fetuin  (New England Biolabs)


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    New England Biolabs fetuin
    Characterization of wild-type and D614G S glycoproteins in GALE/GALK2 293T cells. (A) The wild-type SARS-CoV-2 S glycoprotein (D614, with an aspartic acid residue at 614) and the D614G variant (G614, with a glycine residue at 614) were expressed in wild-type 293T cells (wt) or in GALE/GALK2 293T cells (ko) . Cell lysates were untreated (No Rx) or were treated with the <t>indicated</t> <t>glycosidase(s),</t> followed by Western blotting with a mouse antibody against S1 (upper) or a rabbit antibody against S2 (lower). The S glycoproteins, either untreated or treated with different glycosidases, are indicated by red arrows. (B) As a control, <t>fetuin,</t> which has N- and O-linked glycans, was treated with the indicated glycosidases. The SDS-polyacrylamide gel was stained with Coomassie blue. The different fetuin glycoforms are indicated by red arrows. The results shown are typical of those obtained in two independent experiments.
    Fetuin, 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/fetuin/product/New England Biolabs
    Average 93 stars, based on 1 article reviews
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    fetuin - by Bioz Stars, 2023-02
    93/100 stars

    Images

    1) Product Images from "Analysis of Glycosylation and Disulfide Bonding of Wild-Type SARS-CoV-2 Spike Glycoprotein"

    Article Title: Analysis of Glycosylation and Disulfide Bonding of Wild-Type SARS-CoV-2 Spike Glycoprotein

    Journal: Journal of Virology

    doi: 10.1128/jvi.01626-21

    Characterization of wild-type and D614G S glycoproteins in GALE/GALK2 293T cells. (A) The wild-type SARS-CoV-2 S glycoprotein (D614, with an aspartic acid residue at 614) and the D614G variant (G614, with a glycine residue at 614) were expressed in wild-type 293T cells (wt) or in GALE/GALK2 293T cells (ko) . Cell lysates were untreated (No Rx) or were treated with the indicated glycosidase(s), followed by Western blotting with a mouse antibody against S1 (upper) or a rabbit antibody against S2 (lower). The S glycoproteins, either untreated or treated with different glycosidases, are indicated by red arrows. (B) As a control, fetuin, which has N- and O-linked glycans, was treated with the indicated glycosidases. The SDS-polyacrylamide gel was stained with Coomassie blue. The different fetuin glycoforms are indicated by red arrows. The results shown are typical of those obtained in two independent experiments.
    Figure Legend Snippet: Characterization of wild-type and D614G S glycoproteins in GALE/GALK2 293T cells. (A) The wild-type SARS-CoV-2 S glycoprotein (D614, with an aspartic acid residue at 614) and the D614G variant (G614, with a glycine residue at 614) were expressed in wild-type 293T cells (wt) or in GALE/GALK2 293T cells (ko) . Cell lysates were untreated (No Rx) or were treated with the indicated glycosidase(s), followed by Western blotting with a mouse antibody against S1 (upper) or a rabbit antibody against S2 (lower). The S glycoproteins, either untreated or treated with different glycosidases, are indicated by red arrows. (B) As a control, fetuin, which has N- and O-linked glycans, was treated with the indicated glycosidases. The SDS-polyacrylamide gel was stained with Coomassie blue. The different fetuin glycoforms are indicated by red arrows. The results shown are typical of those obtained in two independent experiments.

    Techniques Used: Variant Assay, Western Blot, Staining

    fetuin  (New England Biolabs)


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    Structured Review

    New England Biolabs fetuin
    Characterization of wild-type and D614G S glycoproteins in GALE/GALK2 293T cells. (A) The wild-type SARS-CoV-2 S glycoprotein (D614, with an aspartic acid residue at 614) and the D614G variant (G614, with a glycine residue at 614) were expressed in wild-type 293T cells (wt) or in GALE/GALK2 293T cells (ko) . Cell lysates were untreated (No Rx) or were treated with the <t>indicated</t> <t>glycosidase(s),</t> followed by Western blotting with a mouse antibody against S1 (upper) or a rabbit antibody against S2 (lower). The S glycoproteins, either untreated or treated with different glycosidases, are indicated by red arrows. (B) As a control, <t>fetuin,</t> which has N- and O-linked glycans, was treated with the indicated glycosidases. The SDS-polyacrylamide gel was stained with Coomassie blue. The different fetuin glycoforms are indicated by red arrows. The results shown are typical of those obtained in two independent experiments.
    Fetuin, 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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    Average 93 stars, based on 1 article reviews
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    fetuin - by Bioz Stars, 2023-02
    93/100 stars

