recombinant prdx5 Search Results


recombinant prdx5 protein  (ChinaPeptides)
90
ChinaPeptides recombinant prdx5 protein
Target identification of MY in protecting oxidative damage in TBHP‐treated C2C12 myotubes. (A) The structure of the probe MY‐P. (B) Pull‐down labeling with MY‐P in C2C12 myotubes. CBB: Coomassie Brilliant Blue. (C) Volcano plot of MY‐P binding proteins compared with control group (10 µM MY‐P). (D) Pull‐down/Western blotting identified the target protein <t>PRDX5.</t> (E) The PRDX5 expression in Gast muscle from young or aged mice. ## p < 0.01, young versus aged. ** p < 0.01, aged versus aged+MY.L. && p < 0.01, aged versus aged+MY.H. (F) The PRDX5 expression in TBHP‐treated C2C12 myotubes. ## p < 0.01, vehicle versus TBHP, * p < 0.05, ** p < 0.01, MY versus TBHP. (G) ITC titration of MY (100 µM) into recombinant PRDX5 protein (5 µM). (H) Western blotting‐based CETSA validation of thermal stabilization of PRDX5 in response MY treatment at the concentration from 0 to 100 µM. β‐Actin was used as a control. Data are displayed as mean ± SD, n = 6.
Recombinant Prdx5 Protein, supplied by ChinaPeptides, 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/recombinant+prdx5/recombinant+prdx5+protein/pmc11167181-266-7-12
Average 90 stars, based on 1 article reviews
recombinant prdx5 protein - by Bioz Stars, 2026-09
90/100 stars
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peroxiredoxin 5  (ProSci Incorporated)
90
ProSci Incorporated peroxiredoxin 5
Target identification of MY in protecting oxidative damage in TBHP‐treated C2C12 myotubes. (A) The structure of the probe MY‐P. (B) Pull‐down labeling with MY‐P in C2C12 myotubes. CBB: Coomassie Brilliant Blue. (C) Volcano plot of MY‐P binding proteins compared with control group (10 µM MY‐P). (D) Pull‐down/Western blotting identified the target protein <t>PRDX5.</t> (E) The PRDX5 expression in Gast muscle from young or aged mice. ## p < 0.01, young versus aged. ** p < 0.01, aged versus aged+MY.L. && p < 0.01, aged versus aged+MY.H. (F) The PRDX5 expression in TBHP‐treated C2C12 myotubes. ## p < 0.01, vehicle versus TBHP, * p < 0.05, ** p < 0.01, MY versus TBHP. (G) ITC titration of MY (100 µM) into recombinant PRDX5 protein (5 µM). (H) Western blotting‐based CETSA validation of thermal stabilization of PRDX5 in response MY treatment at the concentration from 0 to 100 µM. β‐Actin was used as a control. Data are displayed as mean ± SD, n = 6.
Peroxiredoxin 5, supplied by ProSci Incorporated, 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/recombinant+prdx5/Peroxiredoxin-5+Recombinant+Protein/pm30485711-68-16-32
Average 90 stars, based on 1 article reviews
peroxiredoxin 5 - by Bioz Stars, 2026-09
90/100 stars
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recombinant mouse peroxiredoxin 5 prdx5 protein  (Elabscience)
N/A
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recombinant human peroxiredoxin 5 prdx5 protein  (Elabscience)
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peroxiredoxin 5 prdx5 nm 181651 human recombinant protein  (OriGene)
N/A
Recombinant protein of human peroxiredoxin 5 PRDX5 nuclear gene encoding mitochondrial protein transcript variant 2
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recombinant zebrafish prdx5  (Creative BioMart)
N/A
Recombinant Zebrafish PRDX5 full length or partial length protein was expressed.http://www.creativebiomart.net/description_423299_12.htm
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recombinant human peroxiredoxin-5/prdx5  (Beijing Solarbio Science)
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recombinant rat prdx5 protein  (Creative BioMart)
N/A
Recombinant Rat PRDX5 full length or partial length protein was expressed.http://www.creativebiomart.net/Recombinant-Rat-PRDX5-Protein-453485.htm
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prdx5 nm 012021 mouse recombinant protein  (OriGene)
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Purified recombinant protein of Mouse peroxiredoxin 5 Prdx5 with C terminal MYC DDK tag expressed in HEK293T cells 20ug
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recombinant mouse prdx5 protein  (Creative BioMart)
N/A
Recombinant Mouse PRDX5 full length or partial length protein was expressed.http://www.creativebiomart.net/Recombinant-Mouse-PRDX5-Protein-445447.htm
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prdx5 human - recombinant human peroxiredoxin-5  (Aviva Systems)
N/A
PRDX5; Recombinant Human Peroxiredoxin-5; Recombinant Human Peroxiredoxin-5
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recombinant human peroxiredoxin 5/prdx5 protein  (Elabscience Biotechnology)
N/A
Peroxisomes are essential organelles that participate in multiple important metabolic processes, including the β-oxidation of fatty acids, plasmalogen synthesis, and the metabolism of reactive oxygen species (ROS). Peroxiredoxins is overexpressed in breast cancer tissues to
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Image Search Results


