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anti p62 c myc  (MedChemExpress)


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    Structured Review

    MedChemExpress anti p62 c myc
    Anti P62 C Myc, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 94/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/anti+myc/MYC%2C+Human/pm42552375-162-13-14
    Average 94 stars, based on 6 article reviews
    anti p62 c myc - by Bioz Stars, 2026-09
    94/100 stars

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    Related Articles

    Incubation:

    Article Title: Snakehead vesiculovirus hijacks SH3RF1 for replication via mediating K63-linked ubiquitination at K264 of the phosphoprotein.
    Article Snippet: Snakehead vesiculovirus (SHVV) is a type of rhabdovirus that causes serious economic losses in snakehead fish culture in China.. However, no specific antiviral drugs or vaccines are currently available for SHVV infection.. In this study, 4D label-free ubiquitome analysis of SHVV-infected cells revealed dozens of ubiquitinated sites on the five SHVV proteins.

    Article Title: p38MAPK- and GSK3-Mediated Phosphorylation of Snakehead Vesiculovirus Phosphoprotein at Threonine 160 Facilitates Viral Replication.
    Article Snippet: Phosphoprotein (P), co-factor of the polymerase (large protein, L) of singlestranded negative-sense RNA viruses, is phosphorylated during viral infection and its phosphorylation has been reported to play important roles in viral replication.. However, the function of P phosphorylation in viral replication is still far from clear.. Snakehead vesiculovirus (SHVV) is a kind of fish rhabdovirus that has caused serious economic losses in snakehead fish culture in China without any effective preventive or therapeutical measures currently.

    Article Title: A novel peptide 66CTG stabilizes Myc proto-oncogene protein to promote triple-negative breast cancer growth.
    Article Snippet: .. The remaining protein sample was incubated with Anti-Flag (MedChemExpress, Cat: HYK0207) or Anti-Myc (MedChemExpress, Cat: HY-K0206) magnetic beads at 4 °C for 4–6 h. The immunoprecipitation (IP) complexes were washed with wash buffer (50 mM Tris-HCl pH 7.4, 150 mM NaCl, 0.1% NP-40, 2 mM EDTA pH 8.0) five times, each lasting 5min with shaking at 4 °C. ..

    Article Title: A novel peptide 66CTG stabilizes Myc proto-oncogene protein to promote triple-negative breast cancer growth
    Article Snippet: .. The remaining protein sample was incubated with Anti-Flag (MedChemExpress, Cat: HY-K0207) or Anti-Myc (MedChemExpress, Cat: HY-K0206) magnetic beads at 4 °C for 4–6 h. The immunoprecipitation (IP) complexes were washed with wash buffer (50 mM Tris-HCl pH 7.4, 150 mM NaCl, 0.1% NP-40, 2 mM EDTA pH 8.0) five times, each lasting 5 min with shaking at 4 °C. ..

    Magnetic Beads:

    Article Title: Snakehead vesiculovirus hijacks SH3RF1 for replication via mediating K63-linked ubiquitination at K264 of the phosphoprotein.
    Article Snippet: Snakehead vesiculovirus (SHVV) is a type of rhabdovirus that causes serious economic losses in snakehead fish culture in China.. However, no specific antiviral drugs or vaccines are currently available for SHVV infection.. In this study, 4D label-free ubiquitome analysis of SHVV-infected cells revealed dozens of ubiquitinated sites on the five SHVV proteins.

    Article Title: Real-time visualization of STAT activation in live cells using genetically encoded biosensors
    Article Snippet: Data were analyzed using FlowJo software. .. Immunoprecipitation was performed using anti-FLAG (MedChemExpress, HY-K0207) and anti-Myc (MedChemExpress, HY-K0206) magnetic beads according to the manufacturer’s instructions. ..

    Article Title: p38MAPK- and GSK3-Mediated Phosphorylation of Snakehead Vesiculovirus Phosphoprotein at Threonine 160 Facilitates Viral Replication.
    Article Snippet: Phosphoprotein (P), co-factor of the polymerase (large protein, L) of singlestranded negative-sense RNA viruses, is phosphorylated during viral infection and its phosphorylation has been reported to play important roles in viral replication.. However, the function of P phosphorylation in viral replication is still far from clear.. Snakehead vesiculovirus (SHVV) is a kind of fish rhabdovirus that has caused serious economic losses in snakehead fish culture in China without any effective preventive or therapeutical measures currently.