    Images

    1) Product Images from "Analysis of Glycosylation and Disulfide Bonding of Wild-Type SARS-CoV-2 Spike Glycoprotein"

    Article Title: Analysis of Glycosylation and Disulfide Bonding of Wild-Type SARS-CoV-2 Spike Glycoprotein

    Journal: Journal of Virology

    doi: 10.1128/jvi.01626-21

    Characterization of wild-type and D614G S glycoproteins in GALE/GALK2 293T cells. (A) The wild-type SARS-CoV-2 S glycoprotein (D614, with an aspartic acid residue at 614) and the D614G variant (G614, with a glycine residue at 614) were expressed in wild-type 293T cells (wt) or in GALE/GALK2 293T cells (ko) . Cell lysates were untreated (No Rx) or were treated with the indicated glycosidase(s), followed by Western blotting with a mouse antibody against S1 (upper) or a rabbit antibody against S2 (lower). The S glycoproteins, either untreated or treated with different glycosidases, are indicated by red arrows. (B) As a control, fetuin, which has N- and O-linked glycans, was treated with the indicated glycosidases. The SDS-polyacrylamide gel was stained with Coomassie blue. The different fetuin glycoforms are indicated by red arrows. The results shown are typical of those obtained in two independent experiments.
    Figure Legend Snippet: Characterization of wild-type and D614G S glycoproteins in GALE/GALK2 293T cells. (A) The wild-type SARS-CoV-2 S glycoprotein (D614, with an aspartic acid residue at 614) and the D614G variant (G614, with a glycine residue at 614) were expressed in wild-type 293T cells (wt) or in GALE/GALK2 293T cells (ko) . Cell lysates were untreated (No Rx) or were treated with the indicated glycosidase(s), followed by Western blotting with a mouse antibody against S1 (upper) or a rabbit antibody against S2 (lower). The S glycoproteins, either untreated or treated with different glycosidases, are indicated by red arrows. (B) As a control, fetuin, which has N- and O-linked glycans, was treated with the indicated glycosidases. The SDS-polyacrylamide gel was stained with Coomassie blue. The different fetuin glycoforms are indicated by red arrows. The results shown are typical of those obtained in two independent experiments.

    Techniques Used: Variant Assay, Western Blot, Staining

    fetuin  (New England Biolabs)


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    Structured Review

    New England Biolabs fetuin
    Experimental conditions for optimal limited deglycosylation of <t>bovine</t> <t>RNase</t> B and <t>fetuin</t> 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.
    Fetuin, 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/fetuin/product/New England Biolabs
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    fetuin - by Bioz Stars, 2023-02
    93/100 stars

    Images

    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

    fetuin  (New England Biolabs)


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    Structured Review

    New England Biolabs fetuin
    Experimental conditions for optimal limited deglycosylation of bovine RNase B and <t>fetuin</t> 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 <t>the</t> <t>glycoproteins</t> in 15% SDS-PAGE. Fully deglycosylated (+) and fully glycosylated (−) proteins were included for each optimization reaction, denoted by FD and FG, respectively.
    Fetuin, 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/fetuin/product/New England Biolabs
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    fetuin - by Bioz Stars, 2023-02
    93/100 stars

    Images

    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

    fetuin  (New England Biolabs)


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    New England Biolabs fetuin
    (A) The wild-type SARS-CoV-2 S glycoprotein (D614, with an aspartic acid residue at 614) and the D614G variant (G614, with a glycine residue at 614) were expressed in wild-type 293T cells (wt) or in GALE/GALK2 293T cells (ko) . Cell lysates were untreated (No Rx) or were treated with the <t>indicated</t> <t>glycosidase(s),</t> followed by Western blotting with a mouse antibody against S1 (upper panels) or a rabbit antibody against S2 (lower panels). The S glycoproteins, either untreated or treated with different glycosidases, are indicated by red arrows. (B) As a control, <t>fetuin,</t> which has N- and O-linked glycans, was treated with the indicated glycosidases. The different fetuin glycoforms are indicated by red arrows.
    Fetuin, 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/fetuin/product/New England Biolabs
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    fetuin - by Bioz Stars, 2023-02
    93/100 stars

