Review



criterion tgx stain  (Bio-Rad)


Bioz Verified Symbol Bio-Rad is a verified supplier  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 96

    Structured Review

    Bio-Rad criterion tgx stain
    Relative HSP abundances in whole skeletal muscle homogenates from young adults and older adults pre and post HIT exercise. Representative Westen blots of (A) HSP72, HSP27, and αB-crystallin and (B) phosphorylated HSP27 Ser15 (pHSP27 Ser15) and pαB-crystallin Ser59 in whole muscle homogenates from the vastus lateralis of the same individuals. Calibration curves of mixed muscle homogenates are indicated and were used to determine the relative number of given proteins (see <t>Methods).</t> <t>Stain-free</t> gels are indicative of total protein loading, and molecular weights are indicated by markers collected under white light capture without moving the membrane between that and chemiluminescence detection. Relative abundances of (C) HSP72, (D) HSP27, (E) pHSP27 Ser15, (F) αB-crystallin, and (G) pαB-crystallin Ser59 from young (circle) and older adults Pre (square) and older adults Post (triangle) HIT exercise are shown relative to average Old (pre) on a given gel (data are presented as mean ± SD). Individuals indicated by the number of symbols ( n : 5–7), with the same color assigned to the same individual and consistent across all graphs. * p ≤ 0.05 indicates Brown-Forsye and Welch’s and post hoc analysis using Games-Horwell. HIT = high-intensity training; HSP = heat shock protein; pαB-crystallin Ser59 = phospho-αB-crystallin at Serine59; pHSP27 Ser15 = phospho-HSP27 at Serine15.
    Criterion Tgx Stain, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 96/100, based on 397 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/tgx+gels/10%25+Criterion+TGX+Stain-Free+Protein+Gel/pmc12828604-94-8-12
    Average 96 stars, based on 397 article reviews
    criterion tgx stain - by Bioz Stars, 2026-09
    96/100 stars

    Images

    1) Product Images from "Exercise attenuates stress-related signaling as sensed by higher phosphorylation of small heat shock proteins in skeletal muscle from older individuals"

    Article Title: Exercise attenuates stress-related signaling as sensed by higher phosphorylation of small heat shock proteins in skeletal muscle from older individuals

    Journal: Journal of Sport and Health Science

    doi: 10.1016/j.jshs.2025.101111

    Relative HSP abundances in whole skeletal muscle homogenates from young adults and older adults pre and post HIT exercise. Representative Westen blots of (A) HSP72, HSP27, and αB-crystallin and (B) phosphorylated HSP27 Ser15 (pHSP27 Ser15) and pαB-crystallin Ser59 in whole muscle homogenates from the vastus lateralis of the same individuals. Calibration curves of mixed muscle homogenates are indicated and were used to determine the relative number of given proteins (see Methods). Stain-free gels are indicative of total protein loading, and molecular weights are indicated by markers collected under white light capture without moving the membrane between that and chemiluminescence detection. Relative abundances of (C) HSP72, (D) HSP27, (E) pHSP27 Ser15, (F) αB-crystallin, and (G) pαB-crystallin Ser59 from young (circle) and older adults Pre (square) and older adults Post (triangle) HIT exercise are shown relative to average Old (pre) on a given gel (data are presented as mean ± SD). Individuals indicated by the number of symbols ( n : 5–7), with the same color assigned to the same individual and consistent across all graphs. * p ≤ 0.05 indicates Brown-Forsye and Welch’s and post hoc analysis using Games-Horwell. HIT = high-intensity training; HSP = heat shock protein; pαB-crystallin Ser59 = phospho-αB-crystallin at Serine59; pHSP27 Ser15 = phospho-HSP27 at Serine15.
    Figure Legend Snippet: Relative HSP abundances in whole skeletal muscle homogenates from young adults and older adults pre and post HIT exercise. Representative Westen blots of (A) HSP72, HSP27, and αB-crystallin and (B) phosphorylated HSP27 Ser15 (pHSP27 Ser15) and pαB-crystallin Ser59 in whole muscle homogenates from the vastus lateralis of the same individuals. Calibration curves of mixed muscle homogenates are indicated and were used to determine the relative number of given proteins (see Methods). Stain-free gels are indicative of total protein loading, and molecular weights are indicated by markers collected under white light capture without moving the membrane between that and chemiluminescence detection. Relative abundances of (C) HSP72, (D) HSP27, (E) pHSP27 Ser15, (F) αB-crystallin, and (G) pαB-crystallin Ser59 from young (circle) and older adults Pre (square) and older adults Post (triangle) HIT exercise are shown relative to average Old (pre) on a given gel (data are presented as mean ± SD). Individuals indicated by the number of symbols ( n : 5–7), with the same color assigned to the same individual and consistent across all graphs. * p ≤ 0.05 indicates Brown-Forsye and Welch’s and post hoc analysis using Games-Horwell. HIT = high-intensity training; HSP = heat shock protein; pαB-crystallin Ser59 = phospho-αB-crystallin at Serine59; pHSP27 Ser15 = phospho-HSP27 at Serine15.

