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chl 1 crl 9446  (ATCC)


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    ATCC chl 1 crl 9446
    Chl 1 Crl 9446, supplied by ATCC, used in various techniques. Bioz Stars score: 95/100, based on 125 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/chl+1+crl+9446/CHL-1/pmc12383553-34-24-43
    Average 95 stars, based on 125 article reviews
    chl 1 crl 9446 - by Bioz Stars, 2026-10
    95/100 stars

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    Isolation:

    Article Title: Genistein and Curcumin Inhibit Proliferation and Invasiveness in BRAFV600E Mutant and Wild-Type Melanoma Cells: Insights into Their Anticancer Effects
    Article Snippet: .. Human A375 CRL-1619 (a cell line exhibiting epithelial morphology that was isolated from the skin of a 54-year-old, female patient with malignant melanoma) and CHL-1 CRL-9446 (primary melanoma cells, homozygous c. 578A > G protein sequence p. H193R) cell lines were acquired by ATCC (ATCC Manassas, Manassas, VA, USA). .. Dulbecco’s Modified Eagle’s Medium (Sigma-Aldrich, St. Louis, MO, USA) with 1% of antibiotic (penicillin/streptomycin, Sigma-Aldrich, St. Louis, MO, USA), 10% fetal bovine serum (FBS) (ATCC Manassas, Manassas, VA, USA) was used for cells cultures, which were incubated at 37 °C with 5% CO 2 .

    Sequencing:

    Article Title: Genistein and Curcumin Inhibit Proliferation and Invasiveness in BRAFV600E Mutant and Wild-Type Melanoma Cells: Insights into Their Anticancer Effects
    Article Snippet: .. Human A375 CRL-1619 (a cell line exhibiting epithelial morphology that was isolated from the skin of a 54-year-old, female patient with malignant melanoma) and CHL-1 CRL-9446 (primary melanoma cells, homozygous c. 578A > G protein sequence p. H193R) cell lines were acquired by ATCC (ATCC Manassas, Manassas, VA, USA). .. Dulbecco’s Modified Eagle’s Medium (Sigma-Aldrich, St. Louis, MO, USA) with 1% of antibiotic (penicillin/streptomycin, Sigma-Aldrich, St. Louis, MO, USA), 10% fetal bovine serum (FBS) (ATCC Manassas, Manassas, VA, USA) was used for cells cultures, which were incubated at 37 °C with 5% CO 2 .