    Images

    1) Product Images from "Analysis of glycosylation and disulfide bonding of wild-type SARS-CoV-2 spike glycoprotein"

    Article Title: Analysis of glycosylation and disulfide bonding of wild-type SARS-CoV-2 spike glycoprotein

    Journal: bioRxiv

    doi: 10.1101/2021.04.01.438120

    (A) The wild-type SARS-CoV-2 S glycoprotein (D614, with an aspartic acid residue at 614) and the D614G variant (G614, with a glycine residue at 614) were expressed in wild-type 293T cells (wt) or in GALE/GALK2 293T cells (ko) . Cell lysates were untreated (No Rx) or were treated with the indicated glycosidase(s), followed by Western blotting with a mouse antibody against S1 (upper panels) or a rabbit antibody against S2 (lower panels). The S glycoproteins, either untreated or treated with different glycosidases, are indicated by red arrows. (B) As a control, fetuin, which has N- and O-linked glycans, was treated with the indicated glycosidases. The different fetuin glycoforms are indicated by red arrows.
    Figure Legend Snippet: (A) The wild-type SARS-CoV-2 S glycoprotein (D614, with an aspartic acid residue at 614) and the D614G variant (G614, with a glycine residue at 614) were expressed in wild-type 293T cells (wt) or in GALE/GALK2 293T cells (ko) . Cell lysates were untreated (No Rx) or were treated with the indicated glycosidase(s), followed by Western blotting with a mouse antibody against S1 (upper panels) or a rabbit antibody against S2 (lower panels). The S glycoproteins, either untreated or treated with different glycosidases, are indicated by red arrows. (B) As a control, fetuin, which has N- and O-linked glycans, was treated with the indicated glycosidases. The different fetuin glycoforms are indicated by red arrows.

    Techniques Used: Variant Assay, Western Blot

    fetuin  (New England Biolabs)


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    New England Biolabs fetuin
    Characterization of wild-type and D614G S glycoproteins in GALE/GALK2 293T cells. (A) The wild-type SARS-CoV-2 S glycoprotein (D614, with an aspartic acid residue at 614) and the D614G variant (G614, with a glycine residue at 614) were expressed in wild-type 293T cells (wt) or in GALE/GALK2 293T cells (ko) . Cell lysates were untreated (No Rx) or were treated with the <t>indicated</t> <t>glycosidase(s),</t> followed by Western blotting with a mouse antibody against S1 (upper panels) or a rabbit antibody against S2 (lower panels). The S glycoproteins, either untreated or treated with different glycosidases, are indicated by red arrows. (B) As a control, <t>fetuin,</t> which has N- and O-linked glycans, was treated with the indicated glycosidases. The different fetuin glycoforms are indicated by red arrows.
    Fetuin, 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/fetuin/product/New England Biolabs
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    93/100 stars

    Images

    1) Product Images from "Analysis of glycosylation and disulfide bonding of wild-type SARS-CoV-2 spike glycoprotein"

    Article Title: Analysis of glycosylation and disulfide bonding of wild-type SARS-CoV-2 spike glycoprotein