Target identification of MY in protecting oxidative damage in TBHP‐treated C2C12 myotubes. (A) The structure of the probe MY‐P. (B) Pull‐down labeling with MY‐P in C2C12 myotubes. CBB: Coomassie Brilliant Blue. (C) Volcano plot of MY‐P binding proteins compared with control group (10 µM MY‐P). (D) Pull‐down/Western blotting identified the target protein PRDX5. (E) The PRDX5 expression in Gast muscle from young or aged mice. ## p < 0.01, young versus aged. ** p < 0.01, aged versus aged+MY.L. && p < 0.01, aged versus aged+MY.H. (F) The PRDX5 expression in TBHP‐treated C2C12 myotubes. ## p < 0.01, vehicle versus TBHP, * p < 0.05, ** p < 0.01, MY versus TBHP. (G) ITC titration of MY (100 µM) into recombinant PRDX5 protein (5 µM). (H) Western blotting‐based CETSA validation of thermal stabilization of PRDX5 in response MY treatment at the concentration from 0 to 100 µM. β‐Actin was used as a control. Data are displayed as mean ± SD, n = 6.

Journal: MedComm

Article Title: Myricanol prevents aging‐related sarcopenia by rescuing mitochondrial dysfunction via targeting peroxiredoxin 5

doi: 10.1002/mco2.566

Figure Lengend Snippet: Target identification of MY in protecting oxidative damage in TBHP‐treated C2C12 myotubes. (A) The structure of the probe MY‐P. (B) Pull‐down labeling with MY‐P in C2C12 myotubes. CBB: Coomassie Brilliant Blue. (C) Volcano plot of MY‐P binding proteins compared with control group (10 µM MY‐P). (D) Pull‐down/Western blotting identified the target protein PRDX5. (E) The PRDX5 expression in Gast muscle from young or aged mice. ## p < 0.01, young versus aged. ** p < 0.01, aged versus aged+MY.L. && p < 0.01, aged versus aged+MY.H. (F) The PRDX5 expression in TBHP‐treated C2C12 myotubes. ## p < 0.01, vehicle versus TBHP, * p < 0.05, ** p < 0.01, MY versus TBHP. (G) ITC titration of MY (100 µM) into recombinant PRDX5 protein (5 µM). (H) Western blotting‐based CETSA validation of thermal stabilization of PRDX5 in response MY treatment at the concentration from 0 to 100 µM. β‐Actin was used as a control. Data are displayed as mean ± SD, n = 6.

Article Snippet: The protein sample, complexed by MY and recombinant PRDX5 protein (synthesized by ChinaPeptides, Shanghai, China), was dialyzed into the ITC buffer overnight.

Techniques: Drug discovery, Labeling, Binding Assay, Control, Western Blot, Expressing, Titration, Recombinant, Biomarker Discovery, Concentration Assay

MY protects C2C12 myotubes against oxidative damage through targeting PRDX5. (A) Protein expression levels of PRDX5, MuRF1, UNG1, and Nrf2 in si‐ Prdx5 and scrambled cells. β‐Actin was used as a loading control. (B) Protein expression level of nuclear Nrf‐2 in si‐ Prdx5 and scrambled cells. Histone H3 was used as the loading control. LDH level (C) and ATP concentration (D) in TBHP‐treated scrambled and si‐ Prdx5 cells. (E) Mitochondrial content in TBHP‐treated scrambled and si‐ Prdx5 cells, assessed by MitoTracker Green staining. (F) Oxygen consumption rate (OCR) and extracellular acidification rate (ECAR) in TBHP‐treated scrambled and si‐ Prdx5 cells, assessed by Seahorse assay. (G) The levels of coprecipitated Nrf2 and UNG1 with PRDX5 in C2C12 myotubes. Data are displayed as mean ± SD, n = 6. # p < 0.05, ## p < 0.01, vehicle versus TBHP. * p < 0.05, ** p < 0.01, TBHP+MY versus TBHP. & p < 0.05, && p < 0.01, si‐ Prdx5 +MY versus scrambled+MY.

