’s T3 posthoc.

    Techniques Used: Activity Assay, Transfection, Expressing, Incubation, Western Blot, SDS Page

    bacteroides heparinase  (New England Biolabs)


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    New England Biolabs bacteroides heparinase
    Bacteroides Heparinase, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    heparinase  (New England Biolabs)


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    New England Biolabs heparinase
    Heparinase, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    bacteroides  (New England Biolabs)


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    New England Biolabs bacteroides
    Bacteroides, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    New England Biolabs heparinase i ii iii
    Heparinase I Ii Iii, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Heparinase I, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    New England Biolabs l protein phosphatase
    Increased phosphorylation of Liprin-α1 in cells overexpressing DYRK3 (A) COS7 cells co-expressing either GFP or GFP-DYRK3 with FLAG-LL5α, -Liprin-α1 or -ERC1 were lysed and analyzed by immunoblotting. A clear shift of part of the band corresponding to lower mobility (red arrowhead) induced by co-expression of DYRK3 was observed only for Liprin-α1. RACK1 used as loading control. (B) Incubation with the λ <t>phosphatase</t> to eliminate phosphorylation increases the mobility of Liprin-α1. (C) COS7 cells co-expressing GFP, GFP-DYRK3 or GFP-DYRK3 K218M with FLAG-Liprin-α1. A clear shift of part of the Liprin-α1 band was observed only in the presence of wild type DYRK3 (left). Immunoprecipitation (right) with anti-Liprin-α1 antibody of FLAG-Liprin-α1 from COS7 cells co-expressing either GFP or GFP-DYRK3. Immunoprecipitates (150 μg protein lysate/lane) and lysates (20 μg protein lysate/lane) were blotted with anti-FLAG (to detect FLAG-Liprin-α1), DYRK3, and GFP Abs. (D) Phosphorylation of endogenous Liprin-α in COS7 and HEK293 cells expressing either GFP or GFP-DYRK3. Cells lysates analyzed by immunoblotting after PhosTag gel (10 μg protein lysate/lane loaded on 6% acrylamide gel with 25 μM PhosTag). Smear for lower mobility (red arrows) was enhanced by GFP-DYRK3 overexpression. (E) MDA-MB-231 cells expressing either GFP or GFP-DYRK3 were incubated for 2 h with 1 μM of the DYRK3 inhibitor GSK-626616 (GSK +) or with control serum-free medium with DMSO (GSK –). Lysates were run on PhosTag SDS-PAGE (top filter: 10 μg protein lysate/lane loaded on 6% acrylamide gel with 25 μM PhosTag), or SDS-PAGE (middle and bottom filters: 30 μg protein lysate/lane loaded on 4–15% acrylamide gradient gels), and blotted to reveal endogenous Liprin-α1 (eLiprin-α1), GFP-DYRK3 and GFP.
    L Protein Phosphatase, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    New England Biolabs bacteroides heparinase
    Increased phosphorylation of Liprin-α1 in cells overexpressing DYRK3 (A) COS7 cells co-expressing either GFP or GFP-DYRK3 with FLAG-LL5α, -Liprin-α1 or -ERC1 were lysed and analyzed by immunoblotting. A clear shift of part of the band corresponding to lower mobility (red arrowhead) induced by co-expression of DYRK3 was observed only for Liprin-α1. RACK1 used as loading control. (B) Incubation with the λ <t>phosphatase</t> to eliminate phosphorylation increases the mobility of Liprin-α1. (C) COS7 cells co-expressing GFP, GFP-DYRK3 or GFP-DYRK3 K218M with FLAG-Liprin-α1. A clear shift of part of the Liprin-α1 band was observed only in the presence of wild type DYRK3 (left). Immunoprecipitation (right) with anti-Liprin-α1 antibody of FLAG-Liprin-α1 from COS7 cells co-expressing either GFP or GFP-DYRK3. Immunoprecipitates (150 μg protein lysate/lane) and lysates (20 μg protein lysate/lane) were blotted with anti-FLAG (to detect FLAG-Liprin-α1), DYRK3, and GFP Abs. (D) Phosphorylation of endogenous Liprin-α in COS7 and HEK293 cells expressing either GFP or GFP-DYRK3. Cells lysates analyzed by immunoblotting after PhosTag gel (10 μg protein lysate/lane loaded on 6% acrylamide gel with 25 μM PhosTag). Smear for lower mobility (red arrows) was enhanced by GFP-DYRK3 overexpression. (E) MDA-MB-231 cells expressing either GFP or GFP-DYRK3 were incubated for 2 h with 1 μM of the DYRK3 inhibitor GSK-626616 (GSK +) or with control serum-free medium with DMSO (GSK –). Lysates were run on PhosTag SDS-PAGE (top filter: 10 μg protein lysate/lane loaded on 6% acrylamide gel with 25 μM PhosTag), or SDS-PAGE (middle and bottom filters: 30 μg protein lysate/lane loaded on 4–15% acrylamide gradient gels), and blotted to reveal endogenous Liprin-α1 (eLiprin-α1), GFP-DYRK3 and GFP.