    Journal: bioRxiv

    doi: 10.1101/2021.04.01.438120

    Characterization of wild-type and D614G S glycoproteins in GALE/GALK2 293T cells. (A) The wild-type SARS-CoV-2 S glycoprotein (D614, with an aspartic acid residue at 614) and the D614G variant (G614, with a glycine residue at 614) were expressed in wild-type 293T cells (wt) or in GALE/GALK2 293T cells (ko) . Cell lysates were untreated (No Rx) or were treated with the indicated glycosidase(s), followed by Western blotting with a mouse antibody against S1 (upper panels) or a rabbit antibody against S2 (lower panels). The S glycoproteins, either untreated or treated with different glycosidases, are indicated by red arrows. (B) As a control, fetuin, which has N- and O-linked glycans, was treated with the indicated glycosidases. The different fetuin glycoforms are indicated by red arrows.
    Figure Legend Snippet: Characterization of wild-type and D614G S glycoproteins in GALE/GALK2 293T cells. (A) The wild-type SARS-CoV-2 S glycoprotein (D614, with an aspartic acid residue at 614) and the D614G variant (G614, with a glycine residue at 614) were expressed in wild-type 293T cells (wt) or in GALE/GALK2 293T cells (ko) . Cell lysates were untreated (No Rx) or were treated with the indicated glycosidase(s), followed by Western blotting with a mouse antibody against S1 (upper panels) or a rabbit antibody against S2 (lower panels). The S glycoproteins, either untreated or treated with different glycosidases, are indicated by red arrows. (B) As a control, fetuin, which has N- and O-linked glycans, was treated with the indicated glycosidases. The different fetuin glycoforms are indicated by red arrows.

    Techniques Used: Variant Assay, Western Blot

    fetuin  (New England Biolabs)


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    Structured Review

    New England Biolabs fetuin
    Fetuin, 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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    glycoprotein fetuin  (New England Biolabs)


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    New England Biolabs glycoprotein fetuin
    Glycoprotein Fetuin, 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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    fetuin  (New England Biolabs)


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    Structured Review

    New England Biolabs fetuin
    Fetuin, 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/fetuin/product/New England Biolabs
    Average 93 stars, based on 1 article reviews
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    glycoprotein fetuin  (New England Biolabs)


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    New England Biolabs glycoprotein fetuin
    Recombinant ErpY-like protein binds to host extracellular matrix and plasma components. (A) Far-UV (190 to 240 nm) CD spectra of rErpY-like protein. The analyzed CD spectral data show the predominance of α-helix (87.6%), which is in agreement with the theoretically predicted secondary structure of the rErpY-like protein. The spectra are represented as averages from three scans with a scanning speed of 100 nm min−1. (B) Interaction between rErpY-like protein and commercial host ECM components. The binding of rErpY-like protein to ECM components (laminin, fibronectin, collagen type I, chondroitin sulfate A and B, hyaluronic acid, heparan sulfate, and elastin) or plasma components (fibrinogen, plasminogen, factor H, and factor I) was analyzed through ELISA. The plasma components <t>fetuin</t> (highly glycosylated protein) and bovine serum albumin fraction V (nonglycosylated protein) were included as negative controls for ligands. rLoa22, which is known to interact moderately with host ECM components, was included in the assay as a negative-control protein. Protein-specific antisera (anti-ErpY-like protein or anti-Loa22 antibody) were used to measure the interaction of recombinant proteins with host ligands. The rErpY-like protein was recorded to interact preferentially with plasma fibrinogen, followed by factor H and other host ligands. The bar represents mean absorbance values (450 nm) for a ligand. Error bars are indicative of SD from two independent experiments, each performed in triplicate. For statistical analyses, the binding of rErpY-like protein with host ligands was compared to that with fetuin <t>or</t> <t>BSA</t> by the two-tailed t test (***, P < 0.001). (C) Pure rErpY-like protein forms a supramolecule. The purified rErpY-like protein (0.5, 1, and 2 μg) was resolved on a 4 to 20% native-PAGE and stained with Coomassie blue. The standard native molecular weight marker (M) was run in lane 1. The rErpY-like protein resolved at around 300 kDa. The gel in this figure has been spliced for labeling purposes. (D) Denaturing polyacrylamide gel electrophoresis of rErpY-like protein after glutaraldehyde (GLD) cross-linking. Chemical cross-linking of rErpY-like protein with glutaraldehyde (0 to 45 min) shows multiple higher-molecular-weight bands when resolved in the presence (+) or absence (−) of DTT. In the panel on the right, the cross-linked products of two control proteins, β-casein and rLIC13341, demonstrate only one band of larger size.
    Glycoprotein Fetuin, 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 "Role of Supramolecule ErpY-Like Lipoprotein of Leptospira in Thrombin-Catalyzed Fibrin Clot Inhibition and Binding to Complement Factors H and I, and Its Diagnostic Potential"

    Article Title: Role of Supramolecule ErpY-Like Lipoprotein of Leptospira in Thrombin-Catalyzed Fibrin Clot Inhibition and Binding to Complement Factors H and I, and Its Diagnostic Potential

