n acetylgalactosaminidase  (New England Biolabs)


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    New England Biolabs n acetylgalactosaminidase
    N Acetylgalactosaminidase, 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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    α n acetylgalactosaminidase  (New England Biolabs)


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    New England Biolabs α n acetylgalactosaminidase
    α N Acetylgalactosaminidase, 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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    endo α n acetylgalactosaminidase  (New England Biolabs)


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    New England Biolabs endo α n acetylgalactosaminidase
    Endo α N Acetylgalactosaminidase, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    endo α n acetylgalactosaminidase  (New England Biolabs)


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    New England Biolabs endo α n acetylgalactosaminidase
    (a) Western blot of splenic membrane and serum proteins. (b) Western blot analysis of the IgD glycosylation in bovine serum. 1, Untreated serum proteins; 2, <t>endo-α-N-acetylgalactosaminidase-treated</t> serum proteins; 3, PNGase-treated serum proteins. The primary antibody 13C2 was diluted at 1∶200 or 1∶400. (c) Serum immunoblot analysis with mAb 13C2 and anti-bovine IgM polyclonal antibody under nonreducing conditions. The arrow indicates the monomer of IgD. (d) Immunoblot detection of serum IgD and IgM in differently aged cows. 1, 60 days old; 2, 180 days; 3, 1 year; 4, 2 years; 5, 3 years; 6, 4 years; 7, 5 years; 8, 6 years. The arrows indicate the IgD heavy chain.
    Endo α N Acetylgalactosaminidase, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Expressional Analysis of Immunoglobulin D in Cattle ( Bos taurus ), a Large Domesticated Ungulate"

    Article Title: Expressional Analysis of Immunoglobulin D in Cattle ( Bos taurus ), a Large Domesticated Ungulate

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0044719

    (a) Western blot of splenic membrane and serum proteins. (b) Western blot analysis of the IgD glycosylation in bovine serum. 1, Untreated serum proteins; 2, endo-α-N-acetylgalactosaminidase-treated serum proteins; 3, PNGase-treated serum proteins. The primary antibody 13C2 was diluted at 1∶200 or 1∶400. (c) Serum immunoblot analysis with mAb 13C2 and anti-bovine IgM polyclonal antibody under nonreducing conditions. The arrow indicates the monomer of IgD. (d) Immunoblot detection of serum IgD and IgM in differently aged cows. 1, 60 days old; 2, 180 days; 3, 1 year; 4, 2 years; 5, 3 years; 6, 4 years; 7, 5 years; 8, 6 years. The arrows indicate the IgD heavy chain.
    Figure Legend Snippet: (a) Western blot of splenic membrane and serum proteins. (b) Western blot analysis of the IgD glycosylation in bovine serum. 1, Untreated serum proteins; 2, endo-α-N-acetylgalactosaminidase-treated serum proteins; 3, PNGase-treated serum proteins. The primary antibody 13C2 was diluted at 1∶200 or 1∶400. (c) Serum immunoblot analysis with mAb 13C2 and anti-bovine IgM polyclonal antibody under nonreducing conditions. The arrow indicates the monomer of IgD. (d) Immunoblot detection of serum IgD and IgM in differently aged cows. 1, 60 days old; 2, 180 days; 3, 1 year; 4, 2 years; 5, 3 years; 6, 4 years; 7, 5 years; 8, 6 years. The arrows indicate the IgD heavy chain.

    Techniques Used: Western Blot

    n acetylgalactosaminidase  (New England Biolabs)


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    New England Biolabs n acetylgalactosaminidase
    N Acetylgalactosaminidase, 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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    endo a n acetylgalactosaminidase p0733  (New England Biolabs)


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    New England Biolabs endo a n acetylgalactosaminidase p0733
    Endo A N Acetylgalactosaminidase P0733, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    α n acetylgalactosaminidase  (New England Biolabs)