    Bacteroides Heparinase, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    New England Biolabs heparinase
    Increased phosphorylation of Liprin-α1 in cells overexpressing DYRK3 (A) COS7 cells co-expressing either GFP or GFP-DYRK3 with FLAG-LL5α, -Liprin-α1 or -ERC1 were lysed and analyzed by immunoblotting. A clear shift of part of the band corresponding to lower mobility (red arrowhead) induced by co-expression of DYRK3 was observed only for Liprin-α1. RACK1 used as loading control. (B) Incubation with the λ <t>phosphatase</t> to eliminate phosphorylation increases the mobility of Liprin-α1. (C) COS7 cells co-expressing GFP, GFP-DYRK3 or GFP-DYRK3 K218M with FLAG-Liprin-α1. A clear shift of part of the Liprin-α1 band was observed only in the presence of wild type DYRK3 (left). Immunoprecipitation (right) with anti-Liprin-α1 antibody of FLAG-Liprin-α1 from COS7 cells co-expressing either GFP or GFP-DYRK3. Immunoprecipitates (150 μg protein lysate/lane) and lysates (20 μg protein lysate/lane) were blotted with anti-FLAG (to detect FLAG-Liprin-α1), DYRK3, and GFP Abs. (D) Phosphorylation of endogenous Liprin-α in COS7 and HEK293 cells expressing either GFP or GFP-DYRK3. Cells lysates analyzed by immunoblotting after PhosTag gel (10 μg protein lysate/lane loaded on 6% acrylamide gel with 25 μM PhosTag). Smear for lower mobility (red arrows) was enhanced by GFP-DYRK3 overexpression. (E) MDA-MB-231 cells expressing either GFP or GFP-DYRK3 were incubated for 2 h with 1 μM of the DYRK3 inhibitor GSK-626616 (GSK +) or with control serum-free medium with DMSO (GSK –). Lysates were run on PhosTag SDS-PAGE (top filter: 10 μg protein lysate/lane loaded on 6% acrylamide gel with 25 μM PhosTag), or SDS-PAGE (middle and bottom filters: 30 μg protein lysate/lane loaded on 4–15% acrylamide gradient gels), and blotted to reveal endogenous Liprin-α1 (eLiprin-α1), GFP-DYRK3 and GFP.
    Heparinase, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    New England Biolabs bacteroides
    Increased phosphorylation of Liprin-α1 in cells overexpressing DYRK3 (A) COS7 cells co-expressing either GFP or GFP-DYRK3 with FLAG-LL5α, -Liprin-α1 or -ERC1 were lysed and analyzed by immunoblotting. A clear shift of part of the band corresponding to lower mobility (red arrowhead) induced by co-expression of DYRK3 was observed only for Liprin-α1. RACK1 used as loading control. (B) Incubation with the λ <t>phosphatase</t> to eliminate phosphorylation increases the mobility of Liprin-α1. (C) COS7 cells co-expressing GFP, GFP-DYRK3 or GFP-DYRK3 K218M with FLAG-Liprin-α1. A clear shift of part of the Liprin-α1 band was observed only in the presence of wild type DYRK3 (left). Immunoprecipitation (right) with anti-Liprin-α1 antibody of FLAG-Liprin-α1 from COS7 cells co-expressing either GFP or GFP-DYRK3. Immunoprecipitates (150 μg protein lysate/lane) and lysates (20 μg protein lysate/lane) were blotted with anti-FLAG (to detect FLAG-Liprin-α1), DYRK3, and GFP Abs. (D) Phosphorylation of endogenous Liprin-α in COS7 and HEK293 cells expressing either GFP or GFP-DYRK3. Cells lysates analyzed by immunoblotting after PhosTag gel (10 μg protein lysate/lane loaded on 6% acrylamide gel with 25 μM PhosTag). Smear for lower mobility (red arrows) was enhanced by GFP-DYRK3 overexpression. (E) MDA-MB-231 cells expressing either GFP or GFP-DYRK3 were incubated for 2 h with 1 μM of the DYRK3 inhibitor GSK-626616 (GSK +) or with control serum-free medium with DMSO (GSK –). Lysates were run on PhosTag SDS-PAGE (top filter: 10 μg protein lysate/lane loaded on 6% acrylamide gel with 25 μM PhosTag), or SDS-PAGE (middle and bottom filters: 30 μg protein lysate/lane loaded on 4–15% acrylamide gradient gels), and blotted to reveal endogenous Liprin-α1 (eLiprin-α1), GFP-DYRK3 and GFP.
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    Image Search Results


    Journal: Cell Reports Medicine

    Article Title: Receptor transfer between immune cells by autoantibody-enhanced, CD32-driven trogocytosis is hijacked by HIV-1 to infect resting CD4 T cells

    doi: 10.1016/j.xcrm.2024.101483

    Figure Lengend Snippet:

    Article Snippet: Heparinase I , New England Biolabs , Cat#P0735S.

