dmem ham s f 12 Search Results


dmem/ham´s f-12 salts (1:1) medium  (Biochrom)
90
Biochrom dmem/ham´s f-12 salts (1:1) medium
Dmem/Ham´S F 12 Salts (1:1) Medium, supplied by Biochrom, 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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dmem/ham's f-12 (1:1) medium with or without n2 supplement  (STEMCELL Technologies Inc)
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STEMCELL Technologies Inc dmem/ham's f-12 (1:1) medium with or without n2 supplement
Dmem/Ham's F 12 (1:1) Medium With Or Without N2 Supplement, supplied by STEMCELL Technologies 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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basal cell culture liquid media–dmem and ham’s f-12, 50/50 mix  (Corning Life Sciences)
90
Corning Life Sciences basal cell culture liquid media–dmem and ham’s f-12, 50/50 mix
Basal Cell Culture Liquid Media–Dmem And Ham’s F 12, 50/50 Mix, supplied by Corning Life Sciences, 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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basal cell culture liquid media–dmem and ham’s f-12, 50/50 mix - by Bioz Stars, 2026-08
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a549 cell line  (FUJIFILM)
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FUJIFILM a549 cell line
A549 Cell Line, supplied by FUJIFILM, 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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a549 cell line - by Bioz Stars, 2026-08
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ham's f-12 dmem 1:1 containing 5% (v/v) delipidated fbs, 50 μ m sodium mevalonate, and 50 μ m mevastatin  (Enzo Biochem)
90
Enzo Biochem ham's f-12 dmem 1:1 containing 5% (v/v) delipidated fbs, 50 μ m sodium mevalonate, and 50 μ m mevastatin
Characterization of the activity of the prodomain deletion mutants. A, SREBP-2 processing by SKI-1/S1P mutants. SRD12B cells were transfected with the indicated SKI-1/S1P constructs. After 32 h, the SREBP-2 pathway was induced by <t>mevastatin</t> treatment for 18 h, whereas control cells were treated with DMSO. After treatment, total RNA was extracted to analyze HGMCS1 gene induction by quantitative RT-PCR. The results were analyzed by the ΔΔCT method, and the data were normalized against hydroxymethylbilane synthase gene expression. Gene expression is represented as fold induction above levels for control treatment (pIR-HA DMSO) (mean ± S.D.; n = 3). B, expression of SKI-1/S1P variants in A was assessed by Western blot as in Fig. 1B. C and D, LASV and LCMV GPC processing by the SKI-1/S1P mutants. SRD12B cell were co-transfected with either LASV GPC (C) or LCMV GPC (D) and the indicated SKI-1/S1P variants. At 48 h post-transfection, the cell lysates were analyzed by Western blot to assess GPC processing. SKI-1/S1P expression was detected with anti-V5 antibody and tubulin (Tub) detected as loading control. Tubulin, the precursor GPC, mature GP2, and maturation forms of SKI-1/S1P (forms A, B, and C) are indicated. E, schematic of the SKI-1/S1P sensor bearing the cleavage motif of LASV GPC. The signal peptide (SP), the GLuc reporter, the LASV GPC-derived cleavage motif, and the SKI-1/S1P-derived stump region are indicated. F, processing of the SKI-1/S1P sensor by SKI-1/S1P mutants. SRD12B cells were co-transfected with the SKI-1/S1P sensor (SS-LASV) and the indicated SKI-1/S1P variants. At 48 h post-transfection, cell lysates and supernatants were collected and analyzed by Western blot using an anti-GLuc antibody (bottom). Cleaved sensor (cGLuc) and the uncleaved precursor (pGLuc) are indicated. Conditioned media were analyzed for GLuc activity by addition of coelenterazine substrate. The data are shown as relative light units (RLU) (means ± S.D.; n = 3).
Ham's F 12 Dmem 1:1 Containing 5% (V/V) Delipidated Fbs, 50 μ M Sodium Mevalonate, And 50 μ M Mevastatin, supplied by Enzo Biochem, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/dmem+ham+s+f+12/pmc04732194-86-31-32?v=Enzo+Biochem
Average 90 stars, based on 1 article reviews
ham's f-12 dmem 1:1 containing 5% (v/v) delipidated fbs, 50 μ m sodium mevalonate, and 50 μ m mevastatin - by Bioz Stars, 2026-08
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dmem/f12 medium asahi techno glass  (Asahi Techno Glass)
90
Asahi Techno Glass dmem/f12 medium asahi techno glass
Characterization of the activity of the prodomain deletion mutants. A, SREBP-2 processing by SKI-1/S1P mutants. SRD12B cells were transfected with the indicated SKI-1/S1P constructs. After 32 h, the SREBP-2 pathway was induced by <t>mevastatin</t> treatment for 18 h, whereas control cells were treated with DMSO. After treatment, total RNA was extracted to analyze HGMCS1 gene induction by quantitative RT-PCR. The results were analyzed by the ΔΔCT method, and the data were normalized against hydroxymethylbilane synthase gene expression. Gene expression is represented as fold induction above levels for control treatment (pIR-HA DMSO) (mean ± S.D.; n = 3). B, expression of SKI-1/S1P variants in A was assessed by Western blot as in Fig. 1B. C and D, LASV and LCMV GPC processing by the SKI-1/S1P mutants. SRD12B cell were co-transfected with either LASV GPC (C) or LCMV GPC (D) and the indicated SKI-1/S1P variants. At 48 h post-transfection, the cell lysates were analyzed by Western blot to assess GPC processing. SKI-1/S1P expression was detected with anti-V5 antibody and tubulin (Tub) detected as loading control. Tubulin, the precursor GPC, mature GP2, and maturation forms of SKI-1/S1P (forms A, B, and C) are indicated. E, schematic of the SKI-1/S1P sensor bearing the cleavage motif of LASV GPC. The signal peptide (SP), the GLuc reporter, the LASV GPC-derived cleavage motif, and the SKI-1/S1P-derived stump region are indicated. F, processing of the SKI-1/S1P sensor by SKI-1/S1P mutants. SRD12B cells were co-transfected with the SKI-1/S1P sensor (SS-LASV) and the indicated SKI-1/S1P variants. At 48 h post-transfection, cell lysates and supernatants were collected and analyzed by Western blot using an anti-GLuc antibody (bottom). Cleaved sensor (cGLuc) and the uncleaved precursor (pGLuc) are indicated. Conditioned media were analyzed for GLuc activity by addition of coelenterazine substrate. The data are shown as relative light units (RLU) (means ± S.D.; n = 3).
Dmem/F12 Medium Asahi Techno Glass, supplied by Asahi Techno Glass, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/dmem+ham+s+f+12/pm24710035-135-63-67?v=Asahi+Techno+Glass
Average 90 stars, based on 1 article reviews
dmem/f12 medium asahi techno glass - by Bioz Stars, 2026-08
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dmem/ham"s f:12 cell culture medium  (Lonza)
90
Lonza dmem/ham"s f:12 cell culture medium