    Techniques Used: Staining, Membrane

    HSP abundances in type I and II skeletal muscle fibers from young and older adults. (A, C, and F) The MHC isoform present was determined in individual muscle fiber segments from the vastus lateralis and, following pooling into type I and type II groups from a given biopsy, were analyzed by Westen blotting. Westen blots of (A) HSP72, (C) HSP27 and pHSP27 Ser15, (F) αB-crystallin and pαB-crystallin Ser59, with MHC isoforms in groups of fibers. Stain-free gels are indicative of total protein loading, and molecular weights are indicated by markers collected under white light capture without moving the membrane between that and chemiluminescence detection. Calibration curves of mixed muscle homogenates are indicated. Relative protein abundances of (B) HSP72, (D) HSP27, (E) pHSP27 Ser15, (G) αB-crystallin, and (H) pαB-crystallin Ser59 in fibers from young (circle) and older adults (square) type I fibers (no outline) and type II fibers (outline). All fibers are expressed relative to the average older adult’s type I fibers. The same color is assigned to the same individual and is consistent with (data are presented as mean ± SD). * p < 0.05 and ** p < 0.01, mixed effect model Univariant using either Tukey’s or Games-Horwell’s multiple comparison test (see Methods). HIT = high-intensity training; HSP = heat shock protein; MHC = myosin heavy chain; pαB-crystallin Ser59 = phospho-αB-crystallin at Serine59; pHSP27 Ser15 = phospho-HSP27 at Serine15.
    Figure Legend Snippet: HSP abundances in type I and II skeletal muscle fibers from young and older adults. (A, C, and F) The MHC isoform present was determined in individual muscle fiber segments from the vastus lateralis and, following pooling into type I and type II groups from a given biopsy, were analyzed by Westen blotting. Westen blots of (A) HSP72, (C) HSP27 and pHSP27 Ser15, (F) αB-crystallin and pαB-crystallin Ser59, with MHC isoforms in groups of fibers. Stain-free gels are indicative of total protein loading, and molecular weights are indicated by markers collected under white light capture without moving the membrane between that and chemiluminescence detection. Calibration curves of mixed muscle homogenates are indicated. Relative protein abundances of (B) HSP72, (D) HSP27, (E) pHSP27 Ser15, (G) αB-crystallin, and (H) pαB-crystallin Ser59 in fibers from young (circle) and older adults (square) type I fibers (no outline) and type II fibers (outline). All fibers are expressed relative to the average older adult’s type I fibers. The same color is assigned to the same individual and is consistent with (data are presented as mean ± SD). * p < 0.05 and ** p < 0.01, mixed effect model Univariant using either Tukey’s or Games-Horwell’s multiple comparison test (see Methods). HIT = high-intensity training; HSP = heat shock protein; MHC = myosin heavy chain; pαB-crystallin Ser59 = phospho-αB-crystallin at Serine59; pHSP27 Ser15 = phospho-HSP27 at Serine15.

    Techniques Used: Staining, Membrane, Comparison

    Related Articles

    Staining:

    Article Title: The Nuclear Effector RIRG190 Interacts with SAS10 to Regulate Arbuscular Mycorrhizal Symbiosis
    Article Snippet: Total protein content was determined using the Qubit protein assay kit as described by the manufacturer (Invitrogen, USA). .. Proteins were separated on a 4–12% gradient Mini-PROTEAN stain-free TGX gels (Bio-Rad, USA) and transferred to a polyvinylidene difluoride membrane. ..

    Article Title: A Bifunctional T3SS-Effector Simultaneously Cleaves Host MAP Kinase and Inhibits PPM1A Phosphatase.
    Article Snippet: .. Protein extracts were separated on Stain-Free TGX gels (Bio-Rad 456–8046) by SDS-PAGE. ..