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    New England Biolabs α n acetylgalactosaminidase
    Glycosylation is critical to maintaining the aqueous solubility of Mg7a (A) Enzymatic deglycosylation of Mg7a. Time-course of deglycosylation of Mg7a, as measured by relative ion count of glycoforms at 1, 2 and 4 h of treatment with α- N <t>-acetylgalactosaminidase.</t> At 1 h, only 2% of detected peptide was still fully glycosylated, while 91% was fully deglycosylated and 7% was partially deglycosylated (i.e., Mg7a with the loss of 2 GalNAc moieties). At 2 h, no fully glycosylated peptide was detected, and 94% was fully deglycosylated. (B) Purification of deglyco-Mg7a by HPLC on a Gemini NX-C18 column (250 × 4.6 mm; particle size, 3 μm; pore size, 110 Å; Phenomenex) using a gradient of 5 to 50% solvent B (90% MeCN and 0.05% TFA) over 45 min at a flow rate of 1 mL/min. Mass of eluting peaks was confirmed by MALDI-MS (linear mode). Theoretical monoisotopic [M+1H] 1+ of Mg7a (loss of 2 GalNAc) = m/z 6705; Mg7a (loss of 3 GalNAc) = m/z 6503. Trace from Mg7a (fully glycosylated), run under the same conditions, is shown for comparison. (C) Fibrillar precipitate formed upon reconstitution of deglycosylated Mg7a in water at a concentration of ∼100 μM. Image was acquired on a Nikon DS-Qi2 microscope; scale bar = 100 μm. (D) Activity of Mg7a and analogs on F11 cells. Data are expressed as mean ± SEM ( n = 3).
    α N Acetylgalactosaminidase, 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 "A pain-causing and paralytic ant venom glycopeptide"

    Article Title: A pain-causing and paralytic ant venom glycopeptide

    Journal: iScience

    doi: 10.1016/j.isci.2021.103175

    Glycosylation is critical to maintaining the aqueous solubility of Mg7a (A) Enzymatic deglycosylation of Mg7a. Time-course of deglycosylation of Mg7a, as measured by relative ion count of glycoforms at 1, 2 and 4 h of treatment with α- N -acetylgalactosaminidase. At 1 h, only 2% of detected peptide was still fully glycosylated, while 91% was fully deglycosylated and 7% was partially deglycosylated (i.e., Mg7a with the loss of 2 GalNAc moieties). At 2 h, no fully glycosylated peptide was detected, and 94% was fully deglycosylated. (B) Purification of deglyco-Mg7a by HPLC on a Gemini NX-C18 column (250 × 4.6 mm; particle size, 3 μm; pore size, 110 Å; Phenomenex) using a gradient of 5 to 50% solvent B (90% MeCN and 0.05% TFA) over 45 min at a flow rate of 1 mL/min. Mass of eluting peaks was confirmed by MALDI-MS (linear mode). Theoretical monoisotopic [M+1H] 1+ of Mg7a (loss of 2 GalNAc) = m/z 6705; Mg7a (loss of 3 GalNAc) = m/z 6503. Trace from Mg7a (fully glycosylated), run under the same conditions, is shown for comparison. (C) Fibrillar precipitate formed upon reconstitution of deglycosylated Mg7a in water at a concentration of ∼100 μM. Image was acquired on a Nikon DS-Qi2 microscope; scale bar = 100 μm. (D) Activity of Mg7a and analogs on F11 cells. Data are expressed as mean ± SEM ( n = 3).
    Figure Legend Snippet: Glycosylation is critical to maintaining the aqueous solubility of Mg7a (A) Enzymatic deglycosylation of Mg7a. Time-course of deglycosylation of Mg7a, as measured by relative ion count of glycoforms at 1, 2 and 4 h of treatment with α- N -acetylgalactosaminidase. At 1 h, only 2% of detected peptide was still fully glycosylated, while 91% was fully deglycosylated and 7% was partially deglycosylated (i.e., Mg7a with the loss of 2 GalNAc moieties). At 2 h, no fully glycosylated peptide was detected, and 94% was fully deglycosylated. (B) Purification of deglyco-Mg7a by HPLC on a Gemini NX-C18 column (250 × 4.6 mm; particle size, 3 μm; pore size, 110 Å; Phenomenex) using a gradient of 5 to 50% solvent B (90% MeCN and 0.05% TFA) over 45 min at a flow rate of 1 mL/min. Mass of eluting peaks was confirmed by MALDI-MS (linear mode). Theoretical monoisotopic [M+1H] 1+ of Mg7a (loss of 2 GalNAc) = m/z 6705; Mg7a (loss of 3 GalNAc) = m/z 6503. Trace from Mg7a (fully glycosylated), run under the same conditions, is shown for comparison. (C) Fibrillar precipitate formed upon reconstitution of deglycosylated Mg7a in water at a concentration of ∼100 μM. Image was acquired on a Nikon DS-Qi2 microscope; scale bar = 100 μm. (D) Activity of Mg7a and analogs on F11 cells. Data are expressed as mean ± SEM ( n = 3).

