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Glyxera GmbH mu pngase f

Mu Pngase F, supplied by Glyxera GmbH, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1) Product Images from "A hierarchical structure in the N-glycosylation process governs the N-glycosylation output: prolonged cultivation induces glycoenzymes expression variations that are reflected in the cellular N-glycome but not in the protein and site-specific glycoprofile of CHO cells"

Article Title: A hierarchical structure in the N-glycosylation process governs the N-glycosylation output: prolonged cultivation induces glycoenzymes expression variations that are reflected in the cellular N-glycome but not in the protein and site-specific glycoprofile of CHO cells

Journal: Glycobiology

doi: 10.1093/glycob/cwae045


Figure Legend Snippet:

Techniques Used: Protease Inhibitor, Labeling, Hydrophilic Interaction Liquid Chromatography, Polymer

pngase f solution  (New England Biolabs)


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    New England Biolabs pngase f solution
    Pngase F Solution, 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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    pngase f solution  (New England Biolabs)


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    New England Biolabs pngase f solution
    Pngase F Solution, 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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    pngase f deglycosylation  (Thermo Fisher)


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    Thermo Fisher pngase f deglycosylation
    Pngase F Deglycosylation, supplied by Thermo Fisher, 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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    pngase f glycan cleavage kit gibco cat  (Thermo Fisher)


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    Thermo Fisher pngase f glycan cleavage kit gibco cat
    Pngase F Glycan Cleavage Kit Gibco Cat, supplied by Thermo Fisher, 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 pngase f 3u sigma aldrich
    Pngase F 3u Sigma Aldrich, 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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    pngase f neb  (New England Biolabs)


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    New England Biolabs pngase f neb
    Pngase F Neb, 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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    pngase f glycan cleavage kit  (Thermo Fisher)


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    Thermo Fisher pngase f glycan cleavage kit
    Pngase F Glycan Cleavage Kit, supplied by Thermo Fisher, 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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    pngase f  (New England Biolabs)


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    New England Biolabs pngase f
    Pngase F, 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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    pngase f new england biolabs  (New England Biolabs)


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    New England Biolabs pngase f new england biolabs
    Left atrial appendages from 10 control (sinus rhythm, SR) and 10 AF patients were homogenized using protein solubilization buffer (Bio-Rad; Urea, Thiourea, CHAPS buffer), ceramic beads, and a bead homogenizer. A . Lysates were separated using Tris-acetate gels (3-8%), and proteins were then transferred to PVDF membranes. B . No changes in total levels of PC1/GAPDH were observed among samples (both bands). However, we noted that upper PC1 bands were upregulated in SR vs AF samples. The top band represents the fully glycosylated N-terminal of PC1 (mature; EndoH resistant; NTR), and the bottom band represents the N-terminal of PC1 with immature glycans as found in ER-resident proteins (immature; EndoH sensitive; NTS). C . Quantification of PC1 top/bottom bands from blot presented in A reveals impaired maturation in AF samples vs. SR. D . Representative Endo H and <t>PNGase</t> <t>F</t> showing PC1 immature and mature glycosylation. As expected, mature PC1 (top band) was significantly reduced in AF samples. N = patients are presented as violin plots, including individual data points, median and upper and lower quartiles. No data was excluded or added after the initial analysis design (refer to Table S1a for further statistical information). E . Proposed model: loss of function of PC1 reduces DNA repair genes through impaired E2F signaling. This reduction increases susceptibility to DNA damage. Additionally, impaired PC1 leads to shortened action potential and reduced Ca 2+ transients. These combined factors likely contribute to the increased AF inducibility observed in PC1-deficient mice.
    Pngase F New England Biolabs, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Polycystin-1 loss of function increases susceptibility to atrial fibrillation through impaired DNA damage response"

    Article Title: Polycystin-1 loss of function increases susceptibility to atrial fibrillation through impaired DNA damage response