    Techniques: Purification, Virus, Recombinant, Staining, Western Blot, Cell Isolation, Isolation, Marker, BIA-KA, Software, Membrane, Cell Culture

    Increased phosphorylation of Liprin-α1 in cells overexpressing DYRK3 (A) COS7 cells co-expressing either GFP or GFP-DYRK3 with FLAG-LL5α, -Liprin-α1 or -ERC1 were lysed and analyzed by immunoblotting. A clear shift of part of the band corresponding to lower mobility (red arrowhead) induced by co-expression of DYRK3 was observed only for Liprin-α1. RACK1 used as loading control. (B) Incubation with the λ phosphatase to eliminate phosphorylation increases the mobility of Liprin-α1. (C) COS7 cells co-expressing GFP, GFP-DYRK3 or GFP-DYRK3 K218M with FLAG-Liprin-α1. A clear shift of part of the Liprin-α1 band was observed only in the presence of wild type DYRK3 (left). Immunoprecipitation (right) with anti-Liprin-α1 antibody of FLAG-Liprin-α1 from COS7 cells co-expressing either GFP or GFP-DYRK3. Immunoprecipitates (150 μg protein lysate/lane) and lysates (20 μg protein lysate/lane) were blotted with anti-FLAG (to detect FLAG-Liprin-α1), DYRK3, and GFP Abs. (D) Phosphorylation of endogenous Liprin-α in COS7 and HEK293 cells expressing either GFP or GFP-DYRK3. Cells lysates analyzed by immunoblotting after PhosTag gel (10 μg protein lysate/lane loaded on 6% acrylamide gel with 25 μM PhosTag). Smear for lower mobility (red arrows) was enhanced by GFP-DYRK3 overexpression. (E) MDA-MB-231 cells expressing either GFP or GFP-DYRK3 were incubated for 2 h with 1 μM of the DYRK3 inhibitor GSK-626616 (GSK +) or with control serum-free medium with DMSO (GSK –). Lysates were run on PhosTag SDS-PAGE (top filter: 10 μg protein lysate/lane loaded on 6% acrylamide gel with 25 μM PhosTag), or SDS-PAGE (middle and bottom filters: 30 μg protein lysate/lane loaded on 4–15% acrylamide gradient gels), and blotted to reveal endogenous Liprin-α1 (eLiprin-α1), GFP-DYRK3 and GFP.

    Journal: iScience

    Article Title: Dual specificity kinase DYRK3 regulates cell migration by influencing the stability of protrusions

    doi: 10.1016/j.isci.2024.109440

    Figure Lengend Snippet: Increased phosphorylation of Liprin-α1 in cells overexpressing DYRK3 (A) COS7 cells co-expressing either GFP or GFP-DYRK3 with FLAG-LL5α, -Liprin-α1 or -ERC1 were lysed and analyzed by immunoblotting. A clear shift of part of the band corresponding to lower mobility (red arrowhead) induced by co-expression of DYRK3 was observed only for Liprin-α1. RACK1 used as loading control. (B) Incubation with the λ phosphatase to eliminate phosphorylation increases the mobility of Liprin-α1. (C) COS7 cells co-expressing GFP, GFP-DYRK3 or GFP-DYRK3 K218M with FLAG-Liprin-α1. A clear shift of part of the Liprin-α1 band was observed only in the presence of wild type DYRK3 (left). Immunoprecipitation (right) with anti-Liprin-α1 antibody of FLAG-Liprin-α1 from COS7 cells co-expressing either GFP or GFP-DYRK3. Immunoprecipitates (150 μg protein lysate/lane) and lysates (20 μg protein lysate/lane) were blotted with anti-FLAG (to detect FLAG-Liprin-α1), DYRK3, and GFP Abs. (D) Phosphorylation of endogenous Liprin-α in COS7 and HEK293 cells expressing either GFP or GFP-DYRK3. Cells lysates analyzed by immunoblotting after PhosTag gel (10 μg protein lysate/lane loaded on 6% acrylamide gel with 25 μM PhosTag). Smear for lower mobility (red arrows) was enhanced by GFP-DYRK3 overexpression. (E) MDA-MB-231 cells expressing either GFP or GFP-DYRK3 were incubated for 2 h with 1 μM of the DYRK3 inhibitor GSK-626616 (GSK +) or with control serum-free medium with DMSO (GSK –). Lysates were run on PhosTag SDS-PAGE (top filter: 10 μg protein lysate/lane loaded on 6% acrylamide gel with 25 μM PhosTag), or SDS-PAGE (middle and bottom filters: 30 μg protein lysate/lane loaded on 4–15% acrylamide gradient gels), and blotted to reveal endogenous Liprin-α1 (eLiprin-α1), GFP-DYRK3 and GFP.

