human erythrocyte gapdh  (Millipore)


Bioz Verified Symbol Millipore is a verified supplier  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 80

    Structured Review

    Millipore human erythrocyte gapdh
    Elution profiles of products formed from reaction of selenium-binding proteins with GSH and . Reaction mixtures (100 μl), containing PBS (pH 7.4), 0.1 mM , 0.4 mM GSH, and 10 μM <t>rhodanese</t> E form ( A and C ), 3-MST ( B and E ), or <t>GAPDH</t> ( C
    Human Erythrocyte Gapdh, supplied by Millipore, used in various techniques. Bioz Stars score: 80/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/human erythrocyte gapdh/product/Millipore
    Average 80 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    human erythrocyte gapdh - by Bioz Stars, 2020-03
    80/100 stars

    Images

    1) Product Images from "Characterization of potential selenium-binding proteins in the selenophosphate synthetase system"

    Article Title: Characterization of potential selenium-binding proteins in the selenophosphate synthetase system

    Journal:

    doi: 10.1073/pnas.0409042102

    Elution profiles of products formed from reaction of selenium-binding proteins with GSH and . Reaction mixtures (100 μl), containing PBS (pH 7.4), 0.1 mM , 0.4 mM GSH, and 10 μM rhodanese E form ( A and C ), 3-MST ( B and E ), or GAPDH ( C
    Figure Legend Snippet: Elution profiles of products formed from reaction of selenium-binding proteins with GSH and . Reaction mixtures (100 μl), containing PBS (pH 7.4), 0.1 mM , 0.4 mM GSH, and 10 μM rhodanese E form ( A and C ), 3-MST ( B and E ), or GAPDH ( C

    Techniques Used: Binding Assay, Microscale Thermophoresis

    Related Articles

    Clone Assay:

    Article Title: Characterization of potential selenium-binding proteins in the selenophosphate synthetase system
    Article Snippet: Bovine liver rhodanese, human erythrocyte GAPDH, Na2 SeO3 , ATP, thioctic acid (α-lipoic acid), and AMP were obtained from Sigma. .. Dihydrolipoic acid (DHLA) was prepared according to the method of Pagani et al . ( ) The 3 - mst gene from human liver was cloned into pGEX-2T (pGEX-2T/MS 1.2), and the gene product from the recombinant expression system was purified as the glutathione S -transferase fusion protein.

    Nucleic Acid Electrophoresis:

    Article Title: Reactions of Glyceraldehyde 3-Phosphate Dehydrogenase Sulfhydryl Groups with bis-Electrophiles Produce DNA-Protein Crosslinks but Not Mutations
    Article Snippet: The oligonucleotide 5′-GGAGGAGGAGGAGGAG-3′ was synthesized by Midland Certified (Midland, TX) and purified by denaturing gel electrophoresis. .. Purified human erythrocyte GAPDH was purchased from Sigma-Aldrich (St. Louis, MO) and E. coli recombinant human AGT was a gift of A. E. Pegg (Pennsylvania State Univ., Hershey, PA).

    Synthesized:

    Article Title: Reactions of Glyceraldehyde 3-Phosphate Dehydrogenase Sulfhydryl Groups with bis-Electrophiles Produce DNA-Protein Crosslinks but Not Mutations
    Article Snippet: The oligonucleotide 5′-GGAGGAGGAGGAGGAG-3′ was synthesized by Midland Certified (Midland, TX) and purified by denaturing gel electrophoresis. .. Purified human erythrocyte GAPDH was purchased from Sigma-Aldrich (St. Louis, MO) and E. coli recombinant human AGT was a gift of A. E. Pegg (Pennsylvania State Univ., Hershey, PA).

    Microscale Thermophoresis:

    Article Title: Characterization of potential selenium-binding proteins in the selenophosphate synthetase system
    Article Snippet: Bovine liver rhodanese, human erythrocyte GAPDH, Na2 SeO3 , ATP, thioctic acid (α-lipoic acid), and AMP were obtained from Sigma. .. Dihydrolipoic acid (DHLA) was prepared according to the method of Pagani et al . ( ) The 3 - mst gene from human liver was cloned into pGEX-2T (pGEX-2T/MS 1.2), and the gene product from the recombinant expression system was purified as the glutathione S -transferase fusion protein.