    Membrane:

    Article Title: The Nuclear Effector RIRG190 Interacts with SAS10 to Regulate Arbuscular Mycorrhizal Symbiosis
    Article Snippet: Total protein content was determined using the Qubit protein assay kit as described by the manufacturer (Invitrogen, USA). .. Proteins were separated on a 4–12% gradient Mini-PROTEAN stain-free TGX gels (Bio-Rad, USA) and transferred to a polyvinylidene difluoride membrane. ..

    Electrophoresis:

    Article Title: Tumor microenvironment–targeted PROTAC nanoparticle self-assembly broadly predicted by structural descriptors
    Article Snippet: .. Thirty micrograms of protein was loaded into Criterion 4-20% TGX gels (Bio-Rad), resolved via electrophoresis, and then transferred to polyvinylidene difluoride membranes (Bio-Rad). .. The following primary antibodies were used in this work: BRD4 (E2A7X), β-actin (D6A8), MEK 1/2 (D1A5), pMEK1/2 (41G9), and ERK 1/2 (9102) from Cell Signaling Technology.

    Article Title: Tumor microenvironment-targeted PROTAC nanoparticle self-assembly broadly predicted by structural descriptors.
    Article Snippet: .. Thirty micrograms of protein was loaded into Criterion 4- 20% TGX gels (Bio- Rad), resolved via electrophoresis, and then transferred to polyvinylidene difluoride membranes (Bio- Rad). .. The following primary antibodies were used in this work: BRD4 (E2A7X), β- actin (D6A8), MEK 1/2 (D1A5), pMEK1/2 (41G9), and ERK 1/2 (9102) from Cell Signaling Technology.

    Nucleic Acid Electrophoresis:

    Article Title: Deletion of neuronal Idol ameliorates Alzheimer's disease–related pathologies via APOE receptors
    Article Snippet: .. Equal amounts of protein (10 μg) were loaded onto 4%–20% TGX gels (Bio‐Rad, Cat #5671095), separated by gel electrophoresis, and transferred onto polyvinylidene difluoride (PVDF) membranes. .. The membranes were probed with antibodies against LDLR (MBL, JM‐3839‐100, 1:2000), APOE (Abclonal, A16344, 1:1000), APOER2 (Abcam, ab108208, 1:1000), VLDLR (R&D Systems, AF2258, 1:1000), or β‐actin (Sigma, A1978, 1:20,000).



    Similar Products

    96
    Bio-Rad criterion tgx stain
    Relative HSP abundances in whole skeletal muscle homogenates from young adults and older adults pre and post HIT exercise. Representative Westen blots of (A) HSP72, HSP27, and αB-crystallin and (B) phosphorylated HSP27 Ser15 (pHSP27 Ser15) and pαB-crystallin Ser59 in whole muscle homogenates from the vastus lateralis of the same individuals. Calibration curves of mixed muscle homogenates are indicated and were used to determine the relative number of given proteins (see <t>Methods).</t> <t>Stain-free</t> gels are indicative of total protein loading, and molecular weights are indicated by markers collected under white light capture without moving the membrane between that and chemiluminescence detection. Relative abundances of (C) HSP72, (D) HSP27, (E) pHSP27 Ser15, (F) αB-crystallin, and (G) pαB-crystallin Ser59 from young (circle) and older adults Pre (square) and older adults Post (triangle) HIT exercise are shown relative to average Old (pre) on a given gel (data are presented as mean ± SD). Individuals indicated by the number of symbols ( n : 5–7), with the same color assigned to the same individual and consistent across all graphs. * p ≤ 0.05 indicates Brown-Forsye and Welch’s and post hoc analysis using Games-Horwell. HIT = high-intensity training; HSP = heat shock protein; pαB-crystallin Ser59 = phospho-αB-crystallin at Serine59; pHSP27 Ser15 = phospho-HSP27 at Serine15.
    Criterion Tgx Stain, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/tgx+gels/10%25+Criterion+TGX+Stain-Free+Protein+Gel/pmc12828604-94-8-12
    Average 96 stars, based on 1 article reviews
    criterion tgx stain - by Bioz Stars, 2026-09
    96/100 stars
      Buy from Supplier

