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cleaved atf6  (Proteintech)


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    Structured Review

    Proteintech cleaved atf6
    Cleaved Atf6, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 412 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/cleaved atf6/product/Proteintech
    Average 96 stars, based on 412 article reviews
    cleaved atf6 - by Bioz Stars, 2026-05
    96/100 stars

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    a Quantification of conjugated ubiquitin levels (measured as median fluorescence levels of mono- and poly-ubiquitinylated conjugates ( n = 5), specific K48-linked poly-ubiquitinylated conjugates ( n = 3) or specific K63-linked poly-ubiquitinylated conjugates ( n = 3)) in control and PCK2 KD1 ECs in 5.5 versus 0 mM glucose. AU, arbitrary units. b Quantification of proteasome activity (measured as luminescence signal emitted upon the degradation of aminoluciferin-tagged peptide substrate Z-nLPnLD-aminoluciferin upon caspase-like proteolytic activity) in control and PCK2 KD1 ECs in 5.5 versus 0 mM glucose ( n = 4); RLU relative luminescence units. c Heatmap of transcript levels of molecular chaperones (BiP (HSPA5), eIF2α (EIF2A), ATF4, CHOP (DDIT3), XBP1, <t>ATF6,</t> heat shock protein 90 (HSP90B1), Derlin (DERL2/3), PDI (PDIA3/4/6), EDEM1/2/3, DNAJB9, calreticulin (CALR) and calnexin (CANX)) involved in the unfolded protein response (UPR) assessed by bulk RNA sequencing of control and PCK2 KD1 ECs in 5.5 versus 0 mM glucose ( n = 3). Color scale: red, high expression; blue, low expression. d – h Representative immunoblot and densitometric quantification of BiP ( d ; n = 6), ATF4 ( e ; n = 4), CHOP ( e ; n = 3), spliced XBP1 (XBP1s; see black arrowhead) ( f ; n = 3), cleaved ATF6 (cATF6) ( g ; n = 7) and ERp72 ( h ; n = 4) protein levels in control and PCK2 KD1 ECs in 5.5 versus 0 mM glucose. GAPDH was used as a loading control. Data are mean ± s.e.m. Statistics: ANOVA ( a , b–h ); * P < 0.05; ** P < 0.01; *** P < 0.001; **** P < 0.0001.
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    a Quantification of conjugated ubiquitin levels (measured as median fluorescence levels of mono- and poly-ubiquitinylated conjugates ( n = 5), specific K48-linked poly-ubiquitinylated conjugates ( n = 3) or specific K63-linked poly-ubiquitinylated conjugates ( n = 3)) in control and PCK2 KD1 ECs in 5.5 versus 0 mM glucose. AU, arbitrary units. b Quantification of proteasome activity (measured as luminescence signal emitted upon the degradation of aminoluciferin-tagged peptide substrate Z-nLPnLD-aminoluciferin upon caspase-like proteolytic activity) in control and PCK2 KD1 ECs in 5.5 versus 0 mM glucose ( n = 4); RLU relative luminescence units. c Heatmap of transcript levels of molecular chaperones (BiP (HSPA5), eIF2α (EIF2A), ATF4, CHOP (DDIT3), XBP1, <t>ATF6,</t> heat shock protein 90 (HSP90B1), Derlin (DERL2/3), PDI (PDIA3/4/6), EDEM1/2/3, DNAJB9, calreticulin (CALR) and calnexin (CANX)) involved in the unfolded protein response (UPR) assessed by bulk RNA sequencing of control and PCK2 KD1 ECs in 5.5 versus 0 mM glucose ( n = 3). Color scale: red, high expression; blue, low expression. d – h Representative immunoblot and densitometric quantification of BiP ( d ; n = 6), ATF4 ( e ; n = 4), CHOP ( e ; n = 3), spliced XBP1 (XBP1s; see black arrowhead) ( f ; n = 3), cleaved ATF6 (cATF6) ( g ; n = 7) and ERp72 ( h ; n = 4) protein levels in control and PCK2 KD1 ECs in 5.5 versus 0 mM glucose. GAPDH was used as a loading control. Data are mean ± s.e.m. Statistics: ANOVA ( a , b–h ); * P < 0.05; ** P < 0.01; *** P < 0.001; **** P < 0.0001.
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    a Quantification of conjugated ubiquitin levels (measured as median fluorescence levels of mono- and poly-ubiquitinylated conjugates ( n = 5), specific K48-linked poly-ubiquitinylated conjugates ( n = 3) or specific K63-linked poly-ubiquitinylated conjugates ( n = 3)) in control and PCK2 KD1 ECs in 5.5 versus 0 mM glucose. AU, arbitrary units. b Quantification of proteasome activity (measured as luminescence signal emitted upon the degradation of aminoluciferin-tagged peptide substrate Z-nLPnLD-aminoluciferin upon caspase-like proteolytic activity) in control and PCK2 KD1 ECs in 5.5 versus 0 mM glucose ( n = 4); RLU relative luminescence units. c Heatmap of transcript levels of molecular chaperones (BiP (HSPA5), eIF2α (EIF2A), ATF4, CHOP (DDIT3), XBP1, <t>ATF6,</t> heat shock protein 90 (HSP90B1), Derlin (DERL2/3), PDI (PDIA3/4/6), EDEM1/2/3, DNAJB9, calreticulin (CALR) and calnexin (CANX)) involved in the unfolded protein response (UPR) assessed by bulk RNA sequencing of control and PCK2 KD1 ECs in 5.5 versus 0 mM glucose ( n = 3). Color scale: red, high expression; blue, low expression. d – h Representative immunoblot and densitometric quantification of BiP ( d ; n = 6), ATF4 ( e ; n = 4), CHOP ( e ; n = 3), spliced XBP1 (XBP1s; see black arrowhead) ( f ; n = 3), cleaved ATF6 (cATF6) ( g ; n = 7) and ERp72 ( h ; n = 4) protein levels in control and PCK2 KD1 ECs in 5.5 versus 0 mM glucose. GAPDH was used as a loading control. Data are mean ± s.e.m. Statistics: ANOVA ( a , b–h ); * P < 0.05; ** P < 0.01; *** P < 0.001; **** P < 0.0001.
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    Image Search Results


