n glycoprotein bovine pancreatic ribonuclease b  (New England Biolabs)


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    New England Biolabs n glycoprotein bovine pancreatic ribonuclease b
    The enzymatic activity of recombinant NGLY1. Each experiment was done once (n = 1). (A-1) SDS-PAGE analysis of RNase B treated with NGLY1. (A-2) SDS-PAGE analysis of OVA treated with NGLY1. (A-3) SDS-PAGE analysis of IgG treated with NGLY1. The schematic diagram of RNase B, OVA, and IgG is shown [ , , ]. RNase B: ribonuclease B; OVA: ovalbumin; IgG: immunoglobulin G; CHO: carbon hydrogen oligosaccharide; +CHO: glycosylated forms of the substrates; –CHO: deglycosylated forms of the substrates. (B-1) The enzymatic reaction temperature of NGLY1. (B-2) Enzymatic reaction pH of NGLY1. NA: substrate control, without treatment; “-”: without NGLY1. (C) The released N-glycans from RNase B were detected by MALDI-TOF MS. (D) The released N-glycans from RNase B were detected by CE . (E) The released N-glycans from total serum <t>glycoproteins</t> of healthy individuals were detected by CE. Structure formulas: blue square, N-acetylglucosamine; green circle, mannose; yellow circle, galactose; red triangle, fucose.
    N Glycoprotein Bovine Pancreatic Ribonuclease B, 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 "Functional prediction of the potential NGLY1 mutations associated with rare disease CDG"

    Article Title: Functional prediction of the potential NGLY1 mutations associated with rare disease CDG

    Journal: Heliyon

    doi: 10.1016/j.heliyon.2024.e28787

    The enzymatic activity of recombinant NGLY1. Each experiment was done once (n = 1). (A-1) SDS-PAGE analysis of RNase B treated with NGLY1. (A-2) SDS-PAGE analysis of OVA treated with NGLY1. (A-3) SDS-PAGE analysis of IgG treated with NGLY1. The schematic diagram of RNase B, OVA, and IgG is shown [ , , ]. RNase B: ribonuclease B; OVA: ovalbumin; IgG: immunoglobulin G; CHO: carbon hydrogen oligosaccharide; +CHO: glycosylated forms of the substrates; –CHO: deglycosylated forms of the substrates. (B-1) The enzymatic reaction temperature of NGLY1. (B-2) Enzymatic reaction pH of NGLY1. NA: substrate control, without treatment; “-”: without NGLY1. (C) The released N-glycans from RNase B were detected by MALDI-TOF MS. (D) The released N-glycans from RNase B were detected by CE . (E) The released N-glycans from total serum glycoproteins of healthy individuals were detected by CE. Structure formulas: blue square, N-acetylglucosamine; green circle, mannose; yellow circle, galactose; red triangle, fucose.
    Figure Legend Snippet: The enzymatic activity of recombinant NGLY1. Each experiment was done once (n = 1). (A-1) SDS-PAGE analysis of RNase B treated with NGLY1. (A-2) SDS-PAGE analysis of OVA treated with NGLY1. (A-3) SDS-PAGE analysis of IgG treated with NGLY1. The schematic diagram of RNase B, OVA, and IgG is shown [ , , ]. RNase B: ribonuclease B; OVA: ovalbumin; IgG: immunoglobulin G; CHO: carbon hydrogen oligosaccharide; +CHO: glycosylated forms of the substrates; –CHO: deglycosylated forms of the substrates. (B-1) The enzymatic reaction temperature of NGLY1. (B-2) Enzymatic reaction pH of NGLY1. NA: substrate control, without treatment; “-”: without NGLY1. (C) The released N-glycans from RNase B were detected by MALDI-TOF MS. (D) The released N-glycans from RNase B were detected by CE . (E) The released N-glycans from total serum glycoproteins of healthy individuals were detected by CE. Structure formulas: blue square, N-acetylglucosamine; green circle, mannose; yellow circle, galactose; red triangle, fucose.