Journal: MedComm

Article Title: Myricanol prevents aging‐related sarcopenia by rescuing mitochondrial dysfunction via targeting peroxiredoxin 5

doi: 10.1002/mco2.566

Figure Lengend Snippet: MY protects C2C12 myotubes against oxidative damage through targeting PRDX5. (A) Protein expression levels of PRDX5, MuRF1, UNG1, and Nrf2 in si‐ Prdx5 and scrambled cells. β‐Actin was used as a loading control. (B) Protein expression level of nuclear Nrf‐2 in si‐ Prdx5 and scrambled cells. Histone H3 was used as the loading control. LDH level (C) and ATP concentration (D) in TBHP‐treated scrambled and si‐ Prdx5 cells. (E) Mitochondrial content in TBHP‐treated scrambled and si‐ Prdx5 cells, assessed by MitoTracker Green staining. (F) Oxygen consumption rate (OCR) and extracellular acidification rate (ECAR) in TBHP‐treated scrambled and si‐ Prdx5 cells, assessed by Seahorse assay. (G) The levels of coprecipitated Nrf2 and UNG1 with PRDX5 in C2C12 myotubes. Data are displayed as mean ± SD, n = 6. # p < 0.05, ## p < 0.01, vehicle versus TBHP. * p < 0.05, ** p < 0.01, TBHP+MY versus TBHP. & p < 0.05, && p < 0.01, si‐ Prdx5 +MY versus scrambled+MY.

Article Snippet: The protein sample, complexed by MY and recombinant PRDX5 protein (synthesized by ChinaPeptides, Shanghai, China), was dialyzed into the ITC buffer overnight.

Techniques: Expressing, Control, Concentration Assay, Staining

Cys100 of PRDX5 is critical for binding to MY. (A) Binding sites of MY–PRDX5 by virtual docking analysis. (B) The PRDX5 expression level in PRDX5‐WT and PRDX5‐C100A overexpression C2C12 cell lines, respectively. (C) ROS production. (D) ATP concentration. (E) Protein expression levels of MuRF1, UNG1 and Nrf2 in TBHP‐treated PRDX5‐WT and PRDX5‐C100A overexpression cells. β‐Actin was used as a loading control. (F) Protein expression level of nuclear Nrf‐2 in TBHP‐treated PRDX5‐WT and PRDX5‐C100A overexpression cells. Histone H3 was used as the loading control. Data are shown as mean ± SD, n = 6. # p < 0.05, ## p < 0.01, vehicle versus TBHP. * p < 0.05, ** p < 0.01, TBHP+MY versus TBHP. & p < 0.05, && p < 0.01, WT+MY versus C100+MY. $ p < 0.05, $$ p < 0.01, TBHP versus MY+TBHP.

Journal: MedComm

Article Title: Myricanol prevents aging‐related sarcopenia by rescuing mitochondrial dysfunction via targeting peroxiredoxin 5

doi: 10.1002/mco2.566

Figure Lengend Snippet: Cys100 of PRDX5 is critical for binding to MY. (A) Binding sites of MY–PRDX5 by virtual docking analysis. (B) The PRDX5 expression level in PRDX5‐WT and PRDX5‐C100A overexpression C2C12 cell lines, respectively. (C) ROS production. (D) ATP concentration. (E) Protein expression levels of MuRF1, UNG1 and Nrf2 in TBHP‐treated PRDX5‐WT and PRDX5‐C100A overexpression cells. β‐Actin was used as a loading control. (F) Protein expression level of nuclear Nrf‐2 in TBHP‐treated PRDX5‐WT and PRDX5‐C100A overexpression cells. Histone H3 was used as the loading control. Data are shown as mean ± SD, n = 6. # p < 0.05, ## p < 0.01, vehicle versus TBHP. * p < 0.05, ** p < 0.01, TBHP+MY versus TBHP. & p < 0.05, && p < 0.01, WT+MY versus C100+MY. $ p < 0.05, $$ p < 0.01, TBHP versus MY+TBHP.

Article Snippet: The protein sample, complexed by MY and recombinant PRDX5 protein (synthesized by ChinaPeptides, Shanghai, China), was dialyzed into the ITC buffer overnight.

Techniques: Binding Assay, Expressing, Over Expression, Concentration Assay, Control