    a Quantification of conjugated ubiquitin levels (measured as median fluorescence levels of mono- and poly-ubiquitinylated conjugates ( n = 5), specific K48-linked poly-ubiquitinylated conjugates ( n = 3) or specific K63-linked poly-ubiquitinylated conjugates ( n = 3)) in control and PCK2 KD1 ECs in 5.5 versus 0 mM glucose. AU, arbitrary units. b Quantification of proteasome activity (measured as luminescence signal emitted upon the degradation of aminoluciferin-tagged peptide substrate Z-nLPnLD-aminoluciferin upon caspase-like proteolytic activity) in control and PCK2 KD1 ECs in 5.5 versus 0 mM glucose ( n = 4); RLU relative luminescence units. c Heatmap of transcript levels of molecular chaperones (BiP (HSPA5), eIF2α (EIF2A), ATF4, CHOP (DDIT3), XBP1, ATF6, heat shock protein 90 (HSP90B1), Derlin (DERL2/3), PDI (PDIA3/4/6), EDEM1/2/3, DNAJB9, calreticulin (CALR) and calnexin (CANX)) involved in the unfolded protein response (UPR) assessed by bulk RNA sequencing of control and PCK2 KD1 ECs in 5.5 versus 0 mM glucose ( n = 3). Color scale: red, high expression; blue, low expression. d – h Representative immunoblot and densitometric quantification of BiP ( d ; n = 6), ATF4 ( e ; n = 4), CHOP ( e ; n = 3), spliced XBP1 (XBP1s; see black arrowhead) ( f ; n = 3), cleaved ATF6 (cATF6) ( g ; n = 7) and ERp72 ( h ; n = 4) protein levels in control and PCK2 KD1 ECs in 5.5 versus 0 mM glucose. GAPDH was used as a loading control. Data are mean ± s.e.m. Statistics: ANOVA ( a , b–h ); * P < 0.05; ** P < 0.01; *** P < 0.001; **** P < 0.0001.

