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anti his  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti his
    Anti His, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 571 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/anti+his+2365s/His-Tag+Antibody/10__1007_slash_s10863___026___10088___z-145-7-8
    Average 96 stars, based on 571 article reviews
    anti his - by Bioz Stars, 2026-10
    96/100 stars

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    other:

    Article Title: Host E3 ligase RNF2 restricts African swine fever virus replication through targeting viral pA104R for its K5 site ubiquitination degradation
    Article Snippet: The anti-ubiquitin antibody (A19686) was purchased from AbClone; the anti-FLAG-Tag (14793S), anti-HA (3724S), anti-His (2365S) and anti-MYC (2278S) antibodies were purchased from Cell Signaling Technology (CST; USA); anti-β-actin (A1978), anti-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (G8795) antibodies and 4’,6-diamidino-2-phenylindole (DAPI; D8417) were purchased from Sigma (USA).

    Article Title: Host E3 ligase RNF2 restricts African swine fever virus replication through targeting viral pA104R for its K5 site ubiquitination degradation.
    Article Snippet: The anti-ubiquitin antibody 166 (A19686) was purchased from AbClone; the anti-FLAG-Tag (14793S), anti-HA 167 (3724S), anti-His (2365S) and anti-MYC (2278S) antibodies were purchased 168 from Cell Signaling Technology (CST; USA); anti-β-actin (A1978), 169 anti-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (G8795) 170 antibodies and 4’,6-diamidino-2-phenylindole (DAPI; D8417) were purchased 171 from Sigma (USA).



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    ( a ) A scheme of the G-PROV approach that enables functional analysis of glutathionylation on the protein of interest (POI): dehydroglutathione (dhG) is used to introduce a non-reducible glutathione modification on the purified engineered NISCH construct (enNISCH). Subsequently, the glutathione-modified NISCH construct is delivered to cells via fusogenic liposome, where the effect of glutathionylation on NISCH can be analyzed. ( b ) dhG modification on purified enNISCH. Purified enNISCH WT and C185S were incubated with dhG. The dhG-mediated glutathione modification was analyzed by glutathione antibody (n = 2). ( c ) Analysis of enNISCH delivered to MDA-MB-231 cells via fusogenic liposome. After incubating fusogenic liposomes containing <t>His-enNISCH</t> constructs (modified or non-modified by dhG) for 2 h, lysates were analyzed by Western blot (n = 2). ( d-e ) The migration and invasion assays. After incubating fusogenic liposomes for 2 h, MDA-MB-231 cells were analyzed by the wound-healing migration ( d , n = 6) and transwell invasion ( e , n = 2) assays. ( f ) The colony formation by enNISCH constructs. Fusogenic liposomes containing enNISCH WT or C185S were incubated with MDA-MB-231 cells on plates, and the number of colonies formed was counted after 15 days. Cells were incubated in DMEM containing 25 mM Glc ( d – e ) or 5 mM Glc ( f ). The statistical difference was analyzed by one-way ANOVA and Tukey’s post-hoc test ( b – e ) or two-way ANOVA and Sidak’s post-hoc test ( f ), where *p < 0.03, **p < 0.002, ***p < 0.0002, ****p < 0.0001.
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    ( a ) A scheme of the G-PROV approach that enables functional analysis of glutathionylation on the protein of interest (POI): dehydroglutathione (dhG) is used to introduce a non-reducible glutathione modification on the purified engineered NISCH construct (enNISCH). Subsequently, the glutathione-modified NISCH construct is delivered to cells via fusogenic liposome, where the effect of glutathionylation on NISCH can be analyzed. ( b ) dhG modification on purified enNISCH. Purified enNISCH WT and C185S were incubated with dhG. The dhG-mediated glutathione modification was analyzed by glutathione antibody (n = 2). ( c ) Analysis of enNISCH delivered to MDA-MB-231 cells via fusogenic liposome. After incubating fusogenic liposomes containing <t>His-enNISCH</t> constructs (modified or non-modified by dhG) for 2 h, lysates were analyzed by Western blot (n = 2). ( d-e ) The migration and invasion assays. After incubating fusogenic liposomes for 2 h, MDA-MB-231 cells were analyzed by the wound-healing migration ( d , n = 6) and transwell invasion ( e , n = 2) assays. ( f ) The colony formation by enNISCH constructs. Fusogenic liposomes containing enNISCH WT or C185S were incubated with MDA-MB-231 cells on plates, and the number of colonies formed was counted after 15 days. Cells were incubated in DMEM containing 25 mM Glc ( d – e ) or 5 mM Glc ( f ). The statistical difference was analyzed by one-way ANOVA and Tukey’s post-hoc test ( b – e ) or two-way ANOVA and Sidak’s post-hoc test ( f ), where *p < 0.03, **p < 0.002, ***p < 0.0002, ****p < 0.0001.
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    ( a ) A scheme of the G-PROV approach that enables functional analysis of glutathionylation on the protein of interest (POI): dehydroglutathione (dhG) is used to introduce a non-reducible glutathione modification on the purified engineered NISCH construct (enNISCH). Subsequently, the glutathione-modified NISCH construct is delivered to cells via fusogenic liposome, where the effect of glutathionylation on NISCH can be analyzed. ( b ) dhG modification on purified enNISCH. Purified enNISCH WT and C185S were incubated with dhG. The dhG-mediated glutathione modification was analyzed by glutathione antibody (n = 2). ( c ) Analysis of enNISCH delivered to MDA-MB-231 cells via fusogenic liposome. After incubating fusogenic liposomes containing His-enNISCH constructs (modified or non-modified by dhG) for 2 h, lysates were analyzed by Western blot (n = 2). ( d-e ) The migration and invasion assays. After incubating fusogenic liposomes for 2 h, MDA-MB-231 cells were analyzed by the wound-healing migration ( d , n = 6) and transwell invasion ( e , n = 2) assays. ( f ) The colony formation by enNISCH constructs. Fusogenic liposomes containing enNISCH WT or C185S were incubated with MDA-MB-231 cells on plates, and the number of colonies formed was counted after 15 days. Cells were incubated in DMEM containing 25 mM Glc ( d – e ) or 5 mM Glc ( f ). The statistical difference was analyzed by one-way ANOVA and Tukey’s post-hoc test ( b – e ) or two-way ANOVA and Sidak’s post-hoc test ( f ), where *p < 0.03, **p < 0.002, ***p < 0.0002, ****p < 0.0001.