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    (A) A two-week growth CRISPR screen of 150 common Ras-proximal proteins in diploid primary human melanocytes (MC) and 5 MT Ras cell lines. Left heatmap negative selection FDR values (FDR ≤ 0.18) in each cell type by the MAGeCK algorithm (Li et al., 2014). The right heatmap relative enrichment MT vs WT Ras in mass spectrometry data for each Ras isoform; new proteins (red), known proteins (*). Ranked by combined FDR and log2(PSM MT/WT Ras) score. (B) Common Ras-proximal interacting protein-protein network based on candidates with ≥1 database interaction with another common interactor. Large squares are novel and small squares are known interactors. (C) PLA in MT NRAS MM415 melanoma cells with endogenous mTOR and Pan-Ras or Ras:GTP; interaction (red), nuclei (blue). Scale bar, 20 μm. (D) Quantification of PLA analysis in (C). n=8-10 fields/condition. (E) Western blot of HA co-immunoprecipitation of empty vector (EV), FLAG-HA-6xHIS tagged NRASWT or FHH: NRASQ61K with endogenous mTOR, p110α and Raf1 in wild-type RAS <t>CHL-1</t> cells. (F) Quantification of HA co-IP experiments as in (E). Values are normalized to HA pulldown signal and relative to NRASWT signal, n= 6 (Wilcoxon Signed Rank Test). (G) PLA in genotyped human colorectal adenocarcinomas with endogenous Pan-Ras and mTOR. Scale bar, 20 μm. (H) Quantification of PLA analysis in (G). Each dot represents median signal per patient. n=5 patients/genotype group, ≥7 images analyzed per patient (Mann-Whitney U Test). (I) Microscale thermophoresis with labeled FHH:Raf1RBD (18.2nM) with a titration series of GDP or GTPγs-loaded Ras. The binding curve is negative as the MST signal of the complex is lower than that of Raf1RBD alone. MST-on time of 15s, n = 3 independent replicates. (J) Microscale thermophoresis with labeled FHH:mTORKinaseDomain and FHH:mTORHEAT (23.4nM) with a titration series of GDP or GTPγs-loaded Ras. MST-on time of 2.5s, n ≥ 3 independent replicates. MST is mean ± SD. All other data mean ± SEM; *p< 0.05. See also Figures S3 and S4, Tables S2–4.
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    (A) A two-week growth CRISPR screen of 150 common Ras-proximal proteins in diploid primary human melanocytes (MC) and 5 MT Ras cell lines. Left heatmap negative selection FDR values (FDR ≤ 0.18) in each cell type by the MAGeCK algorithm (Li et al., 2014). The right heatmap relative enrichment MT vs WT Ras in mass spectrometry data for each Ras isoform; new proteins (red), known proteins (*). Ranked by combined FDR and log2(PSM MT/WT Ras) score. (B) Common Ras-proximal interacting protein-protein network based on candidates with ≥1 database interaction with another common interactor. Large squares are novel and small squares are known interactors. (C) PLA in MT NRAS MM415 melanoma cells with endogenous mTOR and Pan-Ras or Ras:GTP; interaction (red), nuclei (blue). Scale bar, 20 μm. (D) Quantification of PLA analysis in (C). n=8-10 fields/condition. (E) Western blot of HA co-immunoprecipitation of empty vector (EV), FLAG-HA-6xHIS tagged NRASWT or FHH: NRASQ61K with endogenous mTOR, p110α and Raf1 in wild-type RAS CHL-1 cells. (F) Quantification of HA co-IP experiments as in (E). Values are normalized to HA pulldown signal and relative to NRASWT signal, n= 6 (Wilcoxon Signed Rank Test). (G) PLA in genotyped human colorectal adenocarcinomas with endogenous Pan-Ras and mTOR. Scale bar, 20 μm. (H) Quantification of PLA analysis in (G). Each dot represents median signal per patient. n=5 patients/genotype group, ≥7 images analyzed per patient (Mann-Whitney U Test). (I) Microscale thermophoresis with labeled FHH:Raf1RBD (18.2nM) with a titration series of GDP or GTPγs-loaded Ras. The binding curve is negative as the MST signal of the complex is lower than that of Raf1RBD alone. MST-on time of 15s, n = 3 independent replicates. (J) Microscale thermophoresis with labeled FHH:mTORKinaseDomain and FHH:mTORHEAT (23.4nM) with a titration series of GDP or GTPγs-loaded Ras. MST-on time of 2.5s, n ≥ 3 independent replicates. MST is mean ± SD. All other data mean ± SEM; *p< 0.05. See also Figures S3 and S4, Tables S2–4.

