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purified catd (human liver, calbiochem, gibbstown, nj, usa)  (Millipore)


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    Structured Review

    Millipore purified catd (human liver, calbiochem, gibbstown, nj, usa)
    Purified Catd (Human Liver, Calbiochem, Gibbstown, Nj, Usa), supplied by Millipore, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/purified+human+catd/recombinant+protein/10__3390_slash_molecules25020274-161-8-11
    Average 90 stars, based on 1 article reviews
    purified catd (human liver, calbiochem, gibbstown, nj, usa) - by Bioz Stars, 2026-09
    90/100 stars

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    Related Articles

    Purification:

    Article Title: Isoform-specific proteolysis of apolipoprotein-E in the brain.
    Article Snippet: Isoform-specific proteolysis of apolipoprotein-E in the brain David A. Elliott a, Kayan Tsoi a, Sandra Holinkova a, Sharon L. Chan a, Woojin S. Kim a,b, Glenda M. Halliday a,b, Kerry-Anne Rye c, Brett Garner a,b,∗ a Prince of Wales Medical Research Institute, Randwick, NSW 2031, Australia b School of Medical Sciences, Faculty of Medicine, University of New South Wales, Sydney, NSW 2052, Australia c The Heart Research Institute, Sydney, NSW 2050, Australia

    Incubation:

    Article Title: Isoform-specific proteolysis of apolipoprotein-E in the brain.
    Article Snippet: Isoform-specific proteolysis of apolipoprotein-E in the brain David A. Elliott a, Kayan Tsoi a, Sandra Holinkova a, Sharon L. Chan a, Woojin S. Kim a,b, Glenda M. Halliday a,b, Kerry-Anne Rye c, Brett Garner a,b,∗ a Prince of Wales Medical Research Institute, Randwick, NSW 2031, Australia b School of Medical Sciences, Faculty of Medicine, University of New South Wales, Sydney, NSW 2052, Australia c The Heart Research Institute, Sydney, NSW 2050, Australia

    Control:

    Article Title: Isoform-specific proteolysis of apolipoprotein-E in the brain.
    Article Snippet: Isoform-specific proteolysis of apolipoprotein-E in the brain David A. Elliott a, Kayan Tsoi a, Sandra Holinkova a, Sharon L. Chan a, Woojin S. Kim a,b, Glenda M. Halliday a,b, Kerry-Anne Rye c, Brett Garner a,b,∗ a Prince of Wales Medical Research Institute, Randwick, NSW 2031, Australia b School of Medical Sciences, Faculty of Medicine, University of New South Wales, Sydney, NSW 2052, Australia c The Heart Research Institute, Sydney, NSW 2050, Australia

    Concentration Assay:

    Article Title: Isoform-specific proteolysis of apolipoprotein-E in the brain.
    Article Snippet: Isoform-specific proteolysis of apolipoprotein-E in the brain David A. Elliott a, Kayan Tsoi a, Sandra Holinkova a, Sharon L. Chan a, Woojin S. Kim a,b, Glenda M. Halliday a,b, Kerry-Anne Rye c, Brett Garner a,b,∗ a Prince of Wales Medical Research Institute, Randwick, NSW 2031, Australia b School of Medical Sciences, Faculty of Medicine, University of New South Wales, Sydney, NSW 2052, Australia c The Heart Research Institute, Sydney, NSW 2050, Australia