    Journal: Infection and Immunity

    doi: 10.1128/IAI.00536-19

    Recombinant ErpY-like protein binds to host extracellular matrix and plasma components. (A) Far-UV (190 to 240 nm) CD spectra of rErpY-like protein. The analyzed CD spectral data show the predominance of α-helix (87.6%), which is in agreement with the theoretically predicted secondary structure of the rErpY-like protein. The spectra are represented as averages from three scans with a scanning speed of 100 nm min−1. (B) Interaction between rErpY-like protein and commercial host ECM components. The binding of rErpY-like protein to ECM components (laminin, fibronectin, collagen type I, chondroitin sulfate A and B, hyaluronic acid, heparan sulfate, and elastin) or plasma components (fibrinogen, plasminogen, factor H, and factor I) was analyzed through ELISA. The plasma components fetuin (highly glycosylated protein) and bovine serum albumin fraction V (nonglycosylated protein) were included as negative controls for ligands. rLoa22, which is known to interact moderately with host ECM components, was included in the assay as a negative-control protein. Protein-specific antisera (anti-ErpY-like protein or anti-Loa22 antibody) were used to measure the interaction of recombinant proteins with host ligands. The rErpY-like protein was recorded to interact preferentially with plasma fibrinogen, followed by factor H and other host ligands. The bar represents mean absorbance values (450 nm) for a ligand. Error bars are indicative of SD from two independent experiments, each performed in triplicate. For statistical analyses, the binding of rErpY-like protein with host ligands was compared to that with fetuin or BSA by the two-tailed t test (***, P < 0.001). (C) Pure rErpY-like protein forms a supramolecule. The purified rErpY-like protein (0.5, 1, and 2 μg) was resolved on a 4 to 20% native-PAGE and stained with Coomassie blue. The standard native molecular weight marker (M) was run in lane 1. The rErpY-like protein resolved at around 300 kDa. The gel in this figure has been spliced for labeling purposes. (D) Denaturing polyacrylamide gel electrophoresis of rErpY-like protein after glutaraldehyde (GLD) cross-linking. Chemical cross-linking of rErpY-like protein with glutaraldehyde (0 to 45 min) shows multiple higher-molecular-weight bands when resolved in the presence (+) or absence (−) of DTT. In the panel on the right, the cross-linked products of two control proteins, β-casein and rLIC13341, demonstrate only one band of larger size.
    Figure Legend Snippet: Recombinant ErpY-like protein binds to host extracellular matrix and plasma components. (A) Far-UV (190 to 240 nm) CD spectra of rErpY-like protein. The analyzed CD spectral data show the predominance of α-helix (87.6%), which is in agreement with the theoretically predicted secondary structure of the rErpY-like protein. The spectra are represented as averages from three scans with a scanning speed of 100 nm min−1. (B) Interaction between rErpY-like protein and commercial host ECM components. The binding of rErpY-like protein to ECM components (laminin, fibronectin, collagen type I, chondroitin sulfate A and B, hyaluronic acid, heparan sulfate, and elastin) or plasma components (fibrinogen, plasminogen, factor H, and factor I) was analyzed through ELISA. The plasma components fetuin (highly glycosylated protein) and bovine serum albumin fraction V (nonglycosylated protein) were included as negative controls for ligands. rLoa22, which is known to interact moderately with host ECM components, was included in the assay as a negative-control protein. Protein-specific antisera (anti-ErpY-like protein or anti-Loa22 antibody) were used to measure the interaction of recombinant proteins with host ligands. The rErpY-like protein was recorded to interact preferentially with plasma fibrinogen, followed by factor H and other host ligands. The bar represents mean absorbance values (450 nm) for a ligand. Error bars are indicative of SD from two independent experiments, each performed in triplicate. For statistical analyses, the binding of rErpY-like protein with host ligands was compared to that with fetuin or BSA by the two-tailed t test (***, P < 0.001). (C) Pure rErpY-like protein forms a supramolecule. The purified rErpY-like protein (0.5, 1, and 2 μg) was resolved on a 4 to 20% native-PAGE and stained with Coomassie blue. The standard native molecular weight marker (M) was run in lane 1. The rErpY-like protein resolved at around 300 kDa. The gel in this figure has been spliced for labeling purposes. (D) Denaturing polyacrylamide gel electrophoresis of rErpY-like protein after glutaraldehyde (GLD) cross-linking. Chemical cross-linking of rErpY-like protein with glutaraldehyde (0 to 45 min) shows multiple higher-molecular-weight bands when resolved in the presence (+) or absence (−) of DTT. In the panel on the right, the cross-linked products of two control proteins, β-casein and rLIC13341, demonstrate only one band of larger size.