    Journal: Molecular cell

    Article Title: The Functional Proximal Proteome of Oncogenic Ras Includes mTORC2

    doi: 10.1016/j.molcel.2018.12.001

    Figure Lengend Snippet: (A) A two-week growth CRISPR screen of 150 common Ras-proximal proteins in diploid primary human melanocytes (MC) and 5 MT Ras cell lines. Left heatmap negative selection FDR values (FDR ≤ 0.18) in each cell type by the MAGeCK algorithm (Li et al., 2014). The right heatmap relative enrichment MT vs WT Ras in mass spectrometry data for each Ras isoform; new proteins (red), known proteins (*). Ranked by combined FDR and log2(PSM MT/WT Ras) score. (B) Common Ras-proximal interacting protein-protein network based on candidates with ≥1 database interaction with another common interactor. Large squares are novel and small squares are known interactors. (C) PLA in MT NRAS MM415 melanoma cells with endogenous mTOR and Pan-Ras or Ras:GTP; interaction (red), nuclei (blue). Scale bar, 20 μm. (D) Quantification of PLA analysis in (C). n=8-10 fields/condition. (E) Western blot of HA co-immunoprecipitation of empty vector (EV), FLAG-HA-6xHIS tagged NRASWT or FHH: NRASQ61K with endogenous mTOR, p110α and Raf1 in wild-type RAS CHL-1 cells. (F) Quantification of HA co-IP experiments as in (E). Values are normalized to HA pulldown signal and relative to NRASWT signal, n= 6 (Wilcoxon Signed Rank Test). (G) PLA in genotyped human colorectal adenocarcinomas with endogenous Pan-Ras and mTOR. Scale bar, 20 μm. (H) Quantification of PLA analysis in (G). Each dot represents median signal per patient. n=5 patients/genotype group, ≥7 images analyzed per patient (Mann-Whitney U Test). (I) Microscale thermophoresis with labeled FHH:Raf1RBD (18.2nM) with a titration series of GDP or GTPγs-loaded Ras. The binding curve is negative as the MST signal of the complex is lower than that of Raf1RBD alone. MST-on time of 15s, n = 3 independent replicates. (J) Microscale thermophoresis with labeled FHH:mTORKinaseDomain and FHH:mTORHEAT (23.4nM) with a titration series of GDP or GTPγs-loaded Ras. MST-on time of 2.5s, n ≥ 3 independent replicates. MST is mean ± SD. All other data mean ± SEM; *p< 0.05. See also Figures S3 and S4, Tables S2–4.

    Article Snippet: Catalogue of Somatic Mutations in Cancer (COSMIC) v.72 https://cancer.sanger.ac.uk/cosmic Raw Images of Data This study, Mendeley Data http://dx.doi.org/10.17632/kzxnrmh7fc.1 Experimental Models: Cell Lines Human: CHL-1 ATCC CRL-9446 Human: HEK-293T Lab stock N/A Human: HT-1376 ATCC CRL-1472 Human: Caco-2 ATCC HTB-37 Human: SK-MEL-2 ATCC HTB-68 Human: LS 174T ATCC CL-188 Human: BxPC-3 ATCC CRL-1687 Human: MM415 CellBank Australia CBA-1351 Human: MM485 CellBank Australia CBA-1355 Human: AsPC-1 ATCC CRL-1682 Human: DLD-1 KRAS +/− Horizon Discovery HD 105-002 Human: DLD-1 KRAS G13D/− Horizon Discovery HD 105-011 Human: T24 ATCC HTB-4 Human: SK-MEL-5 ATCC HTB-70 Human: Capan-2 ATCC HTB-80 Primary Melanocytes Stanford University N/A Experimental Models: Organisms/Strains Mouse: SCID Hairless Outbred (SHO) Crl:SHO- Prkdc scid Hr hr Charles River Laboratories 474 Oligonucleotides shRNA sequences, see Table S7 This study N/A qPCR primers, see Table S7 This study N/A CRISPR Library Construction Primers, see Table S7 This study N/A Recombinant DNA pLKO.1 - TRC cloning vector (Puro).

    Techniques: CRISPR, Selection, Mass Spectrometry, Western Blot, Immunoprecipitation, Plasmid Preparation, Co-Immunoprecipitation Assay, MANN-WHITNEY, Microscale Thermophoresis, Labeling, Titration, Binding Assay