Characterization of the activity of the prodomain deletion mutants. A, SREBP-2 processing by SKI-1/S1P mutants. SRD12B cells were transfected with the indicated SKI-1/S1P constructs. After 32 h, the SREBP-2 pathway was induced by <t>mevastatin</t> treatment for 18 h, whereas control cells were treated with DMSO. After treatment, total RNA was extracted to analyze HGMCS1 gene induction by quantitative RT-PCR. The results were analyzed by the ΔΔCT method, and the data were normalized against hydroxymethylbilane synthase gene expression. Gene expression is represented as fold induction above levels for control treatment (pIR-HA DMSO) (mean ± S.D.; n = 3). B, expression of SKI-1/S1P variants in A was assessed by Western blot as in Fig. 1B. C and D, LASV and LCMV GPC processing by the SKI-1/S1P mutants. SRD12B cell were co-transfected with either LASV GPC (C) or LCMV GPC (D) and the indicated SKI-1/S1P variants. At 48 h post-transfection, the cell lysates were analyzed by Western blot to assess GPC processing. SKI-1/S1P expression was detected with anti-V5 antibody and tubulin (Tub) detected as loading control. Tubulin, the precursor GPC, mature GP2, and maturation forms of SKI-1/S1P (forms A, B, and C) are indicated. E, schematic of the SKI-1/S1P sensor bearing the cleavage motif of LASV GPC. The signal peptide (SP), the GLuc reporter, the LASV GPC-derived cleavage motif, and the SKI-1/S1P-derived stump region are indicated. F, processing of the SKI-1/S1P sensor by SKI-1/S1P mutants. SRD12B cells were co-transfected with the SKI-1/S1P sensor (SS-LASV) and the indicated SKI-1/S1P variants. At 48 h post-transfection, cell lysates and supernatants were collected and analyzed by Western blot using an anti-GLuc antibody (bottom). Cleaved sensor (cGLuc) and the uncleaved precursor (pGLuc) are indicated. Conditioned media were analyzed for GLuc activity by addition of coelenterazine substrate. The data are shown as relative light units (RLU) (means ± S.D.; n = 3).
Dmem/Ham"S F:12 Cell Culture Medium, supplied by Lonza, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/dmem+ham+s+f+12/pm30223109-49-22-20?v=Lonza
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dmem/ham"s f:12 cell culture medium - by Bioz Stars, 2026-08
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dmem:ham's f-12 1:1  (Rocha labs)
90
Rocha labs dmem:ham's f-12 1:1
Characterization of the activity of the prodomain deletion mutants. A, SREBP-2 processing by SKI-1/S1P mutants. SRD12B cells were transfected with the indicated SKI-1/S1P constructs. After 32 h, the SREBP-2 pathway was induced by <t>mevastatin</t> treatment for 18 h, whereas control cells were treated with DMSO. After treatment, total RNA was extracted to analyze HGMCS1 gene induction by quantitative RT-PCR. The results were analyzed by the ΔΔCT method, and the data were normalized against hydroxymethylbilane synthase gene expression. Gene expression is represented as fold induction above levels for control treatment (pIR-HA DMSO) (mean ± S.D.; n = 3). B, expression of SKI-1/S1P variants in A was assessed by Western blot as in Fig. 1B. C and D, LASV and LCMV GPC processing by the SKI-1/S1P mutants. SRD12B cell were co-transfected with either LASV GPC (C) or LCMV GPC (D) and the indicated SKI-1/S1P variants. At 48 h post-transfection, the cell lysates were analyzed by Western blot to assess GPC processing. SKI-1/S1P expression was detected with anti-V5 antibody and tubulin (Tub) detected as loading control. Tubulin, the precursor GPC, mature GP2, and maturation forms of SKI-1/S1P (forms A, B, and C) are indicated. E, schematic of the SKI-1/S1P sensor bearing the cleavage motif of LASV GPC. The signal peptide (SP), the GLuc reporter, the LASV GPC-derived cleavage motif, and the SKI-1/S1P-derived stump region are indicated. F, processing of the SKI-1/S1P sensor by SKI-1/S1P mutants. SRD12B cells were co-transfected with the SKI-1/S1P sensor (SS-LASV) and the indicated SKI-1/S1P variants. At 48 h post-transfection, cell lysates and supernatants were collected and analyzed by Western blot using an anti-GLuc antibody (bottom). Cleaved sensor (cGLuc) and the uncleaved precursor (pGLuc) are indicated. Conditioned media were analyzed for GLuc activity by addition of coelenterazine substrate. The data are shown as relative light units (RLU) (means ± S.D.; n = 3).
Dmem:Ham's F 12 1:1, supplied by Rocha labs, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/dmem+ham+s+f+12/pm27515589-65-34-30?v=Rocha+labs
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dmem:ham's f-12 1:1 - by Bioz Stars, 2026-08
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dmem ham s f 12  (Nissui Pharmaceutical)
86
Nissui Pharmaceutical dmem ham s f 12
Characterization of the activity of the prodomain deletion mutants. A, SREBP-2 processing by SKI-1/S1P mutants. SRD12B cells were transfected with the indicated SKI-1/S1P constructs. After 32 h, the SREBP-2 pathway was induced by <t>mevastatin</t> treatment for 18 h, whereas control cells were treated with DMSO. After treatment, total RNA was extracted to analyze HGMCS1 gene induction by quantitative RT-PCR. The results were analyzed by the ΔΔCT method, and the data were normalized against hydroxymethylbilane synthase gene expression. Gene expression is represented as fold induction above levels for control treatment (pIR-HA DMSO) (mean ± S.D.; n = 3). B, expression of SKI-1/S1P variants in A was assessed by Western blot as in Fig. 1B. C and D, LASV and LCMV GPC processing by the SKI-1/S1P mutants. SRD12B cell were co-transfected with either LASV GPC (C) or LCMV GPC (D) and the indicated SKI-1/S1P variants. At 48 h post-transfection, the cell lysates were analyzed by Western blot to assess GPC processing. SKI-1/S1P expression was detected with anti-V5 antibody and tubulin (Tub) detected as loading control. Tubulin, the precursor GPC, mature GP2, and maturation forms of SKI-1/S1P (forms A, B, and C) are indicated. E, schematic of the SKI-1/S1P sensor bearing the cleavage motif of LASV GPC. The signal peptide (SP), the GLuc reporter, the LASV GPC-derived cleavage motif, and the SKI-1/S1P-derived stump region are indicated. F, processing of the SKI-1/S1P sensor by SKI-1/S1P mutants. SRD12B cells were co-transfected with the SKI-1/S1P sensor (SS-LASV) and the indicated SKI-1/S1P variants. At 48 h post-transfection, cell lysates and supernatants were collected and analyzed by Western blot using an anti-GLuc antibody (bottom). Cleaved sensor (cGLuc) and the uncleaved precursor (pGLuc) are indicated. Conditioned media were analyzed for GLuc activity by addition of coelenterazine substrate. The data are shown as relative light units (RLU) (means ± S.D.; n = 3).
Dmem Ham S F 12, supplied by Nissui Pharmaceutical, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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dmem ham s f 12 - by Bioz Stars, 2026-08
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Image Search Results