    Article Snippet: Dephosphorylation assays were performed with 5 units of l protein phosphatase (P0735S, New England Biolabs) per μg of protein lysate in 1× L phosphatase buffer (New England Biolabs buffer for protein metallo-phosphatases with MnCl 2 ), and incubated for 30 min at 30°C.

    Techniques: Expressing, Western Blot, Incubation, Immunoprecipitation, Acrylamide Gel Assay, Over Expression, SDS Page

    N-terminal region of Liprin-α1 contains phosphorylation sites regulated by DYRK3 enzymatic activity (A) Scheme of Liprin-α1 and its N-terminal region Liprin(1–675). (B) Lysates from COS7 cells co-transfected with either GFP or GFP-DYRK3 together with the N-terminal Liprin(1–675) fragment. Smear of the Liprin(1–675) band (red arrowhead) was observed only in lysates from cells co-expressing GFP-DYRK3, and was abolished by incubation with λ phosphatase. (C) Left filters: phosphorylation of N-terminal Liprin(1–675) was detected by immunoblotting from PhosTag gels (7% acrylamide with 50 μM PhosTag) loaded with lysates from cells co-expressing Liprin(1–675) with either GFP (lane 1) or GFP-DYRK3 (lanes 2, 3). Sample in lane 3 was loaded after incubation with λ phosphatase. Right filters: enhanced resolution of DYRK3-induced phosphorylation of Liprin(1–675) after SDS-PAGE on 7% acrylamide gels supplemented with 25 μM PhosTag. (D) Cotransfected COS7 cells analyzed by immunoblotting from 7% acrylamide gels supplemented with 25 μM PhosTag. Incubation for 2 h with 1 μM of the DYRK3 inhibitor GSK-626616 abolished phosphorylation of Liprin(1–675) induced by DYRK3 co-expression (asterisk). (E) Quantification of the increased phosphorylation of Liprin(1–675) induced by DYRK3 (asterisk in panel D); mean ± SEM; n = 3 experiments. Brown-Forsythe and Welch ANOVA test with Dunnett’s T3 posthoc.

    Journal: iScience

    Article Title: Dual specificity kinase DYRK3 regulates cell migration by influencing the stability of protrusions

    doi: 10.1016/j.isci.2024.109440

    Figure Lengend Snippet: N-terminal region of Liprin-α1 contains phosphorylation sites regulated by DYRK3 enzymatic activity (A) Scheme of Liprin-α1 and its N-terminal region Liprin(1–675). (B) Lysates from COS7 cells co-transfected with either GFP or GFP-DYRK3 together with the N-terminal Liprin(1–675) fragment. Smear of the Liprin(1–675) band (red arrowhead) was observed only in lysates from cells co-expressing GFP-DYRK3, and was abolished by incubation with λ phosphatase. (C) Left filters: phosphorylation of N-terminal Liprin(1–675) was detected by immunoblotting from PhosTag gels (7% acrylamide with 50 μM PhosTag) loaded with lysates from cells co-expressing Liprin(1–675) with either GFP (lane 1) or GFP-DYRK3 (lanes 2, 3). Sample in lane 3 was loaded after incubation with λ phosphatase. Right filters: enhanced resolution of DYRK3-induced phosphorylation of Liprin(1–675) after SDS-PAGE on 7% acrylamide gels supplemented with 25 μM PhosTag. (D) Cotransfected COS7 cells analyzed by immunoblotting from 7% acrylamide gels supplemented with 25 μM PhosTag. Incubation for 2 h with 1 μM of the DYRK3 inhibitor GSK-626616 abolished phosphorylation of Liprin(1–675) induced by DYRK3 co-expression (asterisk). (E) Quantification of the increased phosphorylation of Liprin(1–675) induced by DYRK3 (asterisk in panel D); mean ± SEM; n = 3 experiments. Brown-Forsythe and Welch ANOVA test with Dunnett’s T3 posthoc.

    Article Snippet: Dephosphorylation assays were performed with 5 units of l protein phosphatase (P0735S, New England Biolabs) per μg of protein lysate in 1× L phosphatase buffer (New England Biolabs buffer for protein metallo-phosphatases with MnCl 2 ), and incubated for 30 min at 30°C.

    Techniques: Activity Assay, Transfection, Expressing, Incubation, Western Blot, SDS Page