    96
    Bio-Rad sds page gel
    Relative HSP abundances in whole skeletal muscle homogenates from young adults and older adults pre and post HIT exercise. Representative Westen blots of (A) HSP72, HSP27, and αB-crystallin and (B) phosphorylated HSP27 Ser15 (pHSP27 Ser15) and pαB-crystallin Ser59 in whole muscle homogenates from the vastus lateralis of the same individuals. Calibration curves of mixed muscle homogenates are indicated and were used to determine the relative number of given proteins (see <t>Methods).</t> <t>Stain-free</t> gels are indicative of total protein loading, and molecular weights are indicated by markers collected under white light capture without moving the membrane between that and chemiluminescence detection. Relative abundances of (C) HSP72, (D) HSP27, (E) pHSP27 Ser15, (F) αB-crystallin, and (G) pαB-crystallin Ser59 from young (circle) and older adults Pre (square) and older adults Post (triangle) HIT exercise are shown relative to average Old (pre) on a given gel (data are presented as mean ± SD). Individuals indicated by the number of symbols ( n : 5–7), with the same color assigned to the same individual and consistent across all graphs. * p ≤ 0.05 indicates Brown-Forsye and Welch’s and post hoc analysis using Games-Horwell. HIT = high-intensity training; HSP = heat shock protein; pαB-crystallin Ser59 = phospho-αB-crystallin at Serine59; pHSP27 Ser15 = phospho-HSP27 at Serine15.
    Sds Page Gel, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/tgx+gels/TGX+FastCast+Acrylamide+Kit/pmc13123334-28-1-4
    Average 96 stars, based on 1 article reviews
    sds page gel - by Bioz Stars, 2026-09
    96/100 stars
      Buy from Supplier

    99
    Bio-Rad mini protean tgx precast protein gels
    Relative HSP abundances in whole skeletal muscle homogenates from young adults and older adults pre and post HIT exercise. Representative Westen blots of (A) HSP72, HSP27, and αB-crystallin and (B) phosphorylated HSP27 Ser15 (pHSP27 Ser15) and pαB-crystallin Ser59 in whole muscle homogenates from the vastus lateralis of the same individuals. Calibration curves of mixed muscle homogenates are indicated and were used to determine the relative number of given proteins (see <t>Methods).</t> <t>Stain-free</t> gels are indicative of total protein loading, and molecular weights are indicated by markers collected under white light capture without moving the membrane between that and chemiluminescence detection. Relative abundances of (C) HSP72, (D) HSP27, (E) pHSP27 Ser15, (F) αB-crystallin, and (G) pαB-crystallin Ser59 from young (circle) and older adults Pre (square) and older adults Post (triangle) HIT exercise are shown relative to average Old (pre) on a given gel (data are presented as mean ± SD). Individuals indicated by the number of symbols ( n : 5–7), with the same color assigned to the same individual and consistent across all graphs. * p ≤ 0.05 indicates Brown-Forsye and Welch’s and post hoc analysis using Games-Horwell. HIT = high-intensity training; HSP = heat shock protein; pαB-crystallin Ser59 = phospho-αB-crystallin at Serine59; pHSP27 Ser15 = phospho-HSP27 at Serine15.
    Mini Protean Tgx Precast Protein Gels, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/tgx+gels/MINI-PROTEAN+TGX/pmc13101689-161-11-16
    Average 99 stars, based on 1 article reviews
    mini protean tgx precast protein gels - by Bioz Stars, 2026-09
    99/100 stars
      Buy from Supplier

    96
    Bio-Rad criterion tgx stain free protein gel
    Relative HSP abundances in whole skeletal muscle homogenates from young adults and older adults pre and post HIT exercise. Representative Westen blots of (A) HSP72, HSP27, and αB-crystallin and (B) phosphorylated HSP27 Ser15 (pHSP27 Ser15) and pαB-crystallin Ser59 in whole muscle homogenates from the vastus lateralis of the same individuals. Calibration curves of mixed muscle homogenates are indicated and were used to determine the relative number of given proteins (see <t>Methods).</t> <t>Stain-free</t> gels are indicative of total protein loading, and molecular weights are indicated by markers collected under white light capture without moving the membrane between that and chemiluminescence detection. Relative abundances of (C) HSP72, (D) HSP27, (E) pHSP27 Ser15, (F) αB-crystallin, and (G) pαB-crystallin Ser59 from young (circle) and older adults Pre (square) and older adults Post (triangle) HIT exercise are shown relative to average Old (pre) on a given gel (data are presented as mean ± SD). Individuals indicated by the number of symbols ( n : 5–7), with the same color assigned to the same individual and consistent across all graphs. * p ≤ 0.05 indicates Brown-Forsye and Welch’s and post hoc analysis using Games-Horwell. HIT = high-intensity training; HSP = heat shock protein; pαB-crystallin Ser59 = phospho-αB-crystallin at Serine59; pHSP27 Ser15 = phospho-HSP27 at Serine15.
    Criterion Tgx Stain Free Protein Gel, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/tgx+gels/4%E2%80%9320%25+Criterion+TGX+Stain-Free+Protein+Gel/pmc13051718-444-15-20
    Average 96 stars, based on 1 article reviews
    criterion tgx stain free protein gel - by Bioz Stars, 2026-09
    96/100 stars
      Buy from Supplier