    Journal: Communications Biology

    Article Title: The gluconeogenesis enzyme PCK2 has a non-enzymatic role in proteostasis in endothelial cells

    doi: 10.1038/s42003-024-06186-6

    Figure Lengend Snippet: a Quantification of conjugated ubiquitin levels (measured as median fluorescence levels of mono- and poly-ubiquitinylated conjugates ( n = 5), specific K48-linked poly-ubiquitinylated conjugates ( n = 3) or specific K63-linked poly-ubiquitinylated conjugates ( n = 3)) in control and PCK2 KD1 ECs in 5.5 versus 0 mM glucose. AU, arbitrary units. b Quantification of proteasome activity (measured as luminescence signal emitted upon the degradation of aminoluciferin-tagged peptide substrate Z-nLPnLD-aminoluciferin upon caspase-like proteolytic activity) in control and PCK2 KD1 ECs in 5.5 versus 0 mM glucose ( n = 4); RLU relative luminescence units. c Heatmap of transcript levels of molecular chaperones (BiP (HSPA5), eIF2α (EIF2A), ATF4, CHOP (DDIT3), XBP1, ATF6, heat shock protein 90 (HSP90B1), Derlin (DERL2/3), PDI (PDIA3/4/6), EDEM1/2/3, DNAJB9, calreticulin (CALR) and calnexin (CANX)) involved in the unfolded protein response (UPR) assessed by bulk RNA sequencing of control and PCK2 KD1 ECs in 5.5 versus 0 mM glucose ( n = 3). Color scale: red, high expression; blue, low expression. d – h Representative immunoblot and densitometric quantification of BiP ( d ; n = 6), ATF4 ( e ; n = 4), CHOP ( e ; n = 3), spliced XBP1 (XBP1s; see black arrowhead) ( f ; n = 3), cleaved ATF6 (cATF6) ( g ; n = 7) and ERp72 ( h ; n = 4) protein levels in control and PCK2 KD1 ECs in 5.5 versus 0 mM glucose. GAPDH was used as a loading control. Data are mean ± s.e.m. Statistics: ANOVA ( a , b–h ); * P < 0.05; ** P < 0.01; *** P < 0.001; **** P < 0.0001.

    Article Snippet: We used primary antibodies against: PCK2 (D3E11, Cell Signaling Technology #8565, dilution 1:1,000), GAPDH (14C10, Cell Signaling Technology #2118, dilution 1:1,000), LC3B (Abcam #ab51520, dilution 1:3,000), p62/SQSTM1 (Sigma-Aldrich #P0067, dilution 1:1,000), BiP (C50B12, Cell Signaling Technology #3177, dilution 1:1,000), ATF4 (D4B8, Cell Signaling Technology #11815, dilution 1:1,000), CHOP (L63F7, Cell Signaling Technology #2895, dilution 1:1,000), VDAC1 (B-6, Santa Cruz Biotechnology #sc390996, dilution 1:200), SOD1 (Enzo Life Sciences #ADI-SOD-100, dilution 1:1,000), phospho-S6 (Ser235/236) (D57.2.E2, Cell Signaling Technology #4858, dilution 1:2,000), S6 (5G10, Cell Signaling Technology #2217, dilution 1:1,000), phospho-p70S6K (T389) (Cell Signaling Technology #9205, dilution 1:1,000), p70S6K (Cell Signaling Technology #9202, dilution 1:1,000), cleaved ATF6 (Abcam #ab122897, dilution 1:500), spliced XBP1 (XBP1s) (Novus Biologicals #NBP1-77681, dilution 1:1,000), ERp72 (D70D12, Cell Signaling Technology #5033, dilution 1:1,000).

    Techniques: Fluorescence, Activity Assay, RNA Sequencing Assay, Expressing, Western Blot