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full length trpm7
![H 2 O 2 inhibited mouse and human <t>TRPM7</t> current in a [Mg 2+ ] i -dependent manner without affecting expression on the plasma membrane . (A) Time course of whole-cell currents in the presence of various [Mg 2+ ] i in full-length mTRPM7-overexpressing HEK293 cells. Each symbol represents the mean ± SEM of recordings at [Mg 2+ ] i , which are shown on the right. The currents at 2 min (control; black vertical dashed line) and 6 min (H 2 O 2 ; red vertical dashed line) relative to the mean current at 2 min in the absence of Mg 2+ are plotted in . Each symbol represents the mean ± SEM (vertical bar) of 14, 11, 9, 6, 8, 10, 18, 4, and 6 observations in the absence or presence of 2.8 µM, 7.4 µM, 20.9 µM 0.2 mM, 0.5 mM, 1.0 mM, 2.0 mM, and 5.0 mM [Mg 2+ ] i , respectively. (B) Localization of TRPM7 in full-length mTRPM7-wt–overexpressing HEK293 cells. Control conditions (left), 5-min treatment with H 2 O 2 (500 µM; middle), or NMM (100 µM; right). Confocal images show the localization of TRPM7 (green) and nuclei (blue). Scale bar, 20 µm. (C) The effect of oxidative stress induced by H 2 O 2 on the hTRPM7 current. Representative traces of whole-cell currents showing the time course of the current inhibition by H 2 O 2 (500 µM) in the absence (open circles) or presence (closed circles) of 0.2 mM [Mg 2+ ] i in hTRPM7-expressing HEK293 cells. (D) H 2 O 2 (500 µM) inhibited the hTRPM7 current in the presence of 0.2 mM [Mg 2+ ] i ( n = 6), but not in the absence of intracellular Mg 2+ ( n = 5). Each bar represents the mean ± SEM (vertical bar). *, P = 0.00040 versus control. (E) NMM (100 µM) inhibited the hTRPM7 current in the presence of 0.2 mM [Mg 2+ ] i ( n = 5), but not in the absence of intracellular Mg 2+ ( n = 4). Each bar represents the mean ± SEM (vertical bar). *, P = 0.031 versus control.](https://pub-med-central-images-cdn.bioz.com/pub_med_central_ids_ending_with_9778/pmc08129778/pmc08129778__JGP_202012708_FigS1.jpg)
Full Length Trpm7, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 26 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/full+length+trpm7/Anti-TRPM7+Antibody/pmc08129778-57-2-16
Average 94 stars, based on 26 article reviews
Full Length Trpm7, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 26 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/full+length+trpm7/Anti-TRPM7+Antibody/pmc08129778-57-2-16
Average 94 stars, based on 26 article reviews
full length trpm7 - by Bioz Stars,
2026-10
94/100 stars
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1) Product Images from "The zinc-binding motif of TRPM7 acts as an oxidative stress sensor to regulate its channel activity"
Article Title: The zinc-binding motif of TRPM7 acts as an oxidative stress sensor to regulate its channel activity
Journal: The Journal of General Physiology
doi: 10.1085/jgp.202012708
Figure Legend Snippet: H 2 O 2 inhibited mouse and human TRPM7 current in a [Mg 2+ ] i -dependent manner without affecting expression on the plasma membrane . (A) Time course of whole-cell currents in the presence of various [Mg 2+ ] i in full-length mTRPM7-overexpressing HEK293 cells. Each symbol represents the mean ± SEM of recordings at [Mg 2+ ] i , which are shown on the right. The currents at 2 min (control; black vertical dashed line) and 6 min (H 2 O 2 ; red vertical dashed line) relative to the mean current at 2 min in the absence of Mg 2+ are plotted in . Each symbol represents the mean ± SEM (vertical bar) of 14, 11, 9, 6, 8, 10, 18, 4, and 6 observations in the absence or presence of 2.8 µM, 7.4 µM, 20.9 µM 0.2 mM, 0.5 mM, 1.0 mM, 2.0 mM, and 5.0 mM [Mg 2+ ] i , respectively. (B) Localization of TRPM7 in full-length mTRPM7-wt–overexpressing HEK293 cells. Control conditions (left), 5-min treatment with H 2 O 2 (500 µM; middle), or NMM (100 µM; right). Confocal images show the localization of TRPM7 (green) and nuclei (blue). Scale bar, 20 µm. (C) The effect of oxidative stress induced by H 2 O 2 on the hTRPM7 current. Representative traces of whole-cell currents showing the time course of the current inhibition by H 2 O 2 (500 µM) in the absence (open circles) or presence (closed circles) of 0.2 mM [Mg 2+ ] i in hTRPM7-expressing HEK293 cells. (D) H 2 O 2 (500 µM) inhibited the hTRPM7 current in the presence of 0.2 mM [Mg 2+ ] i ( n = 6), but not in the absence of intracellular Mg 2+ ( n = 5). Each bar represents the mean ± SEM (vertical bar). *, P = 0.00040 versus control. (E) NMM (100 µM) inhibited the hTRPM7 current in the presence of 0.2 mM [Mg 2+ ] i ( n = 5), but not in the absence of intracellular Mg 2+ ( n = 4). Each bar represents the mean ± SEM (vertical bar). *, P = 0.031 versus control.