    Journal: bioRxiv

    doi: 10.1101/2024.07.08.602618

    Left atrial appendages from 10 control (sinus rhythm, SR) and 10 AF patients were homogenized using protein solubilization buffer (Bio-Rad; Urea, Thiourea, CHAPS buffer), ceramic beads, and a bead homogenizer. A . Lysates were separated using Tris-acetate gels (3-8%), and proteins were then transferred to PVDF membranes. B . No changes in total levels of PC1/GAPDH were observed among samples (both bands). However, we noted that upper PC1 bands were upregulated in SR vs AF samples. The top band represents the fully glycosylated N-terminal of PC1 (mature; EndoH resistant; NTR), and the bottom band represents the N-terminal of PC1 with immature glycans as found in ER-resident proteins (immature; EndoH sensitive; NTS). C . Quantification of PC1 top/bottom bands from blot presented in A reveals impaired maturation in AF samples vs. SR. D . Representative Endo H and PNGase F showing PC1 immature and mature glycosylation. As expected, mature PC1 (top band) was significantly reduced in AF samples. N = patients are presented as violin plots, including individual data points, median and upper and lower quartiles. No data was excluded or added after the initial analysis design (refer to Table S1a for further statistical information). E . Proposed model: loss of function of PC1 reduces DNA repair genes through impaired E2F signaling. This reduction increases susceptibility to DNA damage. Additionally, impaired PC1 leads to shortened action potential and reduced Ca 2+ transients. These combined factors likely contribute to the increased AF inducibility observed in PC1-deficient mice.
    Figure Legend Snippet: Left atrial appendages from 10 control (sinus rhythm, SR) and 10 AF patients were homogenized using protein solubilization buffer (Bio-Rad; Urea, Thiourea, CHAPS buffer), ceramic beads, and a bead homogenizer. A . Lysates were separated using Tris-acetate gels (3-8%), and proteins were then transferred to PVDF membranes. B . No changes in total levels of PC1/GAPDH were observed among samples (both bands). However, we noted that upper PC1 bands were upregulated in SR vs AF samples. The top band represents the fully glycosylated N-terminal of PC1 (mature; EndoH resistant; NTR), and the bottom band represents the N-terminal of PC1 with immature glycans as found in ER-resident proteins (immature; EndoH sensitive; NTS). C . Quantification of PC1 top/bottom bands from blot presented in A reveals impaired maturation in AF samples vs. SR. D . Representative Endo H and PNGase F showing PC1 immature and mature glycosylation. As expected, mature PC1 (top band) was significantly reduced in AF samples. N = patients are presented as violin plots, including individual data points, median and upper and lower quartiles. No data was excluded or added after the initial analysis design (refer to Table S1a for further statistical information). E . Proposed model: loss of function of PC1 reduces DNA repair genes through impaired E2F signaling. This reduction increases susceptibility to DNA damage. Additionally, impaired PC1 leads to shortened action potential and reduced Ca 2+ transients. These combined factors likely contribute to the increased AF inducibility observed in PC1-deficient mice.

    Techniques Used: Control

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    Left atrial appendages from 10 control (sinus rhythm, SR) and 10 AF patients were homogenized using protein solubilization buffer (Bio-Rad; Urea, Thiourea, CHAPS buffer), ceramic beads, and a bead homogenizer. A . Lysates were separated using Tris-acetate gels (3-8%), and proteins were then transferred to PVDF membranes. B . No changes in total levels of PC1/GAPDH were observed among samples (both bands). However, we noted that upper PC1 bands were upregulated in SR vs AF samples. The top band represents the fully glycosylated N-terminal of PC1 (mature; EndoH resistant; NTR), and the bottom band represents the N-terminal of PC1 with immature glycans as found in ER-resident proteins (immature; EndoH sensitive; NTS). C . Quantification of PC1 top/bottom bands from blot presented in A reveals impaired maturation in AF samples vs. SR. D . Representative Endo H and <t>PNGase</t> <t>F</t> showing PC1 immature and mature glycosylation. As expected, mature PC1 (top band) was significantly reduced in AF samples. N = patients are presented as violin plots, including individual data points, median and upper and lower quartiles. No data was excluded or added after the initial analysis design (refer to Table S1a for further statistical information). E . Proposed model: loss of function of PC1 reduces DNA repair genes through impaired E2F signaling. This reduction increases susceptibility to DNA damage. Additionally, impaired PC1 leads to shortened action potential and reduced Ca 2+ transients. These combined factors likely contribute to the increased AF inducibility observed in PC1-deficient mice.
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    Journal: Glycobiology