    96
    Bio-Rad criterion tgx precast protein gel
    Relative HSP abundances in whole skeletal muscle homogenates from young adults and older adults pre and post HIT exercise. Representative Westen blots of (A) HSP72, HSP27, and αB-crystallin and (B) phosphorylated HSP27 Ser15 (pHSP27 Ser15) and pαB-crystallin Ser59 in whole muscle homogenates from the vastus lateralis of the same individuals. Calibration curves of mixed muscle homogenates are indicated and were used to determine the relative number of given proteins (see <t>Methods).</t> <t>Stain-free</t> gels are indicative of total protein loading, and molecular weights are indicated by markers collected under white light capture without moving the membrane between that and chemiluminescence detection. Relative abundances of (C) HSP72, (D) HSP27, (E) pHSP27 Ser15, (F) αB-crystallin, and (G) pαB-crystallin Ser59 from young (circle) and older adults Pre (square) and older adults Post (triangle) HIT exercise are shown relative to average Old (pre) on a given gel (data are presented as mean ± SD). Individuals indicated by the number of symbols ( n : 5–7), with the same color assigned to the same individual and consistent across all graphs. * p ≤ 0.05 indicates Brown-Forsye and Welch’s and post hoc analysis using Games-Horwell. HIT = high-intensity training; HSP = heat shock protein; pαB-crystallin Ser59 = phospho-αB-crystallin at Serine59; pHSP27 Ser15 = phospho-HSP27 at Serine15.
    Criterion Tgx Precast Protein Gel, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/tgx+gels/10%25+Criterion+TGX+Precast+Midi+Protein+Gel/pmc13148909-279-6-11
    Average 96 stars, based on 1 article reviews
    criterion tgx precast protein gel - by Bioz Stars, 2026-09
    96/100 stars
      Buy from Supplier

    99
    Bio-Rad mini protean tgx precast gels
    Relative HSP abundances in whole skeletal muscle homogenates from young adults and older adults pre and post HIT exercise. Representative Westen blots of (A) HSP72, HSP27, and αB-crystallin and (B) phosphorylated HSP27 Ser15 (pHSP27 Ser15) and pαB-crystallin Ser59 in whole muscle homogenates from the vastus lateralis of the same individuals. Calibration curves of mixed muscle homogenates are indicated and were used to determine the relative number of given proteins (see <t>Methods).</t> <t>Stain-free</t> gels are indicative of total protein loading, and molecular weights are indicated by markers collected under white light capture without moving the membrane between that and chemiluminescence detection. Relative abundances of (C) HSP72, (D) HSP27, (E) pHSP27 Ser15, (F) αB-crystallin, and (G) pαB-crystallin Ser59 from young (circle) and older adults Pre (square) and older adults Post (triangle) HIT exercise are shown relative to average Old (pre) on a given gel (data are presented as mean ± SD). Individuals indicated by the number of symbols ( n : 5–7), with the same color assigned to the same individual and consistent across all graphs. * p ≤ 0.05 indicates Brown-Forsye and Welch’s and post hoc analysis using Games-Horwell. HIT = high-intensity training; HSP = heat shock protein; pαB-crystallin Ser59 = phospho-αB-crystallin at Serine59; pHSP27 Ser15 = phospho-HSP27 at Serine15.
    Mini Protean Tgx Precast Gels, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/tgx+gels/MINI-PROTEAN+TGX/pmc13144600-84-7-11
    Average 99 stars, based on 1 article reviews
    mini protean tgx precast gels - by Bioz Stars, 2026-09
    99/100 stars
      Buy from Supplier