    Techniques Used: Recombinant, Binding Assay, Enzyme-linked Immunosorbent Assay, Negative Control, Two Tailed Test, Purification, Clear Native PAGE, Staining, Molecular Weight, Marker, Labeling, Polyacrylamide Gel Electrophoresis

    fetuin after denaturation  (New England Biolabs)


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    Structured Review

    New England Biolabs fetuin after denaturation
    Rate of glycoprotein immobilization and PNGase F release of N-glycans. ( a ) <t>Fetuin</t> <t>was</t> <t>conjugated</t> to Aminolink resin via reductive amination, whereas the unbound proteins in supernatant were measured by a BCA assay. Fetuin was quickly immobilized to the resin within 4 h; ( b ) N-glycans were released by PNGase F in 25 mM ammonium bicarbonate at 37 °C. The PNGase F digestion was complete within 2 h. Four measurement were made for each condition and error bar represented standard deviation.
    Fetuin After Denaturation, 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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    Average 93 stars, based on 1 article reviews
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    1) Product Images from "High-throughput analysis of N-glycans using AutoTip via glycoprotein immobilization"

    Article Title: High-throughput analysis of N-glycans using AutoTip via glycoprotein immobilization

    Journal: Scientific Reports

    doi: 10.1038/s41598-017-10487-8

    Rate of glycoprotein immobilization and PNGase F release of N-glycans. ( a ) Fetuin was conjugated to Aminolink resin via reductive amination, whereas the unbound proteins in supernatant were measured by a BCA assay. Fetuin was quickly immobilized to the resin within 4 h; ( b ) N-glycans were released by PNGase F in 25 mM ammonium bicarbonate at 37 °C. The PNGase F digestion was complete within 2 h. Four measurement were made for each condition and error bar represented standard deviation.
    Figure Legend Snippet: Rate of glycoprotein immobilization and PNGase F release of N-glycans. ( a ) Fetuin was conjugated to Aminolink resin via reductive amination, whereas the unbound proteins in supernatant were measured by a BCA assay. Fetuin was quickly immobilized to the resin within 4 h; ( b ) N-glycans were released by PNGase F in 25 mM ammonium bicarbonate at 37 °C. The PNGase F digestion was complete within 2 h. Four measurement were made for each condition and error bar represented standard deviation.

    Techniques Used: BIA-KA, Standard Deviation

    Modification of sialic acids using carbodiimide coupling on AutoTip. Fetuin protein was modified by p-Toluidine in the presence of EDC after immobilization on the beads (Four AutoTips). Sialylated N-glycan, S2H5N4, was used to monitor completion of p-Toluidine-EDC reaction. Without derivatization, MALDI-MS detected no sialic acid H5N4 ( a ) and two sialic acids S2H5N4 ( c ); For incomplete derivatization, MALDI-MS detected ( a ), ( c ), and p-Toluidine labeled two sialic acids S2H5N4 ( b ); When completely labeled, only ( b ) was detected by MALDI-MS.
    Figure Legend Snippet: Modification of sialic acids using carbodiimide coupling on AutoTip. Fetuin protein was modified by p-Toluidine in the presence of EDC after immobilization on the beads (Four AutoTips). Sialylated N-glycan, S2H5N4, was used to monitor completion of p-Toluidine-EDC reaction. Without derivatization, MALDI-MS detected no sialic acid H5N4 ( a ) and two sialic acids S2H5N4 ( c ); For incomplete derivatization, MALDI-MS detected ( a ), ( c ), and p-Toluidine labeled two sialic acids S2H5N4 ( b ); When completely labeled, only ( b ) was detected by MALDI-MS.