Techniques Used: Expressing, Clinical Proteomics, Membrane, Control, Inhibition
![Screening of cysteines in mTRPM7 that were responsible for the oxidative stress–induced inhibition. (A) Schematic diagram of 34 cysteines that are conserved in mTRPM7 and hTRPM7. S1107 and D1510 are also depicted (red dots). (B) Expression of TRPM7-wt and its mutants. Immunoblotting of TRPM7 and calnexin (loading control) was performed with HEK293 whole-cell lysates. Numbers on the left represent molecular mass of standards (in kD). (C) The effect of H 2 O 2 (500 µM) on mutant TRPM7 current at 0.2 mM [Mg 2+ ] i . Each bar represents the mean ± SEM (vertical bar). *, P < 0.05 by unpaired t test versus Dox[−] cells. The number of observations ( n ) and exact P values for each mutant are shown in .](https://pub-med-central-images-cdn.bioz.com/pub_med_central_ids_ending_with_9778/pmc08129778/pmc08129778__JGP_202012708_Fig2.jpg "... are also depicted (red dots). (B) Expression of TRPM7-wt and its mutants. Immunoblotting of TRPM7 and calnexin ...")
Figure Legend Snippet: Screening of cysteines in mTRPM7 that were responsible for the oxidative stress–induced inhibition. (A) Schematic diagram of 34 cysteines that are conserved in mTRPM7 and hTRPM7. S1107 and D1510 are also depicted (red dots). (B) Expression of TRPM7-wt and its mutants. Immunoblotting of TRPM7 and calnexin (loading control) was performed with HEK293 whole-cell lysates. Numbers on the left represent molecular mass of standards (in kD). (C) The effect of H 2 O 2 (500 µM) on mutant TRPM7 current at 0.2 mM [Mg 2+ ] i . Each bar represents the mean ± SEM (vertical bar). *, P < 0.05 by unpaired t test versus Dox[−] cells. The number of observations ( n ) and exact P values for each mutant are shown in .
Techniques Used: Inhibition, Expressing, Western Blot, Control, Mutagenesis
![Localization of TRPM7 or its mutants in HEK293 cells. Representative confocal images showing the localization of TRPM7 (green) in doxycycline-untreated (Dox[−]) and mTRPM7-wt (WT)–, -C721A–, -C738A–, -C721S–, -C738S–, -C1809S–, and -C1813S–expressing HEK293 cells. Phase-contrast images are also shown. Scale bar, 20 µm.](https://pub-med-central-images-cdn.bioz.com/pub_med_central_ids_ending_with_9778/pmc08129778/pmc08129778__JGP_202012708_Fig3.jpg "Localization of TRPM7 or its mutants in HEK293 cells. Representative confocal ...")
Figure Legend Snippet: Localization of TRPM7 or its mutants in HEK293 cells. Representative confocal images showing the localization of TRPM7 (green) in doxycycline-untreated (Dox[−]) and mTRPM7-wt (WT)–, -C721A–, -C738A–, -C721S–, -C738S–, -C1809S–, and -C1813S–expressing HEK293 cells. Phase-contrast images are also shown. Scale bar, 20 µm.