    Article Title: A novel peptide 66CTG stabilizes Myc proto-oncogene protein to promote triple-negative breast cancer growth.
    Article Snippet: .. The remaining protein sample was incubated with Anti-Flag (MedChemExpress, Cat: HYK0207) or Anti-Myc (MedChemExpress, Cat: HY-K0206) magnetic beads at 4 °C for 4–6 h. The immunoprecipitation (IP) complexes were washed with wash buffer (50 mM Tris-HCl pH 7.4, 150 mM NaCl, 0.1% NP-40, 2 mM EDTA pH 8.0) five times, each lasting 5min with shaking at 4 °C. ..

    Article Title: A novel peptide 66CTG stabilizes Myc proto-oncogene protein to promote triple-negative breast cancer growth
    Article Snippet: .. The remaining protein sample was incubated with Anti-Flag (MedChemExpress, Cat: HY-K0207) or Anti-Myc (MedChemExpress, Cat: HY-K0206) magnetic beads at 4 °C for 4–6 h. The immunoprecipitation (IP) complexes were washed with wash buffer (50 mM Tris-HCl pH 7.4, 150 mM NaCl, 0.1% NP-40, 2 mM EDTA pH 8.0) five times, each lasting 5 min with shaking at 4 °C. ..

    Article Title: ASCT2 palmitoylation regulated by JNK1-ZDHHC14 axis orchestrates glutamine metabolism and NSCLC progression
    Article Snippet: For Co-IP assays, cells were lysis in NP40 Lysis Buffer (#P0013F, Beyotime) supplemented with protease inhibitor and phosphatase inhibitor. .. Then, the lysates were mixed with anti-Flag, anti-Myc, or anti-HA magnetic beads (#AE061, ABclonal; #HY-K0201, # HY-K0206, MCE) at 4 °C for 4 h and washed with NP40 Lysis Buffer three times, followed by western blot. ..

    Immunoprecipitation:

    Article Title: Real-time visualization of STAT activation in live cells using genetically encoded biosensors
    Article Snippet: Data were analyzed using FlowJo software. .. Immunoprecipitation was performed using anti-FLAG (MedChemExpress, HY-K0207) and anti-Myc (MedChemExpress, HY-K0206) magnetic beads according to the manufacturer’s instructions. ..

    Article Title: A novel peptide 66CTG stabilizes Myc proto-oncogene protein to promote triple-negative breast cancer growth.
    Article Snippet: .. The remaining protein sample was incubated with Anti-Flag (MedChemExpress, Cat: HYK0207) or Anti-Myc (MedChemExpress, Cat: HY-K0206) magnetic beads at 4 °C for 4–6 h. The immunoprecipitation (IP) complexes were washed with wash buffer (50 mM Tris-HCl pH 7.4, 150 mM NaCl, 0.1% NP-40, 2 mM EDTA pH 8.0) five times, each lasting 5min with shaking at 4 °C. ..

    Article Title: A novel peptide 66CTG stabilizes Myc proto-oncogene protein to promote triple-negative breast cancer growth
    Article Snippet: .. The remaining protein sample was incubated with Anti-Flag (MedChemExpress, Cat: HY-K0207) or Anti-Myc (MedChemExpress, Cat: HY-K0206) magnetic beads at 4 °C for 4–6 h. The immunoprecipitation (IP) complexes were washed with wash buffer (50 mM Tris-HCl pH 7.4, 150 mM NaCl, 0.1% NP-40, 2 mM EDTA pH 8.0) five times, each lasting 5 min with shaking at 4 °C. ..

    Binding Assay:

    Article Title: p38MAPK- and GSK3-Mediated Phosphorylation of Snakehead Vesiculovirus Phosphoprotein at Threonine 160 Facilitates Viral Replication.
    Article Snippet: Phosphoprotein (P), co-factor of the polymerase (large protein, L) of singlestranded negative-sense RNA viruses, is phosphorylated during viral infection and its phosphorylation has been reported to play important roles in viral replication.. However, the function of P phosphorylation in viral replication is still far from clear.. Snakehead vesiculovirus (SHVV) is a kind of fish rhabdovirus that has caused serious economic losses in snakehead fish culture in China without any effective preventive or therapeutical measures currently.

    Lysis:

    Article Title: ASCT2 palmitoylation regulated by JNK1-ZDHHC14 axis orchestrates glutamine metabolism and NSCLC progression
    Article Snippet: For Co-IP assays, cells were lysis in NP40 Lysis Buffer (#P0013F, Beyotime) supplemented with protease inhibitor and phosphatase inhibitor. .. Then, the lysates were mixed with anti-Flag, anti-Myc, or anti-HA magnetic beads (#AE061, ABclonal; #HY-K0201, # HY-K0206, MCE) at 4 °C for 4 h and washed with NP40 Lysis Buffer three times, followed by western blot. ..