    Purification:

    Article Title: Reactions of Glyceraldehyde 3-Phosphate Dehydrogenase Sulfhydryl Groups with bis-Electrophiles Produce DNA-Protein Crosslinks but Not Mutations
    Article Snippet: .. Purified human erythrocyte GAPDH was purchased from Sigma-Aldrich (St. Louis, MO) and E. coli recombinant human AGT was a gift of A. E. Pegg (Pennsylvania State Univ., Hershey, PA). .. Activity assays were performed as previously described ( ) using GAPDH.

    Expressing:

    Article Title: Characterization of potential selenium-binding proteins in the selenophosphate synthetase system
    Article Snippet: Bovine liver rhodanese, human erythrocyte GAPDH, Na2 SeO3 , ATP, thioctic acid (α-lipoic acid), and AMP were obtained from Sigma. .. Dihydrolipoic acid (DHLA) was prepared according to the method of Pagani et al . ( ) The 3 - mst gene from human liver was cloned into pGEX-2T (pGEX-2T/MS 1.2), and the gene product from the recombinant expression system was purified as the glutathione S -transferase fusion protein.

    Recombinant:

    Article Title: Characterization of potential selenium-binding proteins in the selenophosphate synthetase system
    Article Snippet: Bovine liver rhodanese, human erythrocyte GAPDH, Na2 SeO3 , ATP, thioctic acid (α-lipoic acid), and AMP were obtained from Sigma. .. Dihydrolipoic acid (DHLA) was prepared according to the method of Pagani et al . ( ) The 3 - mst gene from human liver was cloned into pGEX-2T (pGEX-2T/MS 1.2), and the gene product from the recombinant expression system was purified as the glutathione S -transferase fusion protein.

    Article Title: Reactions of Glyceraldehyde 3-Phosphate Dehydrogenase Sulfhydryl Groups with bis-Electrophiles Produce DNA-Protein Crosslinks but Not Mutations
    Article Snippet: .. Purified human erythrocyte GAPDH was purchased from Sigma-Aldrich (St. Louis, MO) and E. coli recombinant human AGT was a gift of A. E. Pegg (Pennsylvania State Univ., Hershey, PA). .. Activity assays were performed as previously described ( ) using GAPDH.

    Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 84
    Millipore lc3b ii gapdh
    Autophagy caused by starvation does not require MAPK8/9 in immortalized MEFs. (a) RPS6KB1, p-Thr389 RPS6KB1, and TUBA expression by WT and mapk8 −/- mapk9 −/- immortalized MEFs after incubation with EBSS containing 5mM glucose (2 or 4 h) was examined by immunoblot analysis. (b) WT and mapk8 −/- mapk9 −/- immortalized MEFs were transduced with a lentivirus vector that expresses <t>GFP-LC3B.</t> Puncta formation following incubation with EBSS containing 5 mM glucose (2 h) was examined by fluorescence microscopy. Scale bar: 30 µm. (c) LC3B and <t>GAPDH</t> in WT and mapk8 −/- mapk9 −/- immortalized MEFs after incubation (2 h) in medium or with EBSS containing 5 mM glucose in the presence or absence of 25 µM chloroquine (CQ) was examined by immunoblot analysis. The LC3B-II:GAPDH ratios were normalized to the average of WT control condition (first lane). The data presented represent the mean ± SEM; n = 3 independent experiments; *, p
    Lc3b Ii Gapdh, supplied by Millipore, used in various techniques. Bioz Stars score: 84/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/lc3b ii gapdh/product/Millipore
    Average 84 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    lc3b ii gapdh - by Bioz Stars, 2020-03
    84/100 stars
      Buy from Supplier

