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(A, B) Interaction of V5-WSNNP and Myc-PIAS1 in HEK293T cells by using a co-IP assay. HEK293T cells were individually transfected or co-transfected with plasmids expressing V5-WSNNP and Myc-PIAS1. Cell lysates were immunoprecipitated with a mouse anti-V5 mAb (A) or a mouse anti-Myc mAb (B), and subjected to western blotting with a rabbit anti-V5 pAb and a rabbit anti-Myc pAb for the detection of WSNNP and PIAS1, respectively. (C) Interaction of GST-WSNNP and His-PIAS1 by using a GST pull-down assay. His-tagged PIAS1 was expressed in E . coli BL21 (DE3) and purified by using Ni Sepharose Excel resin, and the GST or GST-NP protein was expressed in HEK293T cells and purified by using Glutathione Sepharose 4 Fast Flow. An equal amount of purified PIAS1 was mixed with the Glutathione Sepharose 4 Fast Flow samples that bind GST or GST-NP. After rocking and washing, the mixed samples were separated <t>by</t> <t>SDS-PAGE</t> and stained with Coomassie blue. (D) Interaction of IAV NP and PIAS1 in virus-infected cells. HEK293T cells were transfected for 24 h to express Myc-PIAS1, and were then infected with WSN (H1N1) virus (MOI = 5). At 30 h p.i., cell lysates were immunoprecipitated with a mouse anti-NP mAb, followed by western blotting with a rabbit anti-NP pAb and a rabbit anti-Myc pAb. (E) Co-localization of IAV NP and PIAS1 in A549 cells infected with WSN (H1N1) virus. A549 cells were infected with WSN (H1N1) virus (MOI = 5). At 2, 4, 6, and 8 h p.i., the infected cells were fixed and stained with a mouse anti-NP mAb and a rabbit anti-PIAS1 pAb, followed by incubation with Alexa Fluor 633 goat anti-mouse IgG (H+L) (red) and Alexa Fluor 488 donkey anti-rabbit IgG (H+L) (green). The nuclei were stained with DAPI. (F-H) Co-IP assay to examine the interactions between Myc-PIAS1 and PB2, PB1, and PA of WSN (H1N1) virus in HEK293T cells. HEK293T cells were individually transfected or co-transfected with plasmids expressing WSNPB2, WSNPB1, WSNPA, and Myc-PIAS1. Cell lysates were immunoprecipitated with a mouse anti-Myc mAb and were subjected to western blotting with a rabbit anti-PB2 pAb (F), a rabbit anti-PB1 pAb (G), a rabbit anti-PA pAb (H), and a rabbit anti-Myc pAb (F-H) for the detection of PB2, PB1, PA, and PIAS1, respectively.

Sds Page Loading Buffer, supplied by Solarbio Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1) Product Images from "PIAS1-mediated SUMOylation of influenza A virus PB2 restricts viral replication and virulence"

Article Title: PIAS1-mediated SUMOylation of influenza A virus PB2 restricts viral replication and virulence

Journal: PLoS Pathogens

doi: 10.1371/journal.ppat.1010446

Figure Legend Snippet: (A, B) Interaction of V5-WSNNP and Myc-PIAS1 in HEK293T cells by using a co-IP assay. HEK293T cells were individually transfected or co-transfected with plasmids expressing V5-WSNNP and Myc-PIAS1. Cell lysates were immunoprecipitated with a mouse anti-V5 mAb (A) or a mouse anti-Myc mAb (B), and subjected to western blotting with a rabbit anti-V5 pAb and a rabbit anti-Myc pAb for the detection of WSNNP and PIAS1, respectively. (C) Interaction of GST-WSNNP and His-PIAS1 by using a GST pull-down assay. His-tagged PIAS1 was expressed in E . coli BL21 (DE3) and purified by using Ni Sepharose Excel resin, and the GST or GST-NP protein was expressed in HEK293T cells and purified by using Glutathione Sepharose 4 Fast Flow. An equal amount of purified PIAS1 was mixed with the Glutathione Sepharose 4 Fast Flow samples that bind GST or GST-NP. After rocking and washing, the mixed samples were separated by SDS-PAGE and stained with Coomassie blue. (D) Interaction of IAV NP and PIAS1 in virus-infected cells. HEK293T cells were transfected for 24 h to express Myc-PIAS1, and were then infected with WSN (H1N1) virus (MOI = 5). At 30 h p.i., cell lysates were immunoprecipitated with a mouse anti-NP mAb, followed by western blotting with a rabbit anti-NP pAb and a rabbit anti-Myc pAb. (E) Co-localization of IAV NP and PIAS1 in A549 cells infected with WSN (H1N1) virus. A549 cells were infected with WSN (H1N1) virus (MOI = 5). At 2, 4, 6, and 8 h p.i., the infected cells were fixed and stained with a mouse anti-NP mAb and a rabbit anti-PIAS1 pAb, followed by incubation with Alexa Fluor 633 goat anti-mouse IgG (H+L) (red) and Alexa Fluor 488 donkey anti-rabbit IgG (H+L) (green). The nuclei were stained with DAPI. (F-H) Co-IP assay to examine the interactions between Myc-PIAS1 and PB2, PB1, and PA of WSN (H1N1) virus in HEK293T cells. HEK293T cells were individually transfected or co-transfected with plasmids expressing WSNPB2, WSNPB1, WSNPA, and Myc-PIAS1. Cell lysates were immunoprecipitated with a mouse anti-Myc mAb and were subjected to western blotting with a rabbit anti-PB2 pAb (F), a rabbit anti-PB1 pAb (G), a rabbit anti-PA pAb (H), and a rabbit anti-Myc pAb (F-H) for the detection of PB2, PB1, PA, and PIAS1, respectively.