Techniques Used: Expressing
![Functional expression of the M7cd in HEK293 cells. (A) Time course of M7cd currents in the absence (open circles; n = 15) or presence of 2.8 µM (blue squares; n = 9), 20.9 µM (green triangles; n = 14), and 0.2 mM [Mg 2+ ] i (black circles; n = 16) in HEK293 cells that were treated with doxycycline. Each symbol represents the mean ± SEM (vertical bar). (B) Representative I-V relationship of M7cd current recorded in the presence of various [Mg 2+ ] i at 2 min after break-in. (C) [Mg 2+ ] i -dependent inhibition of M7cd current at 2 min. The current was inhibited by intracellular free Mg 2+ with an IC 50 of 3.0 µM. Each symbol represents the mean ± SEM (vertical bar) of 15, 36, 19, 27, 14, and 20 recordings in the absence or presence of 0.8 µM, 2.8 µM, 7.4 µM, 20.9 µM, and 0.2 mM [Mg 2+ ] i , respectively. The dashed line is the [Mg 2+ ] i -dependent curve of the full-length TRPM7-wt current (from ). (D) M7cd-S1107E current density was similar in the absence (open inversed triangles; n = 10) and presence of 0.2 mM [Mg 2+ ] i (closed inversed triangles; n = 7). Each symbol represents the mean ± SEM (vertical bar). (E) The effect of H 2 O 2 (500 µM) on M7cd current in the absence of intracellular Mg 2+ (open circles). Each symbol represents the mean ± SEM (vertical bar) of 19 recordings. (F) The time course of the M7cd current in the presence of 0.8 µM [Mg 2+ ] i with (red circles; n = 17) or without (black circles; n = 35) H 2 O 2 application at 2 min. Each symbol represents the mean ± SEM (vertical bar). The current decreased over time even in the control conditions (black circles), and repeated-measures ANOVA revealed that H 2 O 2 has no significant effect on the current decrease (degrees of freedom were corrected using the Greenhouse-Geisser estimate of epsilon; P = 0.247).](https://pub-med-central-images-cdn.bioz.com/pub_med_central_ids_ending_with_9778/pmc08129778/pmc08129778__JGP_202012708_Fig4.jpg "... 2+ ] i -dependent curve of the full-length TRPM7-wt current (from ). (D) M7cd-S1107E current density was ...")
Figure Legend Snippet: Functional expression of the M7cd in HEK293 cells. (A) Time course of M7cd currents in the absence (open circles; n = 15) or presence of 2.8 µM (blue squares; n = 9), 20.9 µM (green triangles; n = 14), and 0.2 mM [Mg 2+ ] i (black circles; n = 16) in HEK293 cells that were treated with doxycycline. Each symbol represents the mean ± SEM (vertical bar). (B) Representative I-V relationship of M7cd current recorded in the presence of various [Mg 2+ ] i at 2 min after break-in. (C) [Mg 2+ ] i -dependent inhibition of M7cd current at 2 min. The current was inhibited by intracellular free Mg 2+ with an IC 50 of 3.0 µM. Each symbol represents the mean ± SEM (vertical bar) of 15, 36, 19, 27, 14, and 20 recordings in the absence or presence of 0.8 µM, 2.8 µM, 7.4 µM, 20.9 µM, and 0.2 mM [Mg 2+ ] i , respectively. The dashed line is the [Mg 2+ ] i -dependent curve of the full-length TRPM7-wt current (from ). (D) M7cd-S1107E current density was similar in the absence (open inversed triangles; n = 10) and presence of 0.2 mM [Mg 2+ ] i (closed inversed triangles; n = 7). Each symbol represents the mean ± SEM (vertical bar). (E) The effect of H 2 O 2 (500 µM) on M7cd current in the absence of intracellular Mg 2+ (open circles). Each symbol represents the mean ± SEM (vertical bar) of 19 recordings. (F) The time course of the M7cd current in the presence of 0.8 µM [Mg 2+ ] i with (red circles; n = 17) or without (black circles; n = 35) H 2 O 2 application at 2 min. Each symbol represents the mean ± SEM (vertical bar). The current decreased over time even in the control conditions (black circles), and repeated-measures ANOVA revealed that H 2 O 2 has no significant effect on the current decrease (degrees of freedom were corrected using the Greenhouse-Geisser estimate of epsilon; P = 0.247).