    Techniques Used: Solubility, Purification, Concentration Assay, Microscopy, Activity Assay


    Figure Legend Snippet:

    Techniques Used: Recombinant, Software

    p0734s  (New England Biolabs)


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    New England Biolabs p0734s

    P0734s, 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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    93/100 stars

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    1) Product Images from "A pain-causing and paralytic ant venom glycopeptide"

    Article Title: A pain-causing and paralytic ant venom glycopeptide

    Journal: iScience

    doi: 10.1016/j.isci.2021.103175


    Figure Legend Snippet:

    Techniques Used: Recombinant, Software

    α n acetylgalactosaminidase  (New England Biolabs)


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    New England Biolabs α n acetylgalactosaminidase
    Glycosylation is critical to maintaining the aqueous solubility of Mg7a (A) Enzymatic deglycosylation of Mg7a. Time-course of deglycosylation of Mg7a, as measured by relative ion count of glycoforms at 1, 2 and 4 h of treatment with α- N <t>-acetylgalactosaminidase.</t> At 1 h, only 2% of detected peptide was still fully glycosylated, while 91% was fully deglycosylated and 7% was partially deglycosylated (i.e., Mg7a with the loss of 2 GalNAc moieties). At 2 h, no fully glycosylated peptide was detected, and 94% was fully deglycosylated. (B) Purification of deglyco-Mg7a by HPLC on a Gemini NX-C18 column (250 × 4.6 mm; particle size, 3 μm; pore size, 110 Å; Phenomenex) using a gradient of 5 to 50% solvent B (90% MeCN and 0.05% TFA) over 45 min at a flow rate of 1 mL/min. Mass of eluting peaks was confirmed by MALDI-MS (linear mode). Theoretical monoisotopic [M+1H] 1+ of Mg7a (loss of 2 GalNAc) = m/z 6705; Mg7a (loss of 3 GalNAc) = m/z 6503. Trace from Mg7a (fully glycosylated), run under the same conditions, is shown for comparison. (C) Fibrillar precipitate formed upon reconstitution of deglycosylated Mg7a in water at a concentration of ∼100 μM. Image was acquired on a Nikon DS-Qi2 microscope; scale bar = 100 μm. (D) Activity of Mg7a and analogs on F11 cells. Data are expressed as mean ± SEM ( n = 3).
    α N Acetylgalactosaminidase, 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 "A pain-causing and paralytic ant venom glycopeptide"