    99
    Bio-Rad sds polyacrylamide gel
    Purification and biophysical characterization of EEPD1 . A , domain architecture of human EEPD1. B , Coomassie-stained <t>SDS-PAGE</t> gels showing the purified full-length EEPD1 and its nuclease domain, EEPD1 N uc (aa 261–569). C , chromatograms of the final Size-exclusion chromatography (SEC) chromatograms of full-length EEPD1 and EEPD1 N uc . A total of 3 mg of each protein was loaded onto the columns. D , SEC-MALS traces of EEPD1 and EEPD1nuc domain confirming that both proteins form a stable dimers in solution. E , SEC-MALS analysis demonstrating that EEPD1 dimerization is maintained in a reducing environment (2.0 mM DTT).
    Sds Polyacrylamide Gel, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/tgx+gels/MINI-PROTEAN+TGX/pmc13153614-335-11-17
    Average 99 stars, based on 1 article reviews
    sds polyacrylamide gel - by Bioz Stars, 2026-09
    99/100 stars
      Buy from Supplier

    96
    Bio-Rad tgx gel
    Purification and biophysical characterization of EEPD1 . A , domain architecture of human EEPD1. B , Coomassie-stained <t>SDS-PAGE</t> gels showing the purified full-length EEPD1 and its nuclease domain, EEPD1 N uc (aa 261–569). C , chromatograms of the final Size-exclusion chromatography (SEC) chromatograms of full-length EEPD1 and EEPD1 N uc . A total of 3 mg of each protein was loaded onto the columns. D , SEC-MALS traces of EEPD1 and EEPD1nuc domain confirming that both proteins form a stable dimers in solution. E , SEC-MALS analysis demonstrating that EEPD1 dimerization is maintained in a reducing environment (2.0 mM DTT).
    Tgx Gel, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/tgx+gels/TGX+FastCast+Acrylamide+Kit/pmc13124740-61-13-16
    Average 96 stars, based on 1 article reviews
    tgx gel - by Bioz Stars, 2026-09
    96/100 stars
      Buy from Supplier

    99
    Bio-Rad acrylamide gels
    Purification and biophysical characterization of EEPD1 . A , domain architecture of human EEPD1. B , Coomassie-stained <t>SDS-PAGE</t> gels showing the purified full-length EEPD1 and its nuclease domain, EEPD1 N uc (aa 261–569). C , chromatograms of the final Size-exclusion chromatography (SEC) chromatograms of full-length EEPD1 and EEPD1 N uc . A total of 3 mg of each protein was loaded onto the columns. D , SEC-MALS traces of EEPD1 and EEPD1nuc domain confirming that both proteins form a stable dimers in solution. E , SEC-MALS analysis demonstrating that EEPD1 dimerization is maintained in a reducing environment (2.0 mM DTT).
    Acrylamide Gels, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/tgx+gels/MINI-PROTEAN+TGX/pmc13122702-92-14-22
    Average 99 stars, based on 1 article reviews
    acrylamide gels - by Bioz Stars, 2026-09
    99/100 stars
      Buy from Supplier

    99
    Bio-Rad gradient gel
    Purification and biophysical characterization of EEPD1 . A , domain architecture of human EEPD1. B , Coomassie-stained <t>SDS-PAGE</t> gels showing the purified full-length EEPD1 and its nuclease domain, EEPD1 N uc (aa 261–569). C , chromatograms of the final Size-exclusion chromatography (SEC) chromatograms of full-length EEPD1 and EEPD1 N uc . A total of 3 mg of each protein was loaded onto the columns. D , SEC-MALS traces of EEPD1 and EEPD1nuc domain confirming that both proteins form a stable dimers in solution. E , SEC-MALS analysis demonstrating that EEPD1 dimerization is maintained in a reducing environment (2.0 mM DTT).
    Gradient Gel, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/tgx+gels/MINI-PROTEAN+TGX/pmc12908063-89-21-28
    Average 99 stars, based on 1 article reviews
    gradient gel - by Bioz Stars, 2026-09
    99/100 stars
      Buy from Supplier