Techniques Used: Functional Assay, Expressing, Inhibition, Control
![Functional reconstitution of the TRPM7 current by coexpression of M7kd in M7cd-expressing cells. (A) Transient expression of M7kd-wt in M7cd-expressing cells resulted in an increase in the M7cd current density that was inhibited by H 2 O 2 (500 µM) in the presence of 0.2 mM [Mg 2+ ] i (closed circles; n = 8), but not in the absence of intracellular Mg 2+ (open circles; n = 9). Each symbol represents the mean ± SEM (vertical bar). (B and C) Representative I-V relationships of the M7cd current that was recorded in M7cd-expressing cells transfected with M7kd-wt in the presence (B) or absence of 0.2 mM [Mg 2+ ] i (C), before (black line) or 4 min after (red line) the application of H 2 O 2 (500 µM). (D) [Mg 2+ ] i -dependent inhibition of M7cd with coexpression of M7kd-wt in the control (black squares) and H 2 O 2 -treated (red squares) conditions. The data fit well with a biphasic concentration–response curve, assuming the fraction of high-affinity inhibition of 0.314 estimated for full-length TRPM7-wt (in ). Under control conditions, the current was inhibited by intracellular free Mg 2+ with an IC 50(1) of 7.6 µM and an IC 50(2) of 986 µM. After H 2 O 2 treatment, the current was inhibited by intracellular free Mg 2+ with an IC 50 of 3.0 µM. Each symbol represents the mean ± SEM (vertical bar) of 28, 9, 13, 16, 19, 12, 5, and 6 observations in the absence or presence of 2.8 µM, 7.4 µM, 20.9 µM, 0.2 mM, 1 mM, 2 mM, and 5 mM [Mg 2+ ] i , respectively. (E) The time course of the M7cd current when M7kd-wt was transfected by either lipofection (closed circles; n = 20) or baculovirus infection (open squares; n = 8) in the presence of 0.2 mM [Mg 2+ ] i . Each symbol represents the mean ± SEM (vertical bar). (F) The effect of H 2 O 2 (500 µM) on the M7cd current in the presence of 0.2 mM [Mg 2+ ] i in cells that were transfected with M7kd-wt by baculovirus infection. Each symbol represents the mean ± SEM (vertical bar) of eight recordings. (G) The effect of NMM (100 µM) on M7cd current in the presence of 0.2 mM [Mg 2+ ] i in cells that were transfected with M7kd-wt by baculovirus infection. Each symbol represents the mean ± SEM (vertical bar) of six recordings. (H) The effect of coexpression with kinase-inactive mutant M7kd-1645R on M7cd current. Each symbol represents the mean ± SEM (vertical bar) of four recordings. (I) The effect of M6kd coexpression on M7cd current. Each symbol represents the mean ± SEM (vertical bar) of eight recordings.](https://pub-med-central-images-cdn.bioz.com/pub_med_central_ids_ending_with_9778/pmc08129778/pmc08129778__JGP_202012708_Fig5.jpg "Functional reconstitution of the TRPM7 current by coexpression of M7kd in M7cd-expressing cells. ...")
Figure Legend Snippet: Functional reconstitution of the TRPM7 current by coexpression of M7kd in M7cd-expressing cells. (A) Transient expression of M7kd-wt in M7cd-expressing cells resulted in an increase in the M7cd current density that was inhibited by H 2 O 2 (500 µM) in the presence of 0.2 mM [Mg 2+ ] i (closed circles; n = 8), but not in the absence of intracellular Mg 2+ (open circles; n = 9). Each symbol represents the mean ± SEM (vertical bar). (B and C) Representative I-V relationships of the M7cd current that was recorded in M7cd-expressing cells transfected with M7kd-wt in the presence (B) or absence of 0.2 mM [Mg 2+ ] i (C), before (black line) or 4 min after (red line) the application of H 2 O 2 (500 µM). (D) [Mg 2+ ] i -dependent inhibition of M7cd with coexpression of M7kd-wt in the control (black squares) and H 2 O 2 -treated (red squares) conditions. The data fit well with a biphasic concentration–response curve, assuming the fraction of high-affinity inhibition of 0.314 estimated for full-length TRPM7-wt (in ). Under control conditions, the current was inhibited by intracellular free Mg 2+ with an IC 50(1) of 7.6 µM and an IC 50(2) of 986 µM. After H 2 O 2 treatment, the current was inhibited by intracellular free Mg 2+ with an IC 50 of 3.0 µM. Each symbol represents the mean ± SEM (vertical bar) of 28, 9, 13, 16, 19, 12, 5, and 6 observations in