    Article Title: A pain-causing and paralytic ant venom glycopeptide

    Journal: iScience

    doi: 10.1016/j.isci.2021.103175

    Glycosylation is critical to maintaining the aqueous solubility of Mg7a (A) Enzymatic deglycosylation of Mg7a. Time-course of deglycosylation of Mg7a, as measured by relative ion count of glycoforms at 1, 2 and 4 h of treatment with α- N -acetylgalactosaminidase. At 1 h, only 2% of detected peptide was still fully glycosylated, while 91% was fully deglycosylated and 7% was partially deglycosylated (i.e., Mg7a with the loss of 2 GalNAc moieties). At 2 h, no fully glycosylated peptide was detected, and 94% was fully deglycosylated. (B) Purification of deglyco-Mg7a by HPLC on a Gemini NX-C18 column (250 × 4.6 mm; particle size, 3 μm; pore size, 110 Å; Phenomenex) using a gradient of 5 to 50% solvent B (90% MeCN and 0.05% TFA) over 45 min at a flow rate of 1 mL/min. Mass of eluting peaks was confirmed by MALDI-MS (linear mode). Theoretical monoisotopic [M+1H] 1+ of Mg7a (loss of 2 GalNAc) = m/z 6705; Mg7a (loss of 3 GalNAc) = m/z 6503. Trace from Mg7a (fully glycosylated), run under the same conditions, is shown for comparison. (C) Fibrillar precipitate formed upon reconstitution of deglycosylated Mg7a in water at a concentration of ∼100 μM. Image was acquired on a Nikon DS-Qi2 microscope; scale bar = 100 μm. (D) Activity of Mg7a and analogs on F11 cells. Data are expressed as mean ± SEM ( n = 3).
    Figure Legend Snippet: Glycosylation is critical to maintaining the aqueous solubility of Mg7a (A) Enzymatic deglycosylation of Mg7a. Time-course of deglycosylation of Mg7a, as measured by relative ion count of glycoforms at 1, 2 and 4 h of treatment with α- N -acetylgalactosaminidase. At 1 h, only 2% of detected peptide was still fully glycosylated, while 91% was fully deglycosylated and 7% was partially deglycosylated (i.e., Mg7a with the loss of 2 GalNAc moieties). At 2 h, no fully glycosylated peptide was detected, and 94% was fully deglycosylated. (B) Purification of deglyco-Mg7a by HPLC on a Gemini NX-C18 column (250 × 4.6 mm; particle size, 3 μm; pore size, 110 Å; Phenomenex) using a gradient of 5 to 50% solvent B (90% MeCN and 0.05% TFA) over 45 min at a flow rate of 1 mL/min. Mass of eluting peaks was confirmed by MALDI-MS (linear mode). Theoretical monoisotopic [M+1H] 1+ of Mg7a (loss of 2 GalNAc) = m/z 6705; Mg7a (loss of 3 GalNAc) = m/z 6503. Trace from Mg7a (fully glycosylated), run under the same conditions, is shown for comparison. (C) Fibrillar precipitate formed upon reconstitution of deglycosylated Mg7a in water at a concentration of ∼100 μM. Image was acquired on a Nikon DS-Qi2 microscope; scale bar = 100 μm. (D) Activity of Mg7a and analogs on F11 cells. Data are expressed as mean ± SEM ( n = 3).

    Techniques Used: Solubility, Purification, Concentration Assay, Microscopy, Activity Assay


    Figure Legend Snippet:

    Techniques Used: Recombinant, Software

    α n acetylgalactosaminidase  (New England Biolabs)


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    New England Biolabs α n acetylgalactosaminidase
    Glycosylation is critical to maintaining the aqueous solubility of Mg7a (A) Enzymatic deglycosylation of Mg7a. Time-course of deglycosylation of Mg7a, as measured by relative ion count of glycoforms at 1, 2 and 4 h of treatment with α- N <t>-acetylgalactosaminidase.</t> At 1 h, only 2% of detected peptide was still fully glycosylated, while 91% was fully deglycosylated and 7% was partially deglycosylated (i.e., Mg7a with the loss of 2 GalNAc moieties). At 2 h, no fully glycosylated peptide was detected, and 94% was fully deglycosylated. (B) Purification of deglyco-Mg7a by HPLC on a Gemini NX-C18 column (250 × 4.6 mm; particle size, 3 μm; pore size, 110 Å; Phenomenex) using a gradient of 5 to 50% solvent B (90% MeCN and 0.05% TFA) over 45 min at a flow rate of 1 mL/min. Mass of eluting peaks was confirmed by MALDI-MS (linear mode). Theoretical monoisotopic [M+1H] 1+ of Mg7a (loss of 2 GalNAc) = m/z 6705; Mg7a (loss of 3 GalNAc) = m/z 6503. Trace from Mg7a (fully glycosylated), run under the same conditions, is shown for comparison. (C) Fibrillar precipitate formed upon reconstitution of deglycosylated Mg7a in water at a concentration of ∼100 μM. Image was acquired on a Nikon DS-Qi2 microscope; scale bar = 100 μm. (D) Activity of Mg7a and analogs on F11 cells. Data are expressed as mean ± SEM ( n = 3).
    α N Acetylgalactosaminidase, 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
    https://www.bioz.com/result/α n acetylgalactosaminidase/product/New England Biolabs
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    α n acetylgalactosaminidase - by Bioz Stars, 2023-03
    93/100 stars

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    1) Product Images from "A pain-causing and paralytic ant venom glycopeptide"