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    Inhibition of <t>CatD</t> slows the catabolism of tau in vitro and in cultured cells. ( A ) Representative Coomassie blue-stained polyacrylamide gel loaded with recombinant human tau (rTau) incubated for the indicated times with recombinant <t>human</t> <t>CatD</t> (5 nM) in the absence or presence of equal concentrations (1 µM) of Aβ40 or Aβ42. ( B ) Quantification of rTau levels as a function of time in 4 independent experiments. Note how rTau catabolism is unaffected by Aβ40 but markedly slowed by Aβ42, a potent competitive inhibitor of CatD. Data are mean ± SEM; n = 4. ( C ) Overview of the experimental approach used to quantify hTau catabolism in “Tet-Off” cultured neuroblastoma cells (see main text). ( D ) Representative western blot showing hTau levels (stained with antibody P44) at different time points after cessation of hTau expression in the absence or presence of the CatD inhibitor, pepstatin A (PepA; 1 µM). ( E ) Quantitation of hTau levels as a function of time from 6 independent experiments. Note the marked increase in the half-life of hTau in the presence of PepA (0.98 days; 95% CI 0.80 to 1.25) relative to DMSO-treated controls (0.51 days; 95% CI 0.429 to 0.627; P = 0.0012). Data are mean ± SEM, n = 6
    Purified Human Catd, supplied by Enzo Biochem, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    purified catd (human liver, calbiochem, gibbstown, nj, usa)  (Millipore)
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    Inhibition of <t>CatD</t> slows the catabolism of tau in vitro and in cultured cells. ( A ) Representative Coomassie blue-stained polyacrylamide gel loaded with recombinant human tau (rTau) incubated for the indicated times with recombinant <t>human</t> <t>CatD</t> (5 nM) in the absence or presence of equal concentrations (1 µM) of Aβ40 or Aβ42. ( B ) Quantification of rTau levels as a function of time in 4 independent experiments. Note how rTau catabolism is unaffected by Aβ40 but markedly slowed by Aβ42, a potent competitive inhibitor of CatD. Data are mean ± SEM; n = 4. ( C ) Overview of the experimental approach used to quantify hTau catabolism in “Tet-Off” cultured neuroblastoma cells (see main text). ( D ) Representative western blot showing hTau levels (stained with antibody P44) at different time points after cessation of hTau expression in the absence or presence of the CatD inhibitor, pepstatin A (PepA; 1 µM). ( E ) Quantitation of hTau levels as a function of time from 6 independent experiments. Note the marked increase in the half-life of hTau in the presence of PepA (0.98 days; 95% CI 0.80 to 1.25) relative to DMSO-treated controls (0.51 days; 95% CI 0.429 to 0.627; P = 0.0012). Data are mean ± SEM, n = 6
    Purified Catd (Human Liver, Calbiochem, Gibbstown, Nj, Usa), supplied by Millipore, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 90 stars, based on 1 article reviews
    purified catd (human liver, calbiochem, gibbstown, nj, usa) - by Bioz Stars, 2026-09
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    purified human catd  (Millipore)
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    Inhibition of <t>CatD</t> slows the catabolism of tau in vitro and in cultured cells. ( A ) Representative Coomassie blue-stained polyacrylamide gel loaded with recombinant human tau (rTau) incubated for the indicated times with recombinant <t>human</t> <t>CatD</t> (5 nM) in the absence or presence of equal concentrations (1 µM) of Aβ40 or Aβ42. ( B ) Quantification of rTau levels as a function of time in 4 independent experiments. Note how rTau catabolism is unaffected by Aβ40 but markedly slowed by Aβ42, a potent competitive inhibitor of CatD. Data are mean ± SEM; n = 4. ( C ) Overview of the experimental approach used to quantify hTau catabolism in “Tet-Off” cultured neuroblastoma cells (see main text). ( D ) Representative western blot showing hTau levels (stained with antibody P44) at different time points after cessation of hTau expression in the absence or presence of the CatD inhibitor, pepstatin A (PepA; 1 µM). ( E ) Quantitation of hTau levels as a function of time from 6 independent experiments. Note the marked increase in the half-life of hTau in the presence of PepA (0.98 days; 95% CI 0.80 to 1.25) relative to DMSO-treated controls (0.51 days; 95% CI 0.429 to 0.627; P = 0.0012). Data are mean ± SEM, n = 6
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    purified human catd - by Bioz Stars, 2026-09
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    Image Search Results


    Inhibition of CatD slows the catabolism of tau in vitro and in cultured cells. ( A ) Representative Coomassie blue-stained polyacrylamide gel loaded with recombinant human tau (rTau) incubated for the indicated times with recombinant human CatD (5 nM) in the absence or presence of equal concentrations (1 µM) of Aβ40 or Aβ42. ( B ) Quantification of rTau levels as a function of time in 4 independent experiments. Note how rTau catabolism is unaffected by Aβ40 but markedly slowed by Aβ42, a potent competitive inhibitor of CatD. Data are mean ± SEM; n = 4. ( C ) Overview of the experimental approach used to quantify hTau catabolism in “Tet-Off” cultured neuroblastoma cells (see main text). ( D ) Representative western blot showing hTau levels (stained with antibody P44) at different time points after cessation of hTau expression in the absence or presence of the CatD inhibitor, pepstatin A (PepA; 1 µM). ( E ) Quantitation of hTau levels as a function of time from 6 independent experiments. Note the marked increase in the half-life of hTau in the presence of PepA (0.98 days; 95% CI 0.80 to 1.25) relative to DMSO-treated controls (0.51 days; 95% CI 0.429 to 0.627; P = 0.0012). Data are mean ± SEM, n = 6

    Journal: Alzheimer's Research & Therapy

    Article Title: Prominent tauopathy and intracellular β-amyloid accumulation triggered by genetic deletion of cathepsin D: implications for Alzheimer disease pathogenesis

    doi: 10.1186/s13195-024-01443-6

    Figure Lengend Snippet: Inhibition of CatD slows the catabolism of tau in vitro and in cultured cells. ( A ) Representative Coomassie blue-stained polyacrylamide gel loaded with recombinant human tau (rTau) incubated for the indicated times with recombinant human CatD (5 nM) in the absence or presence of equal concentrations (1 µM) of Aβ40 or Aβ42. ( B ) Quantification of rTau levels as a function of time in 4 independent experiments. Note how rTau catabolism is unaffected by Aβ40 but markedly slowed by Aβ42, a potent competitive inhibitor of CatD. Data are mean ± SEM; n = 4. ( C ) Overview of the experimental approach used to quantify hTau catabolism in “Tet-Off” cultured neuroblastoma cells (see main text). ( D ) Representative western blot showing hTau levels (stained with antibody P44) at different time points after cessation of hTau expression in the absence or presence of the CatD inhibitor, pepstatin A (PepA; 1 µM). ( E ) Quantitation of hTau levels as a function of time from 6 independent experiments. Note the marked increase in the half-life of hTau in the presence of PepA (0.98 days; 95% CI 0.80 to 1.25) relative to DMSO-treated controls (0.51 days; 95% CI 0.429 to 0.627; P = 0.0012). Data are mean ± SEM, n = 6

    Article Snippet: Reactions were initiated by addition of purified human CatD (2.5 nM; Enzo Life Sciences, Farmingdale, NY) dissolved in Assay Buffer, then 20-µL aliquots were removed 0, 0.5, 1, 2, and 4 h thereafter, with CatD activity in each aliquot immediately terminated by addition of PepA (1 µM) and incubation on ice.

    Techniques: Inhibition, In Vitro, Cell Culture, Staining, Recombinant, Incubation, Western Blot, Expressing, Quantitation Assay