    Western Blot:

    Article Title: ASCT2 palmitoylation regulated by JNK1-ZDHHC14 axis orchestrates glutamine metabolism and NSCLC progression
    Article Snippet: For Co-IP assays, cells were lysis in NP40 Lysis Buffer (#P0013F, Beyotime) supplemented with protease inhibitor and phosphatase inhibitor. .. Then, the lysates were mixed with anti-Flag, anti-Myc, or anti-HA magnetic beads (#AE061, ABclonal; #HY-K0201, # HY-K0206, MCE) at 4 °C for 4 h and washed with NP40 Lysis Buffer three times, followed by western blot. ..

    other:

    Article Title: Real-time visualization of STAT activation in live cells using genetically encoded biosensors.
    Article Snippet: Transfected HEK-Blue IL-2 cells were lysed on ice using native PAGE sample buffer, supplemented with digitonin (1%, all from the native PAGE sample prep kit; Thermo Fisher Scientific).



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    Wsv156 targets mitochondria via Cq TOMM70 and triggers mito-aggresome formation. ( A ) Wsv156 expression increased following WSSV infection. Temporal expression of wsv156 at the mRNA (left panel) and protein level (right panel) was assessed by RT-qPCR and western blot, respectively, in Hpt cells after WSSV infection. ( B ) Wsv156 localized to mitochondria. Endogenous wsv156 protein in Hpt cells (left panel) and overexpressed wsv156 in HEK 293T cells (right panel) both predominantly co-fractionated with mitochondria. ( C ) Identification of host mitochondrial proteins interacting with wsv156 by affinity purification-mass spectrometry (AP-MS). ( D ) Wsv156 interacted with Cq TOMM70. Co-IP <t>with</t> <t>anti-Myc</t> beads was performed in HEK 293T cells co-transfected with wsv156-Myc and Cq TOMM70-HA. ( E ) Wsv156 expression induced mitochondrial aggregation. Confocal microscopy of HEK 293T cells showed co-localization of wsv156-GFP (green) with the mitochondrial marker Hs COX IV (red). Cells expressing GFP alone or wsv152-GFP served as controls. ( F ) Wsv156 knockdown attenuated WSSV-induced mitochondrial aggregation. Gene silencing of wsv156 in Hpt cells reduced mitochondrial clustering (red) compared to control cells at 12 hpi. NT, non-targeting dsRNA (GFP dsRNA) control; RNAi wsv156, wsv156-specific dsRNA. The right panel quantifies mitochondrial aggregation using the CI and the percentage of cells containing mito-aggresomes. Nuclei were stained with DAPI. **, P < 0.01.
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    Wsv156 targets mitochondria via Cq TOMM70 and triggers mito-aggresome formation. ( A ) Wsv156 expression increased following WSSV infection. Temporal expression of wsv156 at the mRNA (left panel) and protein level (right panel) was assessed by RT-qPCR and western blot, respectively, in Hpt cells after WSSV infection. ( B ) Wsv156 localized to mitochondria. Endogenous wsv156 protein in Hpt cells (left panel) and overexpressed wsv156 in HEK 293T cells (right panel) both predominantly co-fractionated with mitochondria. ( C ) Identification of host mitochondrial proteins interacting with wsv156 by affinity purification-mass spectrometry (AP-MS). ( D ) Wsv156 interacted with Cq TOMM70. Co-IP <t>with</t> <t>anti-Myc</t> beads was performed in HEK 293T cells co-transfected with wsv156-Myc and Cq TOMM70-HA. ( E ) Wsv156 expression induced mitochondrial aggregation. Confocal microscopy of HEK 293T cells showed co-localization of wsv156-GFP (green) with the mitochondrial marker Hs COX IV (red). Cells expressing GFP alone or wsv152-GFP served as controls. ( F ) Wsv156 knockdown attenuated WSSV-induced mitochondrial aggregation. Gene silencing of wsv156 in Hpt cells reduced mitochondrial clustering (red) compared to control cells at 12 hpi. NT, non-targeting dsRNA (GFP dsRNA) control; RNAi wsv156, wsv156-specific dsRNA. The right panel quantifies mitochondrial aggregation using the CI and the percentage of cells containing mito-aggresomes. Nuclei were stained with DAPI. **, P < 0.01.