    Image Search Results


    Autophagy caused by starvation does not require MAPK8/9 in immortalized MEFs. (a) RPS6KB1, p-Thr389 RPS6KB1, and TUBA expression by WT and mapk8 −/- mapk9 −/- immortalized MEFs after incubation with EBSS containing 5mM glucose (2 or 4 h) was examined by immunoblot analysis. (b) WT and mapk8 −/- mapk9 −/- immortalized MEFs were transduced with a lentivirus vector that expresses GFP-LC3B. Puncta formation following incubation with EBSS containing 5 mM glucose (2 h) was examined by fluorescence microscopy. Scale bar: 30 µm. (c) LC3B and GAPDH in WT and mapk8 −/- mapk9 −/- immortalized MEFs after incubation (2 h) in medium or with EBSS containing 5 mM glucose in the presence or absence of 25 µM chloroquine (CQ) was examined by immunoblot analysis. The LC3B-II:GAPDH ratios were normalized to the average of WT control condition (first lane). The data presented represent the mean ± SEM; n = 3 independent experiments; *, p

    Journal: Autophagy

    Article Title: Role of the MAPK/cJun NH2-terminal kinase signaling pathway in starvation-induced autophagy

    doi: 10.1080/15548627.2018.1466013

    Figure Lengend Snippet: Autophagy caused by starvation does not require MAPK8/9 in immortalized MEFs. (a) RPS6KB1, p-Thr389 RPS6KB1, and TUBA expression by WT and mapk8 −/- mapk9 −/- immortalized MEFs after incubation with EBSS containing 5mM glucose (2 or 4 h) was examined by immunoblot analysis. (b) WT and mapk8 −/- mapk9 −/- immortalized MEFs were transduced with a lentivirus vector that expresses GFP-LC3B. Puncta formation following incubation with EBSS containing 5 mM glucose (2 h) was examined by fluorescence microscopy. Scale bar: 30 µm. (c) LC3B and GAPDH in WT and mapk8 −/- mapk9 −/- immortalized MEFs after incubation (2 h) in medium or with EBSS containing 5 mM glucose in the presence or absence of 25 µM chloroquine (CQ) was examined by immunoblot analysis. The LC3B-II:GAPDH ratios were normalized to the average of WT control condition (first lane). The data presented represent the mean ± SEM; n = 3 independent experiments; *, p

    Article Snippet: Autophagic flux was examined by measuring the LC3B-II:GAPDH ratio or LC3B-II:TUBA (tubulin alpha) ratio by immunoblot analysis, normalization of the data to the control condition (without autophagy induction or CQ), and calculation of the increased LC3B-II:GAPDH (or TUBA) ratio caused by treatment of the cells with 25 µM chloroquine diphosphate (CQ; Millipore Sigma, 25,745) to inhibit lysosomal protein degradation [ ].

    Techniques: Expressing, Incubation, Transduction, Plasmid Preparation, Fluorescence, Microscopy

    Autophagy caused by MTOR inhibition does not require MAPK8/9 in immortalized MEFs. (a) The amount of RPS6KB1, p-Thr389 RPS6KB1, and TUBA (tubulin alpha) in WT and mapk8 −/- mapk9 −/- immortalized MEFs after incubation without or with 250 nM torin 1 (2 or 4 h) was examined by immunoblot analysis. (b) WT and mapk8 −/- mapk9 −/- immortalized MEFs were transduced with a lentivirus vector that expresses GFP-LC3B. Puncta formation following incubation of the cells with 250 nM torin 1 (2 and 4 h) was examined by fluorescence microscopy. Scale bar: 30 µm. (c) LC3B and GAPDH (glyceraldehyde-3-phosphate dehydrogenase) expression by WT and mapk8 −/- mapk9 −/- immortalized MEFs after incubation (2 h) without or with 250 nM torin 1 in the absence or presence of 25 µM chloroquine (CQ) was examined by immunoblot analysis. The LC3B-II:GAPDH ratios were normalized to the mean of WT control condition (first lane). The ‘Change in MAP1LC3B-II’ was calculated by subtracting MAP1LC3B-II:GAPDH (media+ CQ condition) from MAP1LC3B-II:GAPDH (torin 1+ CQ condition). The data presented represent the mean ± SEM; n = 3 independent experiments; *, p