the absence or presence of 2.8 µM, 7.4 µM, 20.9 µM, 0.2 mM, 1 mM, 2 mM, and 5 mM [Mg 2+ ] i , respectively. (E) The time course of the M7cd current when M7kd-wt was transfected by either lipofection (closed circles; n = 20) or baculovirus infection (open squares; n = 8) in the presence of 0.2 mM [Mg 2+ ] i . Each symbol represents the mean ± SEM (vertical bar). (F) The effect of H 2 O 2 (500 µM) on the M7cd current in the presence of 0.2 mM [Mg 2+ ] i in cells that were transfected with M7kd-wt by baculovirus infection. Each symbol represents the mean ± SEM (vertical bar) of eight recordings. (G) The effect of NMM (100 µM) on M7cd current in the presence of 0.2 mM [Mg 2+ ] i in cells that were transfected with M7kd-wt by baculovirus infection. Each symbol represents the mean ± SEM (vertical bar) of six recordings. (H) The effect of coexpression with kinase-inactive mutant M7kd-1645R on M7cd current. Each symbol represents the mean ± SEM (vertical bar) of four recordings. (I) The effect of M6kd coexpression on M7cd current. Each symbol represents the mean ± SEM (vertical bar) of eight recordings.
Techniques Used: Functional Assay, Expressing, Transfection, Inhibition, Control, Concentration Assay, Infection, Mutagenesis
Figure Legend Snippet: Schematic illustration of TRPM7 regulation by oxidative stress. Left: Under basal conditions, the current inhibition by Mg 2+ binding to the high-affinity site (indicated by an orange arrow) is attenuated possibly via the interdomain interaction between the channel domain and the kinase domain. The structural integrity of the kinase domain is guaranteed by the zinc-binding motif that coordinates Zn 2+ (indicated by brown) via C1809, C1813, H1750, and H1807. For simplicity, the low-affinity Mg 2+ -binding site that is assumed to exist in the kinase domain is not shown here. Right: Oxidative stress causes the oxidation of the cysteines (C1809 and C1813) in the zinc-binding motif, which may disrupt the interaction between the channel domain and the kinase domain and enhance the inhibition of TRPM7 by intracellular Mg 2+ .
Techniques Used: Inhibition, Binding Assay
Related Articles
Expressing:Article Title: The zinc-binding motif of TRPM7 acts as an oxidative stress sensor to regulate its channel activity Article Snippet: Proteins in the HEK293 whole-cell lysates were separated by SDS-PAGE using 3–15% linear gradient gels and electrophoretically transferred onto polyvinylidene difluoride membranes.Proteins in the HEK293 whole-cell lysates were separated by SDS-PAGE using 3–15% linear gradient gels and electrophoretically transferred onto polyvinylidene difluoride membranes.. To detect Clinical Proteomics:Article Title: The zinc-binding motif of TRPM7 acts as an oxidative stress sensor to regulate its channel activity Article Snippet: Proteins in the HEK293 whole-cell lysates were separated by SDS-PAGE using 3–15% linear gradient gels and electrophoretically transferred onto polyvinylidene difluoride membranes.Proteins in the HEK293 whole-cell lysates were separated by SDS-PAGE using 3–15% linear gradient gels and electrophoretically transferred onto polyvinylidene difluoride membranes.. To detect Membrane:Article Title: The zinc-binding motif of TRPM7 acts as an oxidative stress sensor to regulate its channel activity Article Snippet: Proteins in the HEK293 whole-cell lysates were separated by SDS-PAGE using 3–15% linear gradient gels and electrophoretically transferred onto polyvinylidene difluoride membranes.Proteins in the HEK293 whole-cell lysates were separated by SDS-PAGE using 3–15% linear gradient gels and electrophoretically transferred onto polyvinylidene difluoride membranes.. To detect Control:Article Title: The zinc-binding motif of TRPM7 acts as an oxidative stress sensor to regulate its channel activity Article Snippet: Proteins in the HEK293 whole-cell lysates were separated by SDS-PAGE using 3–15% linear gradient gels and electrophoretically transferred onto polyvinylidene difluoride membranes.Proteins in the HEK293 whole-cell lysates were separated by SDS-PAGE using 3–15% linear gradient gels and electrophoretically transferred onto