    (A) Schematic of full length MAPKAP1 isoform 1 wild-type (WT) and the MAPKAP1 deletion (Del) proteins with domains highlighted. CRIM, Conserved Region In The Middle. RBD, Ras Binding Domain. PH, Pleckstrin Homology. (B) Microscale thermophoresis of labeled FHH:MAPKAP1RBD (16.8nM) with a titration series of GDP or GTPγs-loaded Ras. The binding curve is positive as the MST signal of the complex is higher than MAPKAP1RBD alone. MST-on time of 5s, n = 3 independent replicates. (C) BioID-western blot streptavidin pulldowns and input levels for birA* control, NRASWT, NRASQ61K and NRASQ61K with FHH:eGFP, MAPKAP1WT:FHH or MAPKAP1Del:FHH expression in CHL-1 cells. PI3K p110α subunit, Raf-1, and HA protein pulldown are controls. Pulldown normalized signal relative to control birA*:NRASQ61K shown below. (D) Quantification of mTOR and Rictor protein levels in the streptavidin pulldowns normalized to HA pulldown. All values and statistical tests relative to birA*:NRASQ61K, n=6 (Welch’s two-sided t-test). (E) PLA with endogenous Pan-Ras and mTOR or Rictor in MT NRAS MM485 melanoma cells. Scale bar, 20 μm. (F) PLA quantification in (E). n=3 independent experiments, 6-8 fields analyzed per condition per experiment (unpaired two-sided t-test). EV, empty vector. (G) Quantification of LocaTOR2 experiments with FHH:eGFP, MAPKAP1WT:FHH or MAPKAP1Del:FHH expression. All values relative to average of FHH:eGFP and MAPKAP1WT:FHH fold induction; n=3 (unpaired two-sided t-test). (H) Quantification of FHH:eGFP, MAPKAP1WT:FHH and MAPKAP1Del:FHH expression relative to MAPKAP1WT:FHH for all experiments graphed in (G). **p< 0.01, ***p< 0.001, ****p< 0.0001, and ns= not significant; all bar graphed data mean ± SEM. MST data are mean ± SD. See also Figure S6 and Table S4.

    Journal: Molecular cell

    Article Title: The Functional Proximal Proteome of Oncogenic Ras Includes mTORC2

    doi: 10.1016/j.molcel.2018.12.001

    Figure Lengend Snippet: (A) Schematic of full length MAPKAP1 isoform 1 wild-type (WT) and the MAPKAP1 deletion (Del) proteins with domains highlighted. CRIM, Conserved Region In The Middle. RBD, Ras Binding Domain. PH, Pleckstrin Homology. (B) Microscale thermophoresis of labeled FHH:MAPKAP1RBD (16.8nM) with a titration series of GDP or GTPγs-loaded Ras. The binding curve is positive as the MST signal of the complex is higher than MAPKAP1RBD alone. MST-on time of 5s, n = 3 independent replicates. (C) BioID-western blot streptavidin pulldowns and input levels for birA* control, NRASWT, NRASQ61K and NRASQ61K with FHH:eGFP, MAPKAP1WT:FHH or MAPKAP1Del:FHH expression in CHL-1 cells. PI3K p110α subunit, Raf-1, and HA protein pulldown are controls. Pulldown normalized signal relative to control birA*:NRASQ61K shown below. (D) Quantification of mTOR and Rictor protein levels in the streptavidin pulldowns normalized to HA pulldown. All values and statistical tests relative to birA*:NRASQ61K, n=6 (Welch’s two-sided t-test). (E) PLA with endogenous Pan-Ras and mTOR or Rictor in MT NRAS MM485 melanoma cells. Scale bar, 20 μm. (F) PLA quantification in (E). n=3 independent experiments, 6-8 fields analyzed per condition per experiment (unpaired two-sided t-test). EV, empty vector. (G) Quantification of LocaTOR2 experiments with FHH:eGFP, MAPKAP1WT:FHH or MAPKAP1Del:FHH expression. All values relative to average of FHH:eGFP and MAPKAP1WT:FHH fold induction; n=3 (unpaired two-sided t-test). (H) Quantification of FHH:eGFP, MAPKAP1WT:FHH and MAPKAP1Del:FHH expression relative to MAPKAP1WT:FHH for all experiments graphed in (G). **p< 0.01, ***p< 0.001, ****p< 0.0001, and ns= not significant; all bar graphed data mean ± SEM. MST data are mean ± SD. See also Figure S6 and Table S4.