    Journal: Autophagy

    Article Title: Role of the MAPK/cJun NH2-terminal kinase signaling pathway in starvation-induced autophagy

    doi: 10.1080/15548627.2018.1466013

    Figure Lengend Snippet: Autophagy caused by MTOR inhibition does not require MAPK8/9 in immortalized MEFs. (a) The amount of RPS6KB1, p-Thr389 RPS6KB1, and TUBA (tubulin alpha) in WT and mapk8 −/- mapk9 −/- immortalized MEFs after incubation without or with 250 nM torin 1 (2 or 4 h) was examined by immunoblot analysis. (b) WT and mapk8 −/- mapk9 −/- immortalized MEFs were transduced with a lentivirus vector that expresses GFP-LC3B. Puncta formation following incubation of the cells with 250 nM torin 1 (2 and 4 h) was examined by fluorescence microscopy. Scale bar: 30 µm. (c) LC3B and GAPDH (glyceraldehyde-3-phosphate dehydrogenase) expression by WT and mapk8 −/- mapk9 −/- immortalized MEFs after incubation (2 h) without or with 250 nM torin 1 in the absence or presence of 25 µM chloroquine (CQ) was examined by immunoblot analysis. The LC3B-II:GAPDH ratios were normalized to the mean of WT control condition (first lane). The ‘Change in MAP1LC3B-II’ was calculated by subtracting MAP1LC3B-II:GAPDH (media+ CQ condition) from MAP1LC3B-II:GAPDH (torin 1+ CQ condition). The data presented represent the mean ± SEM; n = 3 independent experiments; *, p

    Article Snippet: Autophagic flux was examined by measuring the LC3B-II:GAPDH ratio or LC3B-II:TUBA (tubulin alpha) ratio by immunoblot analysis, normalization of the data to the control condition (without autophagy induction or CQ), and calculation of the increased LC3B-II:GAPDH (or TUBA) ratio caused by treatment of the cells with 25 µM chloroquine diphosphate (CQ; Millipore Sigma, 25,745) to inhibit lysosomal protein degradation [ ].

    Techniques: Inhibition, Incubation, Transduction, Plasmid Preparation, Fluorescence, Microscopy, Expressing

    Autophagy caused by starvation does not require MAPK8/9 in primary MEFs. (a) (Z)-4-Hydroxytamoxifen-treated primary Rosa- Cre ERT (WT) MEFs and Rosa- Cre ERT Mapk8 LoxP/LoxP mapk9 −/- MEFs were examined by immunoblot analysis by probing with antibodies to MAPK8/9 and TUBA. (b) WT and mapk8 −/- mapk9 −/- primary MEFs were transduced with a lentivirus vector that expresses GFP-LC3B. Puncta formation following incubation with EBSS containing 5 mM glucose (2 and 4 h) was examined by fluorescence microscopy. Scale bar: 25 µm. (c) LC3B and GAPDH expression by WT and mapk8 −/- mapk9 −/- primary MEFs after incubation (2 h) in medium or with EBSS containing 5 mM glucose in the presence or absence of 25 µM chloroquine (CQ) was examined by immunoblot analysis. The LC3B-II:GAPDH ratios were normalized to the mean of WT control (first lane). The data presented represent the mean ± SEM; n = 3 independent experiments; *, p