    Image Search Results


    Relative HSP abundances in whole skeletal muscle homogenates from young adults and older adults pre and post HIT exercise. Representative Westen blots of (A) HSP72, HSP27, and αB-crystallin and (B) phosphorylated HSP27 Ser15 (pHSP27 Ser15) and pαB-crystallin Ser59 in whole muscle homogenates from the vastus lateralis of the same individuals. Calibration curves of mixed muscle homogenates are indicated and were used to determine the relative number of given proteins (see Methods). Stain-free gels are indicative of total protein loading, and molecular weights are indicated by markers collected under white light capture without moving the membrane between that and chemiluminescence detection. Relative abundances of (C) HSP72, (D) HSP27, (E) pHSP27 Ser15, (F) αB-crystallin, and (G) pαB-crystallin Ser59 from young (circle) and older adults Pre (square) and older adults Post (triangle) HIT exercise are shown relative to average Old (pre) on a given gel (data are presented as mean ± SD). Individuals indicated by the number of symbols ( n : 5–7), with the same color assigned to the same individual and consistent across all graphs. * p ≤ 0.05 indicates Brown-Forsye and Welch’s and post hoc analysis using Games-Horwell. HIT = high-intensity training; HSP = heat shock protein; pαB-crystallin Ser59 = phospho-αB-crystallin at Serine59; pHSP27 Ser15 = phospho-HSP27 at Serine15.

    Journal: Journal of Sport and Health Science

    Article Title: Exercise attenuates stress-related signaling as sensed by higher phosphorylation of small heat shock proteins in skeletal muscle from older individuals

    doi: 10.1016/j.jshs.2025.101111

    Figure Lengend Snippet: Relative HSP abundances in whole skeletal muscle homogenates from young adults and older adults pre and post HIT exercise. Representative Westen blots of (A) HSP72, HSP27, and αB-crystallin and (B) phosphorylated HSP27 Ser15 (pHSP27 Ser15) and pαB-crystallin Ser59 in whole muscle homogenates from the vastus lateralis of the same individuals. Calibration curves of mixed muscle homogenates are indicated and were used to determine the relative number of given proteins (see Methods). Stain-free gels are indicative of total protein loading, and molecular weights are indicated by markers collected under white light capture without moving the membrane between that and chemiluminescence detection. Relative abundances of (C) HSP72, (D) HSP27, (E) pHSP27 Ser15, (F) αB-crystallin, and (G) pαB-crystallin Ser59 from young (circle) and older adults Pre (square) and older adults Post (triangle) HIT exercise are shown relative to average Old (pre) on a given gel (data are presented as mean ± SD). Individuals indicated by the number of symbols ( n : 5–7), with the same color assigned to the same individual and consistent across all graphs. * p ≤ 0.05 indicates Brown-Forsye and Welch’s and post hoc analysis using Games-Horwell. HIT = high-intensity training; HSP = heat shock protein; pαB-crystallin Ser59 = phospho-αB-crystallin at Serine59; pHSP27 Ser15 = phospho-HSP27 at Serine15.

    Article Snippet: Total protein was separated on 10% or 4%–15% Criterion TGX stain-free gels (Bio-Rad Laboratories) and run for 45 min at 200 V. Using a wet transfer protocol, protein was transferred to nitrocellulose membranes at 100 V for 30 min. Membranes were incubated in Miser TM solution (ThermoFisher Scientific) and blocked in 5% skim milk powder in tris-buffered saline-tween (TBST).

    Techniques: Staining, Membrane

    HSP abundances in type I and II skeletal muscle fibers from young and older adults. (A, C, and F) The MHC isoform present was determined in individual muscle fiber segments from the vastus lateralis and, following pooling into type I and type II groups from a given biopsy, were analyzed by Westen blotting. Westen blots of (A) HSP72, (C) HSP27 and pHSP27 Ser15, (F) αB-crystallin and pαB-crystallin Ser59, with MHC isoforms in groups of fibers. Stain-free gels are indicative of total protein loading, and molecular weights are indicated by markers collected under white light capture without moving the membrane between that and chemiluminescence detection. Calibration curves of mixed muscle homogenates are indicated. Relative protein abundances of (B) HSP72, (D) HSP27, (E) pHSP27 Ser15, (G) αB-crystallin, and (H) pαB-crystallin Ser59 in fibers from young (circle) and older adults (square) type I fibers (no outline) and type II fibers (outline). All fibers are expressed relative to the average older adult’s type I fibers. The same color is assigned to the same individual and is consistent with (data are presented as mean ± SD). * p < 0.05 and ** p < 0.01, mixed effect model Univariant using either Tukey’s or Games-Horwell’s multiple comparison test (see Methods). HIT = high-intensity training; HSP = heat shock protein; MHC = myosin heavy chain; pαB-crystallin Ser59 = phospho-αB-crystallin at Serine59; pHSP27 Ser15 = phospho-HSP27 at Serine15.