    Techniques Used: Activity Assay, Recombinant, SDS Page

    n glycoprotein bovine pancreatic ribonuclease b  (New England Biolabs)


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    New England Biolabs n glycoprotein bovine pancreatic ribonuclease b
    The enzymatic activity of recombinant NGLY1. Each experiment was done once (n = 1). (A-1) SDS-PAGE analysis of RNase B treated with NGLY1. (A-2) SDS-PAGE analysis of OVA treated with NGLY1. (A-3) SDS-PAGE analysis of IgG treated with NGLY1. The schematic diagram of RNase B, OVA, and IgG is shown [ , , ]. RNase B: ribonuclease B; OVA: ovalbumin; IgG: immunoglobulin G; CHO: carbon hydrogen oligosaccharide; +CHO: glycosylated forms of the substrates; –CHO: deglycosylated forms of the substrates. (B-1) The enzymatic reaction temperature of NGLY1. (B-2) Enzymatic reaction pH of NGLY1. NA: substrate control, without treatment; “-”: without NGLY1. (C) The released N-glycans from RNase B were detected by MALDI-TOF MS. (D) The released N-glycans from RNase B were detected by CE . (E) The released N-glycans from total serum <t>glycoproteins</t> of healthy individuals were detected by CE. Structure formulas: blue square, N-acetylglucosamine; green circle, mannose; yellow circle, galactose; red triangle, fucose.
    N Glycoprotein Bovine Pancreatic Ribonuclease B, 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 "Functional prediction of the potential NGLY1 mutations associated with rare disease CDG"

    Article Title: Functional prediction of the potential NGLY1 mutations associated with rare disease CDG

    Journal: Heliyon

    doi: 10.1016/j.heliyon.2024.e28787

    The enzymatic activity of recombinant NGLY1. Each experiment was done once (n = 1). (A-1) SDS-PAGE analysis of RNase B treated with NGLY1. (A-2) SDS-PAGE analysis of OVA treated with NGLY1. (A-3) SDS-PAGE analysis of IgG treated with NGLY1. The schematic diagram of RNase B, OVA, and IgG is shown [ , , ]. RNase B: ribonuclease B; OVA: ovalbumin; IgG: immunoglobulin G; CHO: carbon hydrogen oligosaccharide; +CHO: glycosylated forms of the substrates; –CHO: deglycosylated forms of the substrates. (B-1) The enzymatic reaction temperature of NGLY1. (B-2) Enzymatic reaction pH of NGLY1. NA: substrate control, without treatment; “-”: without NGLY1. (C) The released N-glycans from RNase B were detected by MALDI-TOF MS. (D) The released N-glycans from RNase B were detected by CE . (E) The released N-glycans from total serum glycoproteins of healthy individuals were detected by CE. Structure formulas: blue square, N-acetylglucosamine; green circle, mannose; yellow circle, galactose; red triangle, fucose.
    Figure Legend Snippet: The enzymatic activity of recombinant NGLY1. Each experiment was done once (n = 1). (A-1) SDS-PAGE analysis of RNase B treated with NGLY1. (A-2) SDS-PAGE analysis of OVA treated with NGLY1. (A-3) SDS-PAGE analysis of IgG treated with NGLY1. The schematic diagram of RNase B, OVA, and IgG is shown [ , , ]. RNase B: ribonuclease B; OVA: ovalbumin; IgG: immunoglobulin G; CHO: carbon hydrogen oligosaccharide; +CHO: glycosylated forms of the substrates; –CHO: deglycosylated forms of the substrates. (B-1) The enzymatic reaction temperature of NGLY1. (B-2) Enzymatic reaction pH of NGLY1. NA: substrate control, without treatment; “-”: without NGLY1. (C) The released N-glycans from RNase B were detected by MALDI-TOF MS. (D) The released N-glycans from RNase B were detected by CE . (E) The released N-glycans from total serum glycoproteins of healthy individuals were detected by CE. Structure formulas: blue square, N-acetylglucosamine; green circle, mannose; yellow circle, galactose; red triangle, fucose.