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    Wsv156 targets mitochondria via Cq TOMM70 and triggers mito-aggresome formation. ( A ) Wsv156 expression increased following WSSV infection. Temporal expression of wsv156 at the mRNA (left panel) and protein level (right panel) was assessed by RT-qPCR and western blot, respectively, in Hpt cells after WSSV infection. ( B ) Wsv156 localized to mitochondria. Endogenous wsv156 protein in Hpt cells (left panel) and overexpressed wsv156 in HEK 293T cells (right panel) both predominantly co-fractionated with mitochondria. ( C ) Identification of host mitochondrial proteins interacting with wsv156 by affinity purification-mass spectrometry (AP-MS). ( D ) Wsv156 interacted with Cq TOMM70. Co-IP <t>with</t> <t>anti-Myc</t> beads was performed in HEK 293T cells co-transfected with wsv156-Myc and Cq TOMM70-HA. ( E ) Wsv156 expression induced mitochondrial aggregation. Confocal microscopy of HEK 293T cells showed co-localization of wsv156-GFP (green) with the mitochondrial marker Hs COX IV (red). Cells expressing GFP alone or wsv152-GFP served as controls. ( F ) Wsv156 knockdown attenuated WSSV-induced mitochondrial aggregation. Gene silencing of wsv156 in Hpt cells reduced mitochondrial clustering (red) compared to control cells at 12 hpi. NT, non-targeting dsRNA (GFP dsRNA) control; RNAi wsv156, wsv156-specific dsRNA. The right panel quantifies mitochondrial aggregation using the CI and the percentage of cells containing mito-aggresomes. Nuclei were stained with DAPI. **, P < 0.01.
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    Wsv156 targets mitochondria via Cq TOMM70 and triggers mito-aggresome formation. ( A ) Wsv156 expression increased following WSSV infection. Temporal expression of wsv156 at the mRNA (left panel) and protein level (right panel) was assessed by RT-qPCR and western blot, respectively, in Hpt cells after WSSV infection. ( B ) Wsv156 localized to mitochondria. Endogenous wsv156 protein in Hpt cells (left panel) and overexpressed wsv156 in HEK 293T cells (right panel) both predominantly co-fractionated with mitochondria. ( C ) Identification of host mitochondrial proteins interacting with wsv156 by affinity purification-mass spectrometry (AP-MS). ( D ) Wsv156 interacted with Cq TOMM70. Co-IP <t>with</t> <t>anti-Myc</t> beads was performed in HEK 293T cells co-transfected with wsv156-Myc and Cq TOMM70-HA. ( E ) Wsv156 expression induced mitochondrial aggregation. Confocal microscopy of HEK 293T cells showed co-localization of wsv156-GFP (green) with the mitochondrial marker Hs COX IV (red). Cells expressing GFP alone or wsv152-GFP served as controls. ( F ) Wsv156 knockdown attenuated WSSV-induced mitochondrial aggregation. Gene silencing of wsv156 in Hpt cells reduced mitochondrial clustering (red) compared to control cells at 12 hpi. NT, non-targeting dsRNA (GFP dsRNA) control; RNAi wsv156, wsv156-specific dsRNA. The right panel quantifies mitochondrial aggregation using the CI and the percentage of cells containing mito-aggresomes. Nuclei were stained with DAPI. **, P < 0.01.
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    Wsv156 targets mitochondria via Cq TOMM70 and triggers mito-aggresome formation. ( A ) Wsv156 expression increased following WSSV infection. Temporal expression of wsv156 at the mRNA (left panel) and protein level (right panel) was assessed by RT-qPCR and western blot, respectively, in Hpt cells after WSSV infection. ( B ) Wsv156 localized to mitochondria. Endogenous wsv156 protein in Hpt cells (left panel) and overexpressed wsv156 in HEK 293T cells (right panel) both predominantly co-fractionated with mitochondria. ( C ) Identification of host mitochondrial proteins interacting with wsv156 by affinity purification-mass spectrometry (AP-MS). ( D ) Wsv156 interacted with Cq TOMM70. Co-IP <t>with</t> <t>anti-Myc</t> beads was performed in HEK 293T cells co-transfected with wsv156-Myc and Cq TOMM70-HA. ( E ) Wsv156 expression induced mitochondrial aggregation. Confocal microscopy of HEK 293T cells showed co-localization of wsv156-GFP (green) with the mitochondrial marker Hs COX IV (red). Cells expressing GFP alone or wsv152-GFP served as controls. ( F ) Wsv156 knockdown attenuated WSSV-induced mitochondrial aggregation. Gene silencing of wsv156 in Hpt cells reduced mitochondrial clustering (red) compared to control cells at 12 hpi. NT, non-targeting dsRNA (GFP dsRNA) control; RNAi wsv156, wsv156-specific dsRNA. The right panel quantifies mitochondrial aggregation using the CI and the percentage of cells containing mito-aggresomes. Nuclei were stained with DAPI. **, P < 0.01.
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    Image Search Results