Characterization of the activity of the prodomain deletion mutants. A, SREBP-2 processing by SKI-1/S1P mutants. SRD12B cells were transfected with the indicated SKI-1/S1P constructs. After 32 h, the SREBP-2 pathway was induced by mevastatin treatment for 18 h, whereas control cells were treated with DMSO. After treatment, total RNA was extracted to analyze HGMCS1 gene induction by quantitative RT-PCR. The results were analyzed by the ΔΔCT method, and the data were normalized against hydroxymethylbilane synthase gene expression. Gene expression is represented as fold induction above levels for control treatment (pIR-HA DMSO) (mean ± S.D.; n = 3). B, expression of SKI-1/S1P variants in A was assessed by Western blot as in Fig. 1B. C and D, LASV and LCMV GPC processing by the SKI-1/S1P mutants. SRD12B cell were co-transfected with either LASV GPC (C) or LCMV GPC (D) and the indicated SKI-1/S1P variants. At 48 h post-transfection, the cell lysates were analyzed by Western blot to assess GPC processing. SKI-1/S1P expression was detected with anti-V5 antibody and tubulin (Tub) detected as loading control. Tubulin, the precursor GPC, mature GP2, and maturation forms of SKI-1/S1P (forms A, B, and C) are indicated. E, schematic of the SKI-1/S1P sensor bearing the cleavage motif of LASV GPC. The signal peptide (SP), the GLuc reporter, the LASV GPC-derived cleavage motif, and the SKI-1/S1P-derived stump region are indicated. F, processing of the SKI-1/S1P sensor by SKI-1/S1P mutants. SRD12B cells were co-transfected with the SKI-1/S1P sensor (SS-LASV) and the indicated SKI-1/S1P variants. At 48 h post-transfection, cell lysates and supernatants were collected and analyzed by Western blot using an anti-GLuc antibody (bottom). Cleaved sensor (cGLuc) and the uncleaved precursor (pGLuc) are indicated. Conditioned media were analyzed for GLuc activity by addition of coelenterazine substrate. The data are shown as relative light units (RLU) (means ± S.D.; n = 3).