    Techniques Used: Modification, Labeling

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    New England Biolabs fetuin
    Characterization of wild-type and D614G S glycoproteins in GALE/GALK2 293T cells. (A) The wild-type SARS-CoV-2 S glycoprotein (D614, with an aspartic acid residue at 614) and the D614G variant (G614, with a glycine residue at 614) were expressed in wild-type 293T cells (wt) or in GALE/GALK2 293T cells (ko) . Cell lysates were untreated (No Rx) or were treated with the <t>indicated</t> <t>glycosidase(s),</t> followed by Western blotting with a mouse antibody against S1 (upper) or a rabbit antibody against S2 (lower). The S glycoproteins, either untreated or treated with different glycosidases, are indicated by red arrows. (B) As a control, <t>fetuin,</t> which has N- and O-linked glycans, was treated with the indicated glycosidases. The SDS-polyacrylamide gel was stained with Coomassie blue. The different fetuin glycoforms are indicated by red arrows. The results shown are typical of those obtained in two independent experiments.
    Fetuin, 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 glycoprotein fetuin
    Characterization of wild-type and D614G S glycoproteins in GALE/GALK2 293T cells. (A) The wild-type SARS-CoV-2 S glycoprotein (D614, with an aspartic acid residue at 614) and the D614G variant (G614, with a glycine residue at 614) were expressed in wild-type 293T cells (wt) or in GALE/GALK2 293T cells (ko) . Cell lysates were untreated (No Rx) or were treated with the <t>indicated</t> <t>glycosidase(s),</t> followed by Western blotting with a mouse antibody against S1 (upper) or a rabbit antibody against S2 (lower). The S glycoproteins, either untreated or treated with different glycosidases, are indicated by red arrows. (B) As a control, <t>fetuin,</t> which has N- and O-linked glycans, was treated with the indicated glycosidases. The SDS-polyacrylamide gel was stained with Coomassie blue. The different fetuin glycoforms are indicated by red arrows. The results shown are typical of those obtained in two independent experiments.
    Glycoprotein Fetuin, 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 fetuin after denaturation
    Rate of glycoprotein immobilization and PNGase F release of N-glycans. ( a ) <t>Fetuin</t> <t>was</t> <t>conjugated</t> to Aminolink resin via reductive amination, whereas the unbound proteins in supernatant were measured by a BCA assay. Fetuin was quickly immobilized to the resin within 4 h; ( b ) N-glycans were released by PNGase F in 25 mM ammonium bicarbonate at 37 °C. The PNGase F digestion was complete within 2 h. Four measurement were made for each condition and error bar represented standard deviation.
    Fetuin After Denaturation, 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/fetuin after denaturation/product/New England Biolabs
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    fetuin after denaturation - by Bioz Stars, 2023-02
    93/100 stars
      Buy from Supplier

    Image Search Results


    Characterization of wild-type and D614G S glycoproteins in GALE/GALK2 293T cells. (A) The wild-type SARS-CoV-2 S glycoprotein (D614, with an aspartic acid residue at 614) and the D614G variant (G614, with a glycine residue at 614) were expressed in wild-type 293T cells (wt) or in GALE/GALK2 293T cells (ko) . Cell lysates were untreated (No Rx) or were treated with the indicated glycosidase(s), followed by Western blotting with a mouse antibody against S1 (upper) or a rabbit antibody against S2 (lower). The S glycoproteins, either untreated or treated with different glycosidases, are indicated by red arrows. (B) As a control, fetuin, which has N- and O-linked glycans, was treated with the indicated glycosidases. The SDS-polyacrylamide gel was stained with Coomassie blue. The different fetuin glycoforms are indicated by red arrows. The results shown are typical of those obtained in two independent experiments.

    Journal: Journal of Virology

    Article Title: Analysis of Glycosylation and Disulfide Bonding of Wild-Type SARS-CoV-2 Spike Glycoprotein

    doi: 10.1128/jvi.01626-21

    Figure Lengend Snippet: Characterization of wild-type and D614G S glycoproteins in GALE/GALK2 293T cells. (A) The wild-type SARS-CoV-2 S glycoprotein (D614, with an aspartic acid residue at 614) and the D614G variant (G614, with a glycine residue at 614) were expressed in wild-type 293T cells (wt) or in GALE/GALK2 293T cells (ko) . Cell lysates were untreated (No Rx) or were treated with the indicated glycosidase(s), followed by Western blotting with a mouse antibody against S1 (upper) or a rabbit antibody against S2 (lower). The S glycoproteins, either untreated or treated with different glycosidases, are indicated by red arrows. (B) As a control, fetuin, which has N- and O-linked glycans, was treated with the indicated glycosidases. The SDS-polyacrylamide gel was stained with Coomassie blue. The different fetuin glycoforms are indicated by red arrows. The results shown are typical of those obtained in two independent experiments.