    Journal: Journal of Sport and Health Science

    Article Title: Exercise attenuates stress-related signaling as sensed by higher phosphorylation of small heat shock proteins in skeletal muscle from older individuals

    doi: 10.1016/j.jshs.2025.101111

    Figure Lengend Snippet: HSP abundances in type I and II skeletal muscle fibers from young and older adults. (A, C, and F) The MHC isoform present was determined in individual muscle fiber segments from the vastus lateralis and, following pooling into type I and type II groups from a given biopsy, were analyzed by Westen blotting. Westen blots of (A) HSP72, (C) HSP27 and pHSP27 Ser15, (F) αB-crystallin and pαB-crystallin Ser59, with MHC isoforms in groups of fibers. Stain-free gels are indicative of total protein loading, and molecular weights are indicated by markers collected under white light capture without moving the membrane between that and chemiluminescence detection. Calibration curves of mixed muscle homogenates are indicated. Relative protein abundances of (B) HSP72, (D) HSP27, (E) pHSP27 Ser15, (G) αB-crystallin, and (H) pαB-crystallin Ser59 in fibers from young (circle) and older adults (square) type I fibers (no outline) and type II fibers (outline). All fibers are expressed relative to the average older adult’s type I fibers. The same color is assigned to the same individual and is consistent with (data are presented as mean ± SD). * p < 0.05 and ** p < 0.01, mixed effect model Univariant using either Tukey’s or Games-Horwell’s multiple comparison test (see Methods). HIT = high-intensity training; HSP = heat shock protein; MHC = myosin heavy chain; pαB-crystallin Ser59 = phospho-αB-crystallin at Serine59; pHSP27 Ser15 = phospho-HSP27 at Serine15.

    Article Snippet: Total protein was separated on 10% or 4%–15% Criterion TGX stain-free gels (Bio-Rad Laboratories) and run for 45 min at 200 V. Using a wet transfer protocol, protein was transferred to nitrocellulose membranes at 100 V for 30 min. Membranes were incubated in Miser TM solution (ThermoFisher Scientific) and blocked in 5% skim milk powder in tris-buffered saline-tween (TBST).

    Techniques: Staining, Membrane, Comparison

    Purification and biophysical characterization of EEPD1 . A , domain architecture of human EEPD1. B , Coomassie-stained SDS-PAGE gels showing the purified full-length EEPD1 and its nuclease domain, EEPD1 N uc (aa 261–569). C , chromatograms of the final Size-exclusion chromatography (SEC) chromatograms of full-length EEPD1 and EEPD1 N uc . A total of 3 mg of each protein was loaded onto the columns. D , SEC-MALS traces of EEPD1 and EEPD1nuc domain confirming that both proteins form a stable dimers in solution. E , SEC-MALS analysis demonstrating that EEPD1 dimerization is maintained in a reducing environment (2.0 mM DTT).

    Journal: The Journal of Biological Chemistry

    Article Title: Structural basis for the mechanism and stability of the EEPD1 5′ endonuclease

    doi: 10.1016/j.jbc.2026.111432

    Figure Lengend Snippet: Purification and biophysical characterization of EEPD1 . A , domain architecture of human EEPD1. B , Coomassie-stained SDS-PAGE gels showing the purified full-length EEPD1 and its nuclease domain, EEPD1 N uc (aa 261–569). C , chromatograms of the final Size-exclusion chromatography (SEC) chromatograms of full-length EEPD1 and EEPD1 N uc . A total of 3 mg of each protein was loaded onto the columns. D , SEC-MALS traces of EEPD1 and EEPD1nuc domain confirming that both proteins form a stable dimers in solution. E , SEC-MALS analysis demonstrating that EEPD1 dimerization is maintained in a reducing environment (2.0 mM DTT).

    Article Snippet: The isolated Flag-EEPD1 full length WT sample was loaded onto an SDS polyacrylamide gel (12% Mini-PROTEAN TGX, Bio-Rad Laboratories Inc) and electrophoreses to a distance of 1 cm and stained with Coomassie Brilliant Blue R-250.

    Techniques: Purification, Staining, SDS Page, Size-exclusion Chromatography