Journal: The Journal of Biological Chemistry

Article Title: Mechanism of Folding and Activation of Subtilisin Kexin Isozyme-1 (SKI-1)/Site-1 Protease (S1P) *

doi: 10.1074/jbc.M115.677757

Figure Lengend Snippet: Characterization of the activity of the prodomain deletion mutants. A, SREBP-2 processing by SKI-1/S1P mutants. SRD12B cells were transfected with the indicated SKI-1/S1P constructs. After 32 h, the SREBP-2 pathway was induced by mevastatin treatment for 18 h, whereas control cells were treated with DMSO. After treatment, total RNA was extracted to analyze HGMCS1 gene induction by quantitative RT-PCR. The results were analyzed by the ΔΔCT method, and the data were normalized against hydroxymethylbilane synthase gene expression. Gene expression is represented as fold induction above levels for control treatment (pIR-HA DMSO) (mean ± S.D.; n = 3). B, expression of SKI-1/S1P variants in A was assessed by Western blot as in Fig. 1B. C and D, LASV and LCMV GPC processing by the SKI-1/S1P mutants. SRD12B cell were co-transfected with either LASV GPC (C) or LCMV GPC (D) and the indicated SKI-1/S1P variants. At 48 h post-transfection, the cell lysates were analyzed by Western blot to assess GPC processing. SKI-1/S1P expression was detected with anti-V5 antibody and tubulin (Tub) detected as loading control. Tubulin, the precursor GPC, mature GP2, and maturation forms of SKI-1/S1P (forms A, B, and C) are indicated. E, schematic of the SKI-1/S1P sensor bearing the cleavage motif of LASV GPC. The signal peptide (SP), the GLuc reporter, the LASV GPC-derived cleavage motif, and the SKI-1/S1P-derived stump region are indicated. F, processing of the SKI-1/S1P sensor by SKI-1/S1P mutants. SRD12B cells were co-transfected with the SKI-1/S1P sensor (SS-LASV) and the indicated SKI-1/S1P variants. At 48 h post-transfection, cell lysates and supernatants were collected and analyzed by Western blot using an anti-GLuc antibody (bottom). Cleaved sensor (cGLuc) and the uncleaved precursor (pGLuc) are indicated. Conditioned media were analyzed for GLuc activity by addition of coelenterazine substrate. The data are shown as relative light units (RLU) (means ± S.D.; n = 3).

Article Snippet: Drug Treatments Induction of genes regulated by SREBP2 was triggered by treatment with Ham's F-12 DMEM 1:1 containing 5% (v/v) delipidated FBS, 50 μ m sodium mevalonate, and 50 μ m mevastatin (Enzo Lifescience) for 18 h, as reported previously ( 20 ).

Techniques: Activity Assay, Transfection, Construct, Quantitative RT-PCR, Expressing, Western Blot, Derivative Assay