    Article Snippet: Other reagents used in this study included optima liquid chromatography (LC)-MS-grade acetonitrile, water, formic acid (Fisher Scientific), sequencing-grade trypsin (Promega), chymotrypsin (Promega), glycerol-free peptidyl-N-glycosidase F (PNGase F) (New England Biolabs), endoglycosidase Hf (Endo Hf) (New England Biolabs), O-glycosidase (New England Biolabs), neuraminidase (New England Biolabs), and fetuin (New England Biolabs).

    Techniques: Variant Assay, Western Blot, Staining

    Rate of glycoprotein immobilization and PNGase F release of N-glycans. ( a ) Fetuin was conjugated to Aminolink resin via reductive amination, whereas the unbound proteins in supernatant were measured by a BCA assay. Fetuin was quickly immobilized to the resin within 4 h; ( b ) N-glycans were released by PNGase F in 25 mM ammonium bicarbonate at 37 °C. The PNGase F digestion was complete within 2 h. Four measurement were made for each condition and error bar represented standard deviation.

    Journal: Scientific Reports

    Article Title: High-throughput analysis of N-glycans using AutoTip via glycoprotein immobilization

    doi: 10.1038/s41598-017-10487-8

    Figure Lengend Snippet: Rate of glycoprotein immobilization and PNGase F release of N-glycans. ( a ) Fetuin was conjugated to Aminolink resin via reductive amination, whereas the unbound proteins in supernatant were measured by a BCA assay. Fetuin was quickly immobilized to the resin within 4 h; ( b ) N-glycans were released by PNGase F in 25 mM ammonium bicarbonate at 37 °C. The PNGase F digestion was complete within 2 h. Four measurement were made for each condition and error bar represented standard deviation.

    Article Snippet: Each AutoTip conjugated 20 µg of fetuin after denaturation (88 µL fetuin protein in HPLC water +10 µL denaturing buffer (NEB); 100 °C/10 min).

    Techniques: BIA-KA, Standard Deviation

    Modification of sialic acids using carbodiimide coupling on AutoTip. Fetuin protein was modified by p-Toluidine in the presence of EDC after immobilization on the beads (Four AutoTips). Sialylated N-glycan, S2H5N4, was used to monitor completion of p-Toluidine-EDC reaction. Without derivatization, MALDI-MS detected no sialic acid H5N4 ( a ) and two sialic acids S2H5N4 ( c ); For incomplete derivatization, MALDI-MS detected ( a ), ( c ), and p-Toluidine labeled two sialic acids S2H5N4 ( b ); When completely labeled, only ( b ) was detected by MALDI-MS.

    Journal: Scientific Reports

    Article Title: High-throughput analysis of N-glycans using AutoTip via glycoprotein immobilization

    doi: 10.1038/s41598-017-10487-8

    Figure Lengend Snippet: Modification of sialic acids using carbodiimide coupling on AutoTip. Fetuin protein was modified by p-Toluidine in the presence of EDC after immobilization on the beads (Four AutoTips). Sialylated N-glycan, S2H5N4, was used to monitor completion of p-Toluidine-EDC reaction. Without derivatization, MALDI-MS detected no sialic acid H5N4 ( a ) and two sialic acids S2H5N4 ( c ); For incomplete derivatization, MALDI-MS detected ( a ), ( c ), and p-Toluidine labeled two sialic acids S2H5N4 ( b ); When completely labeled, only ( b ) was detected by MALDI-MS.

    Article Snippet: Each AutoTip conjugated 20 µg of fetuin after denaturation (88 µL fetuin protein in HPLC water +10 µL denaturing buffer (NEB); 100 °C/10 min).

    Techniques: Modification, Labeling