    Journal: Free radical biology & medicine

    Article Title: Redox regulation of cell migration via Nischarin S-glutathionylation

    doi: 10.1016/j.freeradbiomed.2025.11.013

    Figure Lengend Snippet: ( a ) A scheme of the G-PROV approach that enables functional analysis of glutathionylation on the protein of interest (POI): dehydroglutathione (dhG) is used to introduce a non-reducible glutathione modification on the purified engineered NISCH construct (enNISCH). Subsequently, the glutathione-modified NISCH construct is delivered to cells via fusogenic liposome, where the effect of glutathionylation on NISCH can be analyzed. ( b ) dhG modification on purified enNISCH. Purified enNISCH WT and C185S were incubated with dhG. The dhG-mediated glutathione modification was analyzed by glutathione antibody (n = 2). ( c ) Analysis of enNISCH delivered to MDA-MB-231 cells via fusogenic liposome. After incubating fusogenic liposomes containing His-enNISCH constructs (modified or non-modified by dhG) for 2 h, lysates were analyzed by Western blot (n = 2). ( d-e ) The migration and invasion assays. After incubating fusogenic liposomes for 2 h, MDA-MB-231 cells were analyzed by the wound-healing migration ( d , n = 6) and transwell invasion ( e , n = 2) assays. ( f ) The colony formation by enNISCH constructs. Fusogenic liposomes containing enNISCH WT or C185S were incubated with MDA-MB-231 cells on plates, and the number of colonies formed was counted after 15 days. Cells were incubated in DMEM containing 25 mM Glc ( d – e ) or 5 mM Glc ( f ). The statistical difference was analyzed by one-way ANOVA and Tukey’s post-hoc test ( b – e ) or two-way ANOVA and Sidak’s post-hoc test ( f ), where *p < 0.03, **p < 0.002, ***p < 0.0002, ****p < 0.0001.

    Article Snippet: For validation of protein delivery, cells were lysed and analyzed by western blotting using anti-HIS antibody (Cell Signaling Cat #2365).

    Techniques: Functional Assay, Introduce, Modification, Purification, Construct, Incubation, Liposomes, Western Blot, Migration