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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 457 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/cleaved+atf6/ATF6+Antibody/pm41926654-317-104-107
    Average 96 stars, based on 457 article reviews
    cleaved atf6 - by Bioz Stars, 2026-10
    96/100 stars

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    Related Articles

    Blocking Assay:

    Article Title: Tetrastigma Hemsleyanum Polysaccharide Suppresses Triple-Negative Breast Cancer by Disrupting the Hippo-YAP/TEAD4-PDIA4 Axis and Endoplasmic Reticulum Stress Adaptation.
    Article Snippet: Equal amounts of protein were separated by 10% sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE, Beyotime, China) and transferred to polyvinylidene fluoride (PVDF) membranes (Millipore, USA). .. At room-temperature, block in 5% skimmed milk diluted with TBST for 1 h, then wash with TBST three times, and then incubate overnight with the primary antibody diluted with the primary antibody dilution solution at 4◦C: GAPDH (1:5,000, Proteintech, Cat.#60004-1Ig, USA), LATS1 (1:1000, Cell Signaling Technology, Cat.#3682, USA), MST1 (1:1,000, Cell Signaling Technology, Cat.#3952, USA), YAP (1:5000, Proteintech, Cat.#13584-1-AP, USA), p-YAP1 (Ser397) (1:2,000, Proteintech, Cat.#29018-1-AP, USA), p-YAP1 (Ser127) (1:10 000, abcam, Cat.#ab76252, USA), Vimentin (1:2000, Proteintech, Cat.#10366-1-AP, USA), TEAD4 (1:2000, Proteintech, Cat.# 12418-1-AP, USA), PDIA4 (1:2000, Proteintech, Cat.#147121-AP, USA), Bip (1:2000, Proteintech, Cat.#11587-1-AP, USA), p-PERK (1:5000, Proteintech, Cat.#82534-1-RR, USA), p-IRE1 (1:5000, abcam, Cat.#ab124945, USA), cleaved ATF6 (1:5000, Proteintech, Cat.#24169-1-AP, USA), and CHOP (1:2000, Proteintech, Cat.#15204-1-AP, USA), β-actin (1:1000, Cell Signaling Technology, Cat.#4970, USA). .. After three 10 min TBST washes, membranes were incubated with HRP-conjugated secondary antibodies (1:10 000, Biosharp, China) in 5% skimmed milk for 1 h at room-temperature, followed by three additional TBST washes.

    Incubation:

    Article Title: Hyperglycemia Aggravates Hepatic Ischemia and Reperfusion Injury by Inhibiting Liver-Resident Macrophage M2 Polarization via C/EBP Homologous Protein-Mediated Endoplasmic Reticulum Stress
    Article Snippet: .. Primary antibodies against cleaved-ATF6 (c-ATF6, Novus, Littleton, CO, USA), ATF4 (Proteintech Group, Chicago, IL, USA), CHOP (Cell Signaling Technology, MA, USA), spliced XBP1 (s-XBP1, Abcam, Cambridge, MA, USA), and β-actin (Cell Signaling Technology, MA, USA) were used and incubated overnight at 4°C. .. After 2 h of incubation with the appropriate HRP-conjugated secondary antibody (1:1,000), ClarityTM Western ECL Substrate (Bio-Rad, CA, USA) was used for chemoluminescence development.



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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