polyvinylidene difluoride membranes.. To detect Inhibition:Article Title: The zinc-binding motif of TRPM7 acts as an oxidative stress sensor to regulate its channel activity Article Snippet: Proteins in the HEK293 whole-cell lysates were separated by SDS-PAGE using 3–15% linear gradient gels and electrophoretically transferred onto polyvinylidene difluoride membranes.Proteins in the HEK293 whole-cell lysates were separated by SDS-PAGE using 3–15% linear gradient gels and electrophoretically transferred onto polyvinylidene difluoride membranes.. To detect Western Blot:Article Title: The zinc-binding motif of TRPM7 acts as an oxidative stress sensor to regulate its channel activity Article Snippet: Proteins in the HEK293 whole-cell lysates were separated by SDS-PAGE using 3–15% linear gradient gels and electrophoretically transferred onto polyvinylidene difluoride membranes.Proteins in the HEK293 whole-cell lysates were separated by SDS-PAGE using 3–15% linear gradient gels and electrophoretically transferred onto polyvinylidene difluoride membranes.. To detect Mutagenesis:Article Title: The zinc-binding motif of TRPM7 acts as an oxidative stress sensor to regulate its channel activity Article Snippet: Proteins in the HEK293 whole-cell lysates were separated by SDS-PAGE using 3–15% linear gradient gels and electrophoretically transferred onto polyvinylidene difluoride membranes.Proteins in the HEK293 whole-cell lysates were separated by SDS-PAGE using 3–15% linear gradient gels and electrophoretically transferred onto polyvinylidene difluoride membranes.. To detect Functional Assay:Article Title: The zinc-binding motif of TRPM7 acts as an oxidative stress sensor to regulate its channel activity Article Snippet: Proteins in the HEK293 whole-cell lysates were separated by SDS-PAGE using 3–15% linear gradient gels and electrophoretically transferred onto polyvinylidene difluoride membranes.Proteins in the HEK293 whole-cell lysates were separated by SDS-PAGE using 3–15% linear gradient gels and electrophoretically transferred onto polyvinylidene difluoride membranes.. To detect Transfection:Article Title: The zinc-binding motif of TRPM7 acts as an oxidative stress sensor to regulate its channel activity Article Snippet: Proteins in the HEK293 whole-cell lysates were separated by SDS-PAGE using 3–15% linear gradient gels and electrophoretically transferred onto polyvinylidene difluoride membranes.Proteins in the HEK293 whole-cell lysates were separated by SDS-PAGE using 3–15% linear gradient gels and electrophoretically transferred onto polyvinylidene difluoride membranes.. To detect Concentration Assay:Article Title: The zinc-binding motif of TRPM7 acts as an oxidative stress sensor to regulate its channel activity Article Snippet: Proteins in the HEK293 whole-cell lysates were separated by SDS-PAGE using 3–15% linear gradient gels and electrophoretically transferred onto polyvinylidene difluoride membranes.Proteins in the HEK293 whole-cell lysates were separated by SDS-PAGE using 3–15% linear gradient gels and electrophoretically transferred onto polyvinylidene difluoride membranes.. To detect Infection:Article Title: The zinc-binding motif of TRPM7 acts as an oxidative stress sensor to regulate its channel activity Article Snippet: Proteins in the HEK293 whole-cell lysates were separated by SDS-PAGE using 3–15% linear gradient gels and electrophoretically transferred onto polyvinylidene difluoride membranes.Proteins in the HEK293 whole-cell lysates were separated by SDS-PAGE using 3–15% linear gradient gels and electrophoretically transferred onto polyvinylidene difluoride membranes.. To detect Binding Assay:Article Title: The zinc-binding motif of TRPM7 acts as an oxidative stress sensor to regulate its channel activity Article Snippet: Proteins in the HEK293 whole-cell lysates were separated by SDS-PAGE using 3–15% linear gradient gels and electrophoretically transferred onto polyvinylidene difluoride membranes.Proteins in the HEK293 whole-cell lysates were separated by SDS-PAGE using 3–15% linear gradient gels and electrophoretically transferred onto polyvinylidene difluoride membranes.. To detect |