    Article Title: A pain-causing and paralytic ant venom glycopeptide

    Journal: iScience

    doi: 10.1016/j.isci.2021.103175

    Glycosylation is critical to maintaining the aqueous solubility of Mg7a (A) Enzymatic deglycosylation of Mg7a. Time-course of deglycosylation of Mg7a, as measured by relative ion count of glycoforms at 1, 2 and 4 h of treatment with α- N -acetylgalactosaminidase. At 1 h, only 2% of detected peptide was still fully glycosylated, while 91% was fully deglycosylated and 7% was partially deglycosylated (i.e., Mg7a with the loss of 2 GalNAc moieties). At 2 h, no fully glycosylated peptide was detected, and 94% was fully deglycosylated. (B) Purification of deglyco-Mg7a by HPLC on a Gemini NX-C18 column (250 × 4.6 mm; particle size, 3 μm; pore size, 110 Å; Phenomenex) using a gradient of 5 to 50% solvent B (90% MeCN and 0.05% TFA) over 45 min at a flow rate of 1 mL/min. Mass of eluting peaks was confirmed by MALDI-MS (linear mode). Theoretical monoisotopic [M+1H] 1+ of Mg7a (loss of 2 GalNAc) = m/z 6705; Mg7a (loss of 3 GalNAc) = m/z 6503. Trace from Mg7a (fully glycosylated), run under the same conditions, is shown for comparison. (C) Fibrillar precipitate formed upon reconstitution of deglycosylated Mg7a in water at a concentration of ∼100 μM. Image was acquired on a Nikon DS-Qi2 microscope; scale bar = 100 μm. (D) Activity of Mg7a and analogs on F11 cells. Data are expressed as mean ± SEM ( n = 3).
    Figure Legend Snippet: Glycosylation is critical to maintaining the aqueous solubility of Mg7a (A) Enzymatic deglycosylation of Mg7a. Time-course of deglycosylation of Mg7a, as measured by relative ion count of glycoforms at 1, 2 and 4 h of treatment with α- N -acetylgalactosaminidase. At 1 h, only 2% of detected peptide was still fully glycosylated, while 91% was fully deglycosylated and 7% was partially deglycosylated (i.e., Mg7a with the loss of 2 GalNAc moieties). At 2 h, no fully glycosylated peptide was detected, and 94% was fully deglycosylated. (B) Purification of deglyco-Mg7a by HPLC on a Gemini NX-C18 column (250 × 4.6 mm; particle size, 3 μm; pore size, 110 Å; Phenomenex) using a gradient of 5 to 50% solvent B (90% MeCN and 0.05% TFA) over 45 min at a flow rate of 1 mL/min. Mass of eluting peaks was confirmed by MALDI-MS (linear mode). Theoretical monoisotopic [M+1H] 1+ of Mg7a (loss of 2 GalNAc) = m/z 6705; Mg7a (loss of 3 GalNAc) = m/z 6503. Trace from Mg7a (fully glycosylated), run under the same conditions, is shown for comparison. (C) Fibrillar precipitate formed upon reconstitution of deglycosylated Mg7a in water at a concentration of ∼100 μM. Image was acquired on a Nikon DS-Qi2 microscope; scale bar = 100 μm. (D) Activity of Mg7a and analogs on F11 cells. Data are expressed as mean ± SEM ( n = 3).

    Techniques Used: Solubility, Purification, Concentration Assay, Microscopy, Activity Assay


    Figure Legend Snippet:

    Techniques Used: Recombinant, Software

    endo α n acetylgalactosaminidase o glycosidase  (New England Biolabs)


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    New England Biolabs endo α n acetylgalactosaminidase o glycosidase
    Endo α N Acetylgalactosaminidase O Glycosidase, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    New England Biolabs n acetylgalactosaminidase
    N Acetylgalactosaminidase, 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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    α n acetylgalactosaminidase  (New England Biolabs)
    93
    New England Biolabs α n acetylgalactosaminidase
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    Image Search Results


    Journal: iScience

    Article Title: A pain-causing and paralytic ant venom glycopeptide

    doi: 10.1016/j.isci.2021.103175

    Figure Lengend Snippet:

    Article Snippet: α-N-acetylgalactosaminidase , New England BioLabs , P0734S.

    Techniques: Recombinant, Software