Techniques Used: Co-Immunoprecipitation Assay, Transfection, Expressing, Immunoprecipitation, Western Blot, Pull Down Assay, Purification, SDS Page, Staining, Infection, Incubation

Membrane:

Article Title: A polyclonal antibody against extracellular loops 1 of chNHE1 blocks avian leukosis virus subgroup J infection.
Article Snippet: Avian leukosis virus subgroup J (ALV-J), an oncogenic retrovirus, induces myelocytomas and other various tumors, leading to great economical losses in poultry industry.. It is a great challenge to develop effective preventive methods for ALV-J control due to its antigenic variations in the variable regions of envelope.. In present study, we generated a mouse polyclonal antibody targeting the first extracellular loop (ECL1) of chicken Na/ H exchanger isoform 1 (chNHE1), the receptor of ALV-J, to block ALV-J infection in vitro and in vivo.

other:

Article Title: The nonstructural protein 5 of coronaviruses antagonizes GSDMD-mediated pyroptosis by cleaving and inactivating its pore-forming p30 fragment
Article Snippet: Cells were lysed with RIPA Lysis Buffer (Beyotime, P0013B) containing PMSF (Beyotime, ST506) for 10 min at 4□ and then denatured in 5 × SDS-PAGE loading buffer (Solarbio, P1040) for 10 min. After harvest, the cell lysate of equal amount was loaded on 8%-12% SDS-PAGE gels (Fdbio science) and electrophoresed, and then transferred to polyvinylidene difluoride membranes (BIO-RAD, 1620177).

Article Title: Zearalenone induces the senescence of cardiovascular cells in vitro and in vivo.
Article Snippet: Zearalenone is a contaminant in food and feed products.. It has been reported that zearalenone could lead to serious damage to health.. So far, it is unclear whether zearalenone could lead to cardiovascular aging–related injury.

Article Title: PIAS1-mediated SUMOylation of influenza A virus PB2 restricts viral replication and virulence
Article Snippet: Whole cell lysates were prepared with SDS-PAGE loading buffer (Solarbio Science & Technology, Beijing, China) at 0, 12, and 24 h p.i.

Article Title: Infectious Bronchitis Virus Triggered Caspase-8/Casapase-3/DFNA5-Mediated Pyroptosis in HD11 Cells Via ROS
Article Snippet: Thiazolyl blue tetrazolium bromide (MTT, M8180), 2.5% glutaraldehyde for electron 73 microscope (P1126), and 5×SDS-PAGE loading buffer (P1040) were purchased from Solarbio 74 (Beijing, China).

Nucleic Acid Electrophoresis:

Article Title: FRET investigation toward DNA tetrahedron-based ratiometric analysis of intracellular telomerase activity.
Article Snippet: Please note that technical editing may introduce minor changes to the text and/or graphics, which may alter content.. The journal’s standard Terms & Conditions and the ethical guidelines, outlined in our author and reviewer resource centre, still apply.. In no event shall the Royal Society of Chemistry be held responsible for any errors or omissions in this Accepted Manuscript or any consequences arising from the use of any information it contains.

Article Title: A PCR-free voltammetric telomerase activity assay using a substrate primer on a gold electrode and DNA-triggered capture of gold nanoparticles.
Article Snippet: The paper describes a voltammetric method for the quantitation of the activity of telomerase extracted from cancer cells.. A thiolated single-stranded telomerase substrate primer was firstly immobilized on a gold electrode.. In the presence of a mixture of telomerase and deoxynucleotide triphosphates, the primer becomes elongated and contains repetitive nucleotide sequences (TTAGGG)n. After hybridization with blocker DNA, gold nanoparticles are added and captured by the elongated singlestranded DNA.