    Techniques Used: Activity Assay, Recombinant, SDS Page


    Structured Review

    Millipore bovine pancreas rnase b
    Bovine Pancreas Rnase B, supplied by Millipore, 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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    n glycoprotein bovine pancreatic ribonuclease b  (New England Biolabs)


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    New England Biolabs n glycoprotein bovine pancreatic ribonuclease b
    The glycosidase activity analysis of NGLY1. (A) The released N-glycans from <t>RNase</t> <t>B</t> were detected by MALDI-TOF MS. Upper right image: SDS-PAGE analysis of RNase B treated with NGLY1. Comparison of the deglycosylation activities of NGLY1 and PNGase F (glycosylated and deglycosylated forms of the substrates are indicated by +CHO and -CHO, respectively). Lane 1: RNase B, Lane 2: NGLY1 + RNase B; Lane 3: PNGase F + RNase B. (B) The released N-glycans from RNase B detected by CE. (C) The released N-glycans from total serum glycoproteins of healthy individuals detected by CE.
    N Glycoprotein Bovine Pancreatic Ribonuclease B, 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 full spectrum PNGase activity analysis of R328 mutations on NGLY1"

    Article Title: A full spectrum PNGase activity analysis of R328 mutations on NGLY1

    Journal: bioRxiv

    doi: 10.1101/2022.04.07.487431

    The glycosidase activity analysis of NGLY1. (A) The released N-glycans from RNase B were detected by MALDI-TOF MS. Upper right image: SDS-PAGE analysis of RNase B treated with NGLY1. Comparison of the deglycosylation activities of NGLY1 and PNGase F (glycosylated and deglycosylated forms of the substrates are indicated by +CHO and -CHO, respectively). Lane 1: RNase B, Lane 2: NGLY1 + RNase B; Lane 3: PNGase F + RNase B. (B) The released N-glycans from RNase B detected by CE. (C) The released N-glycans from total serum glycoproteins of healthy individuals detected by CE.
    Figure Legend Snippet: The glycosidase activity analysis of NGLY1. (A) The released N-glycans from RNase B were detected by MALDI-TOF MS. Upper right image: SDS-PAGE analysis of RNase B treated with NGLY1. Comparison of the deglycosylation activities of NGLY1 and PNGase F (glycosylated and deglycosylated forms of the substrates are indicated by +CHO and -CHO, respectively). Lane 1: RNase B, Lane 2: NGLY1 + RNase B; Lane 3: PNGase F + RNase B. (B) The released N-glycans from RNase B detected by CE. (C) The released N-glycans from total serum glycoproteins of healthy individuals detected by CE.

    Techniques Used: Activity Assay, SDS Page

    The effect of reaction conditions on NGLY1. (A-1) SDS-PAGE analysis of RNase B treated with NGLY1. (A-2) SDS-PAGE analysis of OVA treated with NGLY1. (A-3) SDS-PAGE analysis of IgG treated with NGLY1. The schematic diagram of RNase B, OVA, and IgG is shown ( ; ; ). Structure formulas: blue square, N-acetylglucosamine; green circle, mannose; yellow circle, galactose; red triangle, fucose. (B) The enzymatic reaction temperature of NGLY1. NGLY1 and RNase B were mixed and incubated for 12 h at different temperatures. (C) Enzymatic reaction pH of NGLY1. NGLY1 and RNase B were mixed, incubated for 12 h at different pH. NA: substrate control, without treatment; “-”: without NGLY1.
    Figure Legend Snippet: The effect of reaction conditions on NGLY1. (A-1) SDS-PAGE analysis of RNase B treated with NGLY1. (A-2) SDS-PAGE analysis of OVA treated with NGLY1. (A-3) SDS-PAGE analysis of IgG treated with NGLY1. The schematic diagram of RNase B, OVA, and IgG is shown ( ; ; ). Structure formulas: blue square, N-acetylglucosamine; green circle, mannose; yellow circle, galactose; red triangle, fucose. (B) The enzymatic reaction temperature of NGLY1. NGLY1 and RNase B were mixed and incubated for 12 h at different temperatures. (C) Enzymatic reaction pH of NGLY1. NGLY1 and RNase B were mixed, incubated for 12 h at different pH. NA: substrate control, without treatment; “-”: without NGLY1.