    Article Snippet: Catalogue of Somatic Mutations in Cancer (COSMIC) v.72 https://cancer.sanger.ac.uk/cosmic Raw Images of Data This study, Mendeley Data http://dx.doi.org/10.17632/kzxnrmh7fc.1 Experimental Models: Cell Lines Human: CHL-1 ATCC CRL-9446 Human: HEK-293T Lab stock N/A Human: HT-1376 ATCC CRL-1472 Human: Caco-2 ATCC HTB-37 Human: SK-MEL-2 ATCC HTB-68 Human: LS 174T ATCC CL-188 Human: BxPC-3 ATCC CRL-1687 Human: MM415 CellBank Australia CBA-1351 Human: MM485 CellBank Australia CBA-1355 Human: AsPC-1 ATCC CRL-1682 Human: DLD-1 KRAS +/− Horizon Discovery HD 105-002 Human: DLD-1 KRAS G13D/− Horizon Discovery HD 105-011 Human: T24 ATCC HTB-4 Human: SK-MEL-5 ATCC HTB-70 Human: Capan-2 ATCC HTB-80 Primary Melanocytes Stanford University N/A Experimental Models: Organisms/Strains Mouse: SCID Hairless Outbred (SHO) Crl:SHO- Prkdc scid Hr hr Charles River Laboratories 474 Oligonucleotides shRNA sequences, see Table S7 This study N/A qPCR primers, see Table S7 This study N/A CRISPR Library Construction Primers, see Table S7 This study N/A Recombinant DNA pLKO.1 - TRC cloning vector (Puro).

    Techniques: Binding Assay, Microscale Thermophoresis, Labeling, Titration, Western Blot, Expressing, Plasmid Preparation

    (A) BioID-western blot showing mTOR protein levels in the streptavidin pulldowns of birA*:NRASQ61K with shGFP, shRPTOR, shRICTOR or shMAPKAP1 with two independent hairpins in CHL-1 cells. PI3K p110α subunit, Raf1, and HA protein levels in streptavidin pulldowns are controls. Pulldown and input normalized values relative to the control shown below. (B) Quantification of mTOR, p110α and Raf1 protein levels in the streptavidin pulldown Normalized to HA pulldown and respective input levels and relative to shGFP mean, n=5 (unpaired two-sided t-test). (C) Quantification of protein remaining after knockdown compared to the average of controls for (B). (D) PLA in MT NRAS MM415 melanoma cells with endogenous Ras and mTOR with control, mTORC1 or mTORC2 component knockdown. Scale bar, 20 μm. (E) Quantification of PLA shown in (D). n=2 independent hairpins per knockdown. Relative to the mean of control knockdowns. (unpaired two-sided t-test). (F) Quantification of protein remaining after knockdown relative to mean signal of control knockdowns for PLA in (E). (G) Western blot of HA co-immunoprecipitation of empty vector (EV), FHH:NRASWT or FHH:NRASQ61K with endogenous Rictor, MAPKAP1 and Raptor in wild-type Ras CHL-1 cells. (H) Quantification of HA co-IP experiments as in (G). Values normalized to HA pulldown signal and relative to NRASWT signal. n= 5 or 8 (Welch’s two-sided t-test). (I) Western blot showing mTOR protein levels in the input and streptavidin pulldowns of birA* control, NRASWT, NRASQ61K and NRASQ61K Effector Domain Alanine point mutants. (*) non-specific background band. (J) Quantification of streptavidin pulldown protein levels as in (I). mTOR signal normalized to HA signal. All values relative to birA*: NRASQ61K, n=3 (Welch’s two-sided t-test relative to Q61K). All graphed data are mean ± SEM. *p< 0.05, **p< 0.01, ***p< 0.001, ****p< 0.0001, ns= not significant. See also Figure S5.

