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: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    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: 94/100, 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: 94/100, 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: 94/100, 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


    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: 94/100, 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
    Linkage analysis of the reaction product. ( a ) Linkage-specific N <t>-acetylgalactosaminidase</t> digestion of the reaction product. The reaction product purified by SF-HPLC were digested independently by two N -acetylgalactosaminidases specific for α- and β- linkage. The digested products were separated by SF-HPLC. Numbers at the top represent the elution positions of glucose units. ( b ) Structural representation and fragmentation scheme of GalNAcβ1,4-GlcNAc- p NP. Diagnostic ions are represented in gray characters. ( c ) Negative ion MS/MS fragmentation spectra of N -acetylgalactosaminylated GlcNAc- p NP. The corresponding m/z values of the CID-derived fragment ions and their nomenclatures are assigned in the spectra. The small window shows the enlarged fragment ions in the mass range m/z 200–500. m/z values shown in black and gray indicate 1,4-linked specific and GalNAcβ-GlcNAc- p NP signals, respectively.
    α N Acetylgalactosaminidase, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Bombyx mori β1,4- N -acetylgalactosaminyltransferase possesses relaxed donor substrate specificity in N -glycan synthesis"

    Article Title: Bombyx mori β1,4- N -acetylgalactosaminyltransferase possesses relaxed donor substrate specificity in N -glycan synthesis

    Journal: Scientific Reports

    doi: 10.1038/s41598-021-84771-z

    Linkage analysis of the reaction product. ( a ) Linkage-specific N -acetylgalactosaminidase digestion of the reaction product. The reaction product purified by SF-HPLC were digested independently by two N -acetylgalactosaminidases specific for α- and β- linkage. The digested products were separated by SF-HPLC. Numbers at the top represent the elution positions of glucose units. ( b ) Structural representation and fragmentation scheme of GalNAcβ1,4-GlcNAc- p NP. Diagnostic ions are represented in gray characters. ( c ) Negative ion MS/MS fragmentation spectra of N -acetylgalactosaminylated GlcNAc- p NP. The corresponding m/z values of the CID-derived fragment ions and their nomenclatures are assigned in the spectra. The small window shows the enlarged fragment ions in the mass range m/z 200–500. m/z values shown in black and gray indicate 1,4-linked specific and GalNAcβ-GlcNAc- p NP signals, respectively.
    Figure Legend Snippet: Linkage analysis of the reaction product. ( a ) Linkage-specific N -acetylgalactosaminidase digestion of the reaction product. The reaction product purified by SF-HPLC were digested independently by two N -acetylgalactosaminidases specific for α- and β- linkage. The digested products were separated by SF-HPLC. Numbers at the top represent the elution positions of glucose units. ( b ) Structural representation and fragmentation scheme of GalNAcβ1,4-GlcNAc- p NP. Diagnostic ions are represented in gray characters. ( c ) Negative ion MS/MS fragmentation spectra of N -acetylgalactosaminylated GlcNAc- p NP. The corresponding m/z values of the CID-derived fragment ions and their nomenclatures are assigned in the spectra. The small window shows the enlarged fragment ions in the mass range m/z 200–500. m/z values shown in black and gray indicate 1,4-linked specific and GalNAcβ-GlcNAc- p NP signals, respectively.

    Techniques Used: Purification, Diagnostic Assay, Tandem Mass Spectroscopy, Derivative Assay

    a n acetylgalactosaminidase  (New England Biolabs)


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    New England Biolabs a n acetylgalactosaminidase
    A N Acetylgalactosaminidase, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    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: 94/100, 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: 94/100, 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: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    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: 94/100, 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: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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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: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    New England Biolabs p0734s

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    New England Biolabs a n acetylgalactosaminidase

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    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).

    Journal: iScience

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

    doi: 10.1016/j.isci.2021.103175

    Figure Lengend 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).

    Article Snippet: To overcome this challenge, we enzymatically deglycosylated the full-length synthetic Mg7a 1 using α- N -acetylgalactosaminidase (New England BioLabs) ( A and 3B).

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

    Journal: iScience

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

    doi: 10.1016/j.isci.2021.103175

    Figure Lengend Snippet:

    Article Snippet: To overcome this challenge, we enzymatically deglycosylated the full-length synthetic Mg7a 1 using α- N -acetylgalactosaminidase (New England BioLabs) ( A and 3B).

    Techniques: Recombinant, Software

    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