Image Search Results

Metagenomic thioredoxin E5 is a new i thioredoxin superfamily member with an unusual reaction mechanism. A , E5 is an effective disulfide isomerase in the commercial Escherichia coli SHUFFLE strain and can support oxidative folding of several proteins, including vtPA, which contains nine disulfide bonds when folded correctly. B , it shows higher initial velocity than E. coli TrxA in an insulin reduction assay. C , redox potential determination of E5 using 4-acetamido-4'-maleimidylstilbene-2,2'-disulfonic acid, as described for <xref ref-type=

Figure 7 C . When oxidized in a glutathione redox buffer, E5 forms disulfide-linked dimers, which can be observed in nonreducing SDS-PAGE. M, marker, MW in kDa indicated on the right, ox. and red.: fully oxidized and reduced E5, respectively. D , the redox potential can be calculated from the ratio of reduced and oxidized protein in a given glutathione redox buffer based on the Nernst equation. Based on these calculations, E5 has a standard redox potential of −246 mV, close to the redox potential of thioredoxin. E , reduced E5 and E. coli TrxA reduce insulin when no DTT for enzyme recycling is added. F , E5 protein oxidized in this reaction forms disulfide-linked dimers, which can be observed in a Coomassie-stained SDS-PAGE. Higher molecular weight species indicated by arrows are presumably insulin adducts to the E5 dimer and E5 multimers crosslinked by insulin. G , an E5 C77S mutant, which contains only one cysteine, still forms a disulfide-linked dimer when oxidized with diamide and ( H ) is still active in an insulin reduction assay, while an E5 C74S mutant is inactive. I , size exclusion choromatography of E5 and its C77S mutant suggests a molecular weight consistent approximately with a homohexamer (the calculated mass of E5 is 23,580 Da), when compared with a protein mixture used as standard (THY, thyroglobulin; FER, ferritin; ALD, aldolase; CON, conalbumin; OVA, ovalbumin; CAR, carbonic anhydrase; and RIB, ribonuclease). To calculate the molecular weight of E5, high and low molecular weight standard proteins were run in separate runs, and their molecular mass was plotted against the elution volume. The plot was fitted using an exponential function in Excel. " width="100%" height="100%">

Journal: The Journal of Biological Chemistry

Article Title: Functional metagenomics of the thioredoxin superfamily

doi: 10.1074/jbc.RA120.016350

Figure Lengend Snippet: Metagenomic thioredoxin E5 is a new i thioredoxin superfamily member with an unusual reaction mechanism. A , E5 is an effective disulfide isomerase in the commercial Escherichia coli SHUFFLE strain and can support oxidative folding of several proteins, including vtPA, which contains nine disulfide bonds when folded correctly. B , it shows higher initial velocity than E. coli TrxA in an insulin reduction assay. C , redox potential determination of E5 using 4-acetamido-4'-maleimidylstilbene-2,2'-disulfonic acid, as described for Figure 7 C . When oxidized in a glutathione redox buffer, E5 forms disulfide-linked dimers, which can be observed in nonreducing SDS-PAGE. M, marker, MW in kDa indicated on the right, ox. and red.: fully oxidized and reduced E5, respectively. D , the redox potential can be calculated from the ratio of reduced and oxidized protein in a given glutathione redox buffer based on the Nernst equation. Based on these calculations, E5 has a standard redox potential of −246 mV, close to the redox potential of thioredoxin. E , reduced E5 and E. coli TrxA reduce insulin when no DTT for enzyme recycling is added. F , E5 protein oxidized in this reaction forms disulfide-linked dimers, which can be observed in a Coomassie-stained SDS-PAGE. Higher molecular weight species indicated by arrows are presumably insulin adducts to the E5 dimer and E5 multimers crosslinked by insulin. G , an E5 C77S mutant, which contains only one cysteine, still forms a disulfide-linked dimer when oxidized with diamide and ( H ) is still active in an insulin reduction assay, while an E5 C74S mutant is inactive. I , size exclusion choromatography of E5 and its C77S mutant suggests a molecular weight consistent approximately with a homohexamer (the calculated mass of E5 is 23,580 Da), when compared with a protein mixture used as standard (THY, thyroglobulin; FER, ferritin; ALD, aldolase; CON, conalbumin; OVA, ovalbumin; CAR, carbonic anhydrase; and RIB, ribonuclease). To calculate the molecular weight of E5, high and low molecular weight standard proteins were run in separate runs, and their molecular mass was plotted against the elution volume. The plot was fitted using an exponential function in Excel.

Article Snippet: Then, samples were incubated for 5 min at 95 °C in 1× nonreducing SDS loading buffer (2% [w/v] SDS, 12% [v/v] glycerol, 60 mM Tris–HCl [pH 7.0], and 0.0001% [w/v] bromophenol blue) and loaded onto a precast NuPAGE Novex 4 to 12% Bis–Tris protein gel (Life Technologies).

Techniques: Insulin Reduction Assay, SDS Page, Marker, Enzyme Recycling Assay, Staining, Molecular Weight, Mutagenesis