    Techniques Used: SDS Page, Incubation

    SDS-PAGE analysis of RNase B treated with NGLY1-R328 mutations, and the simulated structures of wild-type and mutated NGLY1 predicted by AlphaFold2. (A) The construction of the R328 site in NGLY1. (B) The enzymatic activity of mutations on the R328 site of NGLY1. (C) The interaction of the R328 site to other amino acids (E340 and E440). (D) The predicted structures of mutated NGLY1 (with enzymatic activity).A: alanine; C: cysteine; D: aspartic acid; E: glutamic acid; F: phenylalanine; G: glycine; H: histidine; I: isoleucine; K: lysine; L: leucine; M: methionine; N: asparagine; P: proline; Q: glutamine; R: arginine; S: serine; T: threonine; V: valine; W: tryptophan; Y: tyrosine.
    Figure Legend Snippet: SDS-PAGE analysis of RNase B treated with NGLY1-R328 mutations, and the simulated structures of wild-type and mutated NGLY1 predicted by AlphaFold2. (A) The construction of the R328 site in NGLY1. (B) The enzymatic activity of mutations on the R328 site of NGLY1. (C) The interaction of the R328 site to other amino acids (E340 and E440). (D) The predicted structures of mutated NGLY1 (with enzymatic activity).A: alanine; C: cysteine; D: aspartic acid; E: glutamic acid; F: phenylalanine; G: glycine; H: histidine; I: isoleucine; K: lysine; L: leucine; M: methionine; N: asparagine; P: proline; Q: glutamine; R: arginine; S: serine; T: threonine; V: valine; W: tryptophan; Y: tyrosine.

    Techniques Used: SDS Page, Activity Assay

    bovine rnase b  (New England Biolabs)


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    New England Biolabs bovine rnase b
    Bovine Rnase B, 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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    bovine rnase b  (New England Biolabs)


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    New England Biolabs bovine rnase b
    Experimental conditions for optimal limited deglycosylation of bovine <t>RNase</t> <t>B</t> and fetuin by PNGase F were determined. The optimal A ) NP-40 concentration, B ) temperature, C ) and D ) PNGase F:glycoprotein ratio for RNase B and fetuin, respectively, and, E ) and F ) the optimal time for the deglycosylation of RNase B and fetuin, respectively, were assayed by differential migration of the glycoproteins in 15% SDS-PAGE. Fully deglycosylated (+) and fully glycosylated (−) proteins were included for each optimization reaction, denoted by FD and FG, respectively.
    Bovine Rnase B, 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 "Systems-wide analysis of glycoprotein conformational changes by limited deglycosylation assay"

    Article Title: Systems-wide analysis of glycoprotein conformational changes by limited deglycosylation assay