    Article Title: A hierarchical structure in the N-glycosylation process governs the N-glycosylation output: prolonged cultivation induces glycoenzymes expression variations that are reflected in the cellular N-glycome but not in the protein and site-specific glycoprofile of CHO cells

    doi: 10.1093/glycob/cwae045

    Figure Lengend Snippet:

    Article Snippet: N-glycans were released by an 16 h incubation at 37 °C with 1 mU PNGase F. Samples were dried in a vacuum concentrator and labeled with the glyXprep™ APTS labeling Kit (glyxera).

    Techniques: Protease Inhibitor, Labeling, Hydrophilic Interaction Liquid Chromatography, Polymer

    Left atrial appendages from 10 control (sinus rhythm, SR) and 10 AF patients were homogenized using protein solubilization buffer (Bio-Rad; Urea, Thiourea, CHAPS buffer), ceramic beads, and a bead homogenizer. A . Lysates were separated using Tris-acetate gels (3-8%), and proteins were then transferred to PVDF membranes. B . No changes in total levels of PC1/GAPDH were observed among samples (both bands). However, we noted that upper PC1 bands were upregulated in SR vs AF samples. The top band represents the fully glycosylated N-terminal of PC1 (mature; EndoH resistant; NTR), and the bottom band represents the N-terminal of PC1 with immature glycans as found in ER-resident proteins (immature; EndoH sensitive; NTS). C . Quantification of PC1 top/bottom bands from blot presented in A reveals impaired maturation in AF samples vs. SR. D . Representative Endo H and PNGase F showing PC1 immature and mature glycosylation. As expected, mature PC1 (top band) was significantly reduced in AF samples. N = patients are presented as violin plots, including individual data points, median and upper and lower quartiles. No data was excluded or added after the initial analysis design (refer to Table S1a for further statistical information). E . Proposed model: loss of function of PC1 reduces DNA repair genes through impaired E2F signaling. This reduction increases susceptibility to DNA damage. Additionally, impaired PC1 leads to shortened action potential and reduced Ca 2+ transients. These combined factors likely contribute to the increased AF inducibility observed in PC1-deficient mice.

    Journal: bioRxiv

    Article Title: Polycystin-1 loss of function increases susceptibility to atrial fibrillation through impaired DNA damage response

    doi: 10.1101/2024.07.08.602618

    Figure Lengend Snippet: Left atrial appendages from 10 control (sinus rhythm, SR) and 10 AF patients were homogenized using protein solubilization buffer (Bio-Rad; Urea, Thiourea, CHAPS buffer), ceramic beads, and a bead homogenizer. A . Lysates were separated using Tris-acetate gels (3-8%), and proteins were then transferred to PVDF membranes. B . No changes in total levels of PC1/GAPDH were observed among samples (both bands). However, we noted that upper PC1 bands were upregulated in SR vs AF samples. The top band represents the fully glycosylated N-terminal of PC1 (mature; EndoH resistant; NTR), and the bottom band represents the N-terminal of PC1 with immature glycans as found in ER-resident proteins (immature; EndoH sensitive; NTS). C . Quantification of PC1 top/bottom bands from blot presented in A reveals impaired maturation in AF samples vs. SR. D . Representative Endo H and PNGase F showing PC1 immature and mature glycosylation. As expected, mature PC1 (top band) was significantly reduced in AF samples. N = patients are presented as violin plots, including individual data points, median and upper and lower quartiles. No data was excluded or added after the initial analysis design (refer to Table S1a for further statistical information). E . Proposed model: loss of function of PC1 reduces DNA repair genes through impaired E2F signaling. This reduction increases susceptibility to DNA damage. Additionally, impaired PC1 leads to shortened action potential and reduced Ca 2+ transients. These combined factors likely contribute to the increased AF inducibility observed in PC1-deficient mice.

    Article Snippet: EndoH and PNGase F (New England BioLabs) were used to remove immature and mature glycosylation as per manufacturer instructions.

    Techniques: Control