    Journal: Autophagy

    Article Title: Role of the MAPK/cJun NH2-terminal kinase signaling pathway in starvation-induced autophagy

    doi: 10.1080/15548627.2018.1466013

    Figure Lengend Snippet: Autophagy caused by starvation does not require MAPK8/9 in primary MEFs. (a) (Z)-4-Hydroxytamoxifen-treated primary Rosa- Cre ERT (WT) MEFs and Rosa- Cre ERT Mapk8 LoxP/LoxP mapk9 −/- MEFs were examined by immunoblot analysis by probing with antibodies to MAPK8/9 and TUBA. (b) WT and mapk8 −/- mapk9 −/- primary MEFs were transduced with a lentivirus vector that expresses GFP-LC3B. Puncta formation following incubation with EBSS containing 5 mM glucose (2 and 4 h) was examined by fluorescence microscopy. Scale bar: 25 µm. (c) LC3B and GAPDH expression by WT and mapk8 −/- mapk9 −/- primary MEFs after incubation (2 h) in medium or with EBSS containing 5 mM glucose in the presence or absence of 25 µM chloroquine (CQ) was examined by immunoblot analysis. The LC3B-II:GAPDH ratios were normalized to the mean of WT control (first lane). The data presented represent the mean ± SEM; n = 3 independent experiments; *, p

    Article Snippet: Autophagic flux was examined by measuring the LC3B-II:GAPDH ratio or LC3B-II:TUBA (tubulin alpha) ratio by immunoblot analysis, normalization of the data to the control condition (without autophagy induction or CQ), and calculation of the increased LC3B-II:GAPDH (or TUBA) ratio caused by treatment of the cells with 25 µM chloroquine diphosphate (CQ; Millipore Sigma, 25,745) to inhibit lysosomal protein degradation [ ].

    Techniques: Transduction, Plasmid Preparation, Incubation, Fluorescence, Microscopy, Expressing

    Effect of starvation and MTOR inhibition on MAPK8/9 activation is not sufficient to cause autophagy. (a and b) MAPK8/9 activation in immortalized MEFs was examined by immunoblot analysis of p-Thr183/Tyr185 MAPK8/9, MAPK8/9, and GAPDH in cells after incubation (2 or 4 h) with EBSS containing 5 mM glucose (a) or 250 nM torin 1 (b). Lanes 1 and 2 represent positive and negative controls: lysates of WT MEFs exposed to 60 J/m 2 UV and mapk8 −/- mapk9 −/- MEFs, respectively. (c) WT and mapk8 −/- mapk9 −/- immortalized MEFs were exposed to UV radiation (60 J/m 2 ) and cell extracts were prepared at 45 min post-irradiation. The expression of LC3B, p-Thr183/Tyr185 MAPK8/9, MAPK8/9, and GAPDH was examined by immunoblot analysis.

    Journal: Autophagy

    Article Title: Role of the MAPK/cJun NH2-terminal kinase signaling pathway in starvation-induced autophagy

    doi: 10.1080/15548627.2018.1466013

    Figure Lengend Snippet: Effect of starvation and MTOR inhibition on MAPK8/9 activation is not sufficient to cause autophagy. (a and b) MAPK8/9 activation in immortalized MEFs was examined by immunoblot analysis of p-Thr183/Tyr185 MAPK8/9, MAPK8/9, and GAPDH in cells after incubation (2 or 4 h) with EBSS containing 5 mM glucose (a) or 250 nM torin 1 (b). Lanes 1 and 2 represent positive and negative controls: lysates of WT MEFs exposed to 60 J/m 2 UV and mapk8 −/- mapk9 −/- MEFs, respectively. (c) WT and mapk8 −/- mapk9 −/- immortalized MEFs were exposed to UV radiation (60 J/m 2 ) and cell extracts were prepared at 45 min post-irradiation. The expression of LC3B, p-Thr183/Tyr185 MAPK8/9, MAPK8/9, and GAPDH was examined by immunoblot analysis.

    Article Snippet: Autophagic flux was examined by measuring the LC3B-II:GAPDH ratio or LC3B-II:TUBA (tubulin alpha) ratio by immunoblot analysis, normalization of the data to the control condition (without autophagy induction or CQ), and calculation of the increased LC3B-II:GAPDH (or TUBA) ratio caused by treatment of the cells with 25 µM chloroquine diphosphate (CQ; Millipore Sigma, 25,745) to inhibit lysosomal protein degradation [ ].

    Techniques: Inhibition, Activation Assay, Incubation, Irradiation, Expressing