    Wsv156 targets mitochondria via Cq TOMM70 and triggers mito-aggresome formation. ( A ) Wsv156 expression increased following WSSV infection. Temporal expression of wsv156 at the mRNA (left panel) and protein level (right panel) was assessed by RT-qPCR and western blot, respectively, in Hpt cells after WSSV infection. ( B ) Wsv156 localized to mitochondria. Endogenous wsv156 protein in Hpt cells (left panel) and overexpressed wsv156 in HEK 293T cells (right panel) both predominantly co-fractionated with mitochondria. ( C ) Identification of host mitochondrial proteins interacting with wsv156 by affinity purification-mass spectrometry (AP-MS). ( D ) Wsv156 interacted with Cq TOMM70. Co-IP with anti-Myc beads was performed in HEK 293T cells co-transfected with wsv156-Myc and Cq TOMM70-HA. ( E ) Wsv156 expression induced mitochondrial aggregation. Confocal microscopy of HEK 293T cells showed co-localization of wsv156-GFP (green) with the mitochondrial marker Hs COX IV (red). Cells expressing GFP alone or wsv152-GFP served as controls. ( F ) Wsv156 knockdown attenuated WSSV-induced mitochondrial aggregation. Gene silencing of wsv156 in Hpt cells reduced mitochondrial clustering (red) compared to control cells at 12 hpi. NT, non-targeting dsRNA (GFP dsRNA) control; RNAi wsv156, wsv156-specific dsRNA. The right panel quantifies mitochondrial aggregation using the CI and the percentage of cells containing mito-aggresomes. Nuclei were stained with DAPI. **, P < 0.01.

    Journal: Journal of Virology

    Article Title: The white spot syndrome virus wsv156 protein hijacks Parkin-dependent mitophagy to promote viral infection

    doi: 10.1128/jvi.00418-26

    Figure Lengend Snippet: Wsv156 targets mitochondria via Cq TOMM70 and triggers mito-aggresome formation. ( A ) Wsv156 expression increased following WSSV infection. Temporal expression of wsv156 at the mRNA (left panel) and protein level (right panel) was assessed by RT-qPCR and western blot, respectively, in Hpt cells after WSSV infection. ( B ) Wsv156 localized to mitochondria. Endogenous wsv156 protein in Hpt cells (left panel) and overexpressed wsv156 in HEK 293T cells (right panel) both predominantly co-fractionated with mitochondria. ( C ) Identification of host mitochondrial proteins interacting with wsv156 by affinity purification-mass spectrometry (AP-MS). ( D ) Wsv156 interacted with Cq TOMM70. Co-IP with anti-Myc beads was performed in HEK 293T cells co-transfected with wsv156-Myc and Cq TOMM70-HA. ( E ) Wsv156 expression induced mitochondrial aggregation. Confocal microscopy of HEK 293T cells showed co-localization of wsv156-GFP (green) with the mitochondrial marker Hs COX IV (red). Cells expressing GFP alone or wsv152-GFP served as controls. ( F ) Wsv156 knockdown attenuated WSSV-induced mitochondrial aggregation. Gene silencing of wsv156 in Hpt cells reduced mitochondrial clustering (red) compared to control cells at 12 hpi. NT, non-targeting dsRNA (GFP dsRNA) control; RNAi wsv156, wsv156-specific dsRNA. The right panel quantifies mitochondrial aggregation using the CI and the percentage of cells containing mito-aggresomes. Nuclei were stained with DAPI. **, P < 0.01.

    Article Snippet: Co-IP was performed using anti-Myc magnetic beads (MedChemExpress, HY-K0206) as previously described ( ).

    Techniques: Expressing, Infection, Quantitative RT-PCR, Western Blot, Affinity Purification, Mass Spectrometry, Protein-Protein interactions, Co-Immunoprecipitation Assay, Transfection, Confocal Microscopy, Marker, Knockdown, Control, Staining