    Journal: bioRxiv

    doi: 10.1101/2021.06.04.447131

    Experimental conditions for optimal limited deglycosylation of bovine RNase B and fetuin by PNGase F were determined. The optimal A ) NP-40 concentration, B ) temperature, C ) and D ) PNGase F:glycoprotein ratio for RNase B and fetuin, respectively, and, E ) and F ) the optimal time for the deglycosylation of RNase B and fetuin, respectively, were assayed by differential migration of the glycoproteins in 15% SDS-PAGE. Fully deglycosylated (+) and fully glycosylated (−) proteins were included for each optimization reaction, denoted by FD and FG, respectively.
    Figure Legend Snippet: Experimental conditions for optimal limited deglycosylation of bovine RNase B and fetuin by PNGase F were determined. The optimal A ) NP-40 concentration, B ) temperature, C ) and D ) PNGase F:glycoprotein ratio for RNase B and fetuin, respectively, and, E ) and F ) the optimal time for the deglycosylation of RNase B and fetuin, respectively, were assayed by differential migration of the glycoproteins in 15% SDS-PAGE. Fully deglycosylated (+) and fully glycosylated (−) proteins were included for each optimization reaction, denoted by FD and FG, respectively.

    Techniques Used: Concentration Assay, Migration, SDS Page


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    Millipore bovine pancreas rnase b
    Bovine Pancreas Rnase B, supplied by Millipore, 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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    Millipore bovine ribonuclease rnase b
    Bovine Ribonuclease Rnase B, supplied by Millipore, 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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    FUJIFILM bovine ribonuclease rnase b
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    Millipore bovine ribonuclease rnase b
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    New England Biolabs n glycoprotein bovine pancreatic ribonuclease b
    The enzymatic activity of recombinant NGLY1. Each experiment was done once (n = 1). (A-1) SDS-PAGE analysis of RNase B treated with NGLY1. (A-2) SDS-PAGE analysis of OVA treated with NGLY1. (A-3) SDS-PAGE analysis of IgG treated with NGLY1. The schematic diagram of RNase B, OVA, and IgG is shown [ , , ]. RNase B: ribonuclease B; OVA: ovalbumin; IgG: immunoglobulin G; CHO: carbon hydrogen oligosaccharide; +CHO: glycosylated forms of the substrates; –CHO: deglycosylated forms of the substrates. (B-1) The enzymatic reaction temperature of NGLY1. (B-2) Enzymatic reaction pH of NGLY1. NA: substrate control, without treatment; “-”: without NGLY1. (C) The released N-glycans from RNase B were detected by MALDI-TOF MS. (D) The released N-glycans from RNase B were detected by CE . (E) The released N-glycans from total serum <t>glycoproteins</t> of healthy individuals were detected by CE. Structure formulas: blue square, N-acetylglucosamine; green circle, mannose; yellow circle, galactose; red triangle, fucose.
    N Glycoprotein Bovine Pancreatic Ribonuclease B, 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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    The enzymatic activity of recombinant NGLY1. Each experiment was done once (n = 1). (A-1) SDS-PAGE analysis of RNase B treated with NGLY1. (A-2) SDS-PAGE analysis of OVA treated with NGLY1. (A-3) SDS-PAGE analysis of IgG treated with NGLY1. The schematic diagram of RNase B, OVA, and IgG is shown [ , , ]. RNase B: ribonuclease B; OVA: ovalbumin; IgG: immunoglobulin G; CHO: carbon hydrogen oligosaccharide; +CHO: glycosylated forms of the substrates; –CHO: deglycosylated forms of the substrates. (B-1) The enzymatic reaction temperature of NGLY1. (B-2) Enzymatic reaction pH of NGLY1. NA: substrate control, without treatment; “-”: without NGLY1. (C) The released N-glycans from RNase B were detected by MALDI-TOF MS. (D) The released N-glycans from RNase B were detected by CE . (E) The released N-glycans from total serum <t>glycoproteins</t> of healthy individuals were detected by CE. Structure formulas: blue square, N-acetylglucosamine; green circle, mannose; yellow circle, galactose; red triangle, fucose.
    Bovine Pancreas Rnase B, supplied by Millipore, 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 bovine rnase b