    Journal: Molecular cell

    Article Title: The Functional Proximal Proteome of Oncogenic Ras Includes mTORC2

    doi: 10.1016/j.molcel.2018.12.001

    Figure Lengend Snippet: (A) BioID-western blot showing mTOR protein levels in the streptavidin pulldowns of birA*:NRASQ61K with shGFP, shRPTOR, shRICTOR or shMAPKAP1 with two independent hairpins in CHL-1 cells. PI3K p110α subunit, Raf1, and HA protein levels in streptavidin pulldowns are controls. Pulldown and input normalized values relative to the control shown below. (B) Quantification of mTOR, p110α and Raf1 protein levels in the streptavidin pulldown Normalized to HA pulldown and respective input levels and relative to shGFP mean, n=5 (unpaired two-sided t-test). (C) Quantification of protein remaining after knockdown compared to the average of controls for (B). (D) PLA in MT NRAS MM415 melanoma cells with endogenous Ras and mTOR with control, mTORC1 or mTORC2 component knockdown. Scale bar, 20 μm. (E) Quantification of PLA shown in (D). n=2 independent hairpins per knockdown. Relative to the mean of control knockdowns. (unpaired two-sided t-test). (F) Quantification of protein remaining after knockdown relative to mean signal of control knockdowns for PLA in (E). (G) Western blot of HA co-immunoprecipitation of empty vector (EV), FHH:NRASWT or FHH:NRASQ61K with endogenous Rictor, MAPKAP1 and Raptor in wild-type Ras CHL-1 cells. (H) Quantification of HA co-IP experiments as in (G). Values normalized to HA pulldown signal and relative to NRASWT signal. n= 5 or 8 (Welch’s two-sided t-test). (I) Western blot showing mTOR protein levels in the input and streptavidin pulldowns of birA* control, NRASWT, NRASQ61K and NRASQ61K Effector Domain Alanine point mutants. (*) non-specific background band. (J) Quantification of streptavidin pulldown protein levels as in (I). mTOR signal normalized to HA signal. All values relative to birA*: NRASQ61K, n=3 (Welch’s two-sided t-test relative to Q61K). All graphed data are mean ± SEM. *p< 0.05, **p< 0.01, ***p< 0.001, ****p< 0.0001, ns= not significant. See also Figure S5.

    Article Snippet: Catalogue of Somatic Mutations in Cancer (COSMIC) v.72 https://cancer.sanger.ac.uk/cosmic Raw Images of Data This study, Mendeley Data http://dx.doi.org/10.17632/kzxnrmh7fc.1 Experimental Models: Cell Lines Human: CHL-1 ATCC CRL-9446 Human: HEK-293T Lab stock N/A Human: HT-1376 ATCC CRL-1472 Human: Caco-2 ATCC HTB-37 Human: SK-MEL-2 ATCC HTB-68 Human: LS 174T ATCC CL-188 Human: BxPC-3 ATCC CRL-1687 Human: MM415 CellBank Australia CBA-1351 Human: MM485 CellBank Australia CBA-1355 Human: AsPC-1 ATCC CRL-1682 Human: DLD-1 KRAS +/− Horizon Discovery HD 105-002 Human: DLD-1 KRAS G13D/− Horizon Discovery HD 105-011 Human: T24 ATCC HTB-4 Human: SK-MEL-5 ATCC HTB-70 Human: Capan-2 ATCC HTB-80 Primary Melanocytes Stanford University N/A Experimental Models: Organisms/Strains Mouse: SCID Hairless Outbred (SHO) Crl:SHO- Prkdc scid Hr hr Charles River Laboratories 474 Oligonucleotides shRNA sequences, see Table S7 This study N/A qPCR primers, see Table S7 This study N/A CRISPR Library Construction Primers, see Table S7 This study N/A Recombinant DNA pLKO.1 - TRC cloning vector (Puro).

    Techniques: Western Blot, Immunoprecipitation, Plasmid Preparation, Co-Immunoprecipitation Assay

    KEY RESOURCES TABLE

    Journal: Molecular cell

    Article Title: The Functional Proximal Proteome of Oncogenic Ras Includes mTORC2

    doi: 10.1016/j.molcel.2018.12.001

    Figure Lengend Snippet: KEY RESOURCES TABLE

    Article Snippet: Human: CHL-1 , ATCC , CRL-9446.

    Techniques: Western Blot, Transduction, In Situ, Virus, Recombinant, Lysis, Protease Inhibitor, Staining, Magnetic Beads, Cloning, Bicinchoninic Acid Protein Assay, Isolation, Labeling, Viability Assay, RNA Sequencing, Sequencing, Gene Expression, CRISPR, Mass Spectrometry, Expressing, Mutagenesis, shRNA, Plasmid Preparation, Control, Luciferase, Software, Membrane, Blocking Assay