    The enzymatic activity of recombinant NGLY1. Each experiment was done once (n = 1). (A-1) SDS-PAGE analysis of RNase B treated with NGLY1. (A-2) SDS-PAGE analysis of OVA treated with NGLY1. (A-3) SDS-PAGE analysis of IgG treated with NGLY1. The schematic diagram of RNase B, OVA, and IgG is shown [ , , ]. RNase B: ribonuclease B; OVA: ovalbumin; IgG: immunoglobulin G; CHO: carbon hydrogen oligosaccharide; +CHO: glycosylated forms of the substrates; –CHO: deglycosylated forms of the substrates. (B-1) The enzymatic reaction temperature of NGLY1. (B-2) Enzymatic reaction pH of NGLY1. NA: substrate control, without treatment; “-”: without NGLY1. (C) The released N-glycans from RNase B were detected by MALDI-TOF MS. (D) The released N-glycans from RNase B were detected by CE . (E) The released N-glycans from total serum <t>glycoproteins</t> of healthy individuals were detected by CE. Structure formulas: blue square, N-acetylglucosamine; green circle, mannose; yellow circle, galactose; red triangle, fucose.
    Bovine Rnase B, 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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    The enzymatic activity of recombinant NGLY1. Each experiment was done once (n = 1). (A-1) SDS-PAGE analysis of RNase B treated with NGLY1. (A-2) SDS-PAGE analysis of OVA treated with NGLY1. (A-3) SDS-PAGE analysis of IgG treated with NGLY1. The schematic diagram of RNase B, OVA, and IgG is shown [ , , ]. RNase B: ribonuclease B; OVA: ovalbumin; IgG: immunoglobulin G; CHO: carbon hydrogen oligosaccharide; +CHO: glycosylated forms of the substrates; –CHO: deglycosylated forms of the substrates. (B-1) The enzymatic reaction temperature of NGLY1. (B-2) Enzymatic reaction pH of NGLY1. NA: substrate control, without treatment; “-”: without NGLY1. (C) The released N-glycans from RNase B were detected by MALDI-TOF MS. (D) The released N-glycans from RNase B were detected by CE . (E) The released N-glycans from total serum <t>glycoproteins</t> of healthy individuals were detected by CE. Structure formulas: blue square, N-acetylglucosamine; green circle, mannose; yellow circle, galactose; red triangle, fucose.
    Bovine Rnase B, supplied by Millipore, 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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    86
    Millipore bovine ribonuclease rnase b
    The enzymatic activity of recombinant NGLY1. Each experiment was done once (n = 1). (A-1) SDS-PAGE analysis of RNase B treated with NGLY1. (A-2) SDS-PAGE analysis of OVA treated with NGLY1. (A-3) SDS-PAGE analysis of IgG treated with NGLY1. The schematic diagram of RNase B, OVA, and IgG is shown [ , , ]. RNase B: ribonuclease B; OVA: ovalbumin; IgG: immunoglobulin G; CHO: carbon hydrogen oligosaccharide; +CHO: glycosylated forms of the substrates; –CHO: deglycosylated forms of the substrates. (B-1) The enzymatic reaction temperature of NGLY1. (B-2) Enzymatic reaction pH of NGLY1. NA: substrate control, without treatment; “-”: without NGLY1. (C) The released N-glycans from RNase B were detected by MALDI-TOF MS. (D) The released N-glycans from RNase B were detected by CE . (E) The released N-glycans from total serum <t>glycoproteins</t> of healthy individuals were detected by CE. Structure formulas: blue square, N-acetylglucosamine; green circle, mannose; yellow circle, galactose; red triangle, fucose.
    Bovine Ribonuclease Rnase B, supplied by Millipore, 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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    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    bovine ribonuclease rnase b - by Bioz Stars, 2024-07
    86/100 stars
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    86
    FUJIFILM bovine ribonuclease rnase b
    The enzymatic activity of recombinant NGLY1. Each experiment was done once (n = 1). (A-1) SDS-PAGE analysis of RNase B treated with NGLY1. (A-2) SDS-PAGE analysis of OVA treated with NGLY1. (A-3) SDS-PAGE analysis of IgG treated with NGLY1. The schematic diagram of RNase B, OVA, and IgG is shown [ , , ]. RNase B: ribonuclease B; OVA: ovalbumin; IgG: immunoglobulin G; CHO: carbon hydrogen oligosaccharide; +CHO: glycosylated forms of the substrates; –CHO: deglycosylated forms of the substrates. (B-1) The enzymatic reaction temperature of NGLY1. (B-2) Enzymatic reaction pH of NGLY1. NA: substrate control, without treatment; “-”: without NGLY1. (C) The released N-glycans from RNase B were detected by MALDI-TOF MS. (D) The released N-glycans from RNase B were detected by CE . (E) The released N-glycans from total serum <t>glycoproteins</t> of healthy individuals were detected by CE. Structure formulas: blue square, N-acetylglucosamine; green circle, mannose; yellow circle, galactose; red triangle, fucose.
    Bovine Ribonuclease Rnase B, supplied by FUJIFILM, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/bovine ribonuclease rnase b/product/FUJIFILM
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    bovine ribonuclease rnase b - by Bioz Stars, 2024-07
    86/100 stars
      Buy from Supplier

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    The enzymatic activity of recombinant NGLY1. Each experiment was done once (n = 1). (A-1) SDS-PAGE analysis of RNase B treated with NGLY1. (A-2) SDS-PAGE analysis of OVA treated with NGLY1. (A-3) SDS-PAGE analysis of IgG treated with NGLY1. The schematic diagram of RNase B, OVA, and IgG is shown [ , , ]. RNase B: ribonuclease B; OVA: ovalbumin; IgG: immunoglobulin G; CHO: carbon hydrogen oligosaccharide; +CHO: glycosylated forms of the substrates; –CHO: deglycosylated forms of the substrates. (B-1) The enzymatic reaction temperature of NGLY1. (B-2) Enzymatic reaction pH of NGLY1. NA: substrate control, without treatment; “-”: without NGLY1. (C) The released N-glycans from RNase B were detected by MALDI-TOF MS. (D) The released N-glycans from RNase B were detected by CE . (E) The released N-glycans from total serum glycoproteins of healthy individuals were detected by CE. Structure formulas: blue square, N-acetylglucosamine; green circle, mannose; yellow circle, galactose; red triangle, fucose.

    Journal: Heliyon

    Article Title: Functional prediction of the potential NGLY1 mutations associated with rare disease CDG

    doi: 10.1016/j.heliyon.2024.e28787

    Figure Lengend Snippet: The enzymatic activity of recombinant NGLY1. Each experiment was done once (n = 1). (A-1) SDS-PAGE analysis of RNase B treated with NGLY1. (A-2) SDS-PAGE analysis of OVA treated with NGLY1. (A-3) SDS-PAGE analysis of IgG treated with NGLY1. The schematic diagram of RNase B, OVA, and IgG is shown [ , , ]. RNase B: ribonuclease B; OVA: ovalbumin; IgG: immunoglobulin G; CHO: carbon hydrogen oligosaccharide; +CHO: glycosylated forms of the substrates; –CHO: deglycosylated forms of the substrates. (B-1) The enzymatic reaction temperature of NGLY1. (B-2) Enzymatic reaction pH of NGLY1. NA: substrate control, without treatment; “-”: without NGLY1. (C) The released N-glycans from RNase B were detected by MALDI-TOF MS. (D) The released N-glycans from RNase B were detected by CE . (E) The released N-glycans from total serum glycoproteins of healthy individuals were detected by CE. Structure formulas: blue square, N-acetylglucosamine; green circle, mannose; yellow circle, galactose; red triangle, fucose.

    Article Snippet: The standard N-glycoprotein bovine pancreatic ribonuclease B (RNase B, New England Biolabs, USA) was used as a substrate to measure NGLY1 activity.

    Techniques: Activity Assay, Recombinant, SDS Page