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  • 93
    ATCC lactobacillus delbrueckii 12315
    Lactobacillus Delbrueckii 12315, supplied by ATCC, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/lactobacillus delbrueckii 12315/product/ATCC
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    lactobacillus delbrueckii 12315 - by Bioz Stars, 2024-04
    93/100 stars
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    N/A
    Thermo Scientific Culti Loops are ready to use QC organisms recommended for use in performance testing of media stains reagents and identification kits and for the evaluation of bacteriological procedures
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    90
    ATCC pca model
    Project overview. a A list of proteins of interest in <t>PCa</t> was generated by extensive literature review, comparison of gene expression data, and in silico analysis of nearest neighbor in androgen receptor (AR) pathway. b To establish which proteins are identifiable in <t>the</t> <t>LNCaP</t> PCa model, cells were grown in a Petri dish and harvested. From the cell pellets the proteome was extracted and extensively fractionated using strong cation exchange (SCX) chromatography and off-gel electrophoresis (OGE). Fractions were purified and peptides identified using LC-MS/MS in discovery (or shotgun) mode. The MS/MS spectra were annotated to obtain a list of proteins identifiable in LNCaP cells. c Quantifying protein abundance following pharmacological treatment was done on undepleted lysate level. Peptides were quantified using targeted proteomics (SRM-MS) and resulting ion chromatograms were analyzed with the software tool Skyline. d Six clinically relevant drugs were chosen and all single plus double drug combinations were added to a PCa model. Proteins served as phenotypic readouts of drug response and were quantified using mass spectrometry in selected reaction monitoring (SRM) mode. Immediate protein abundance changes were analyzed across the dataset identifying a group of proteins consistently upregulated. Publicly available DNA alteration and transcriptomics data from PCa patients was analyzed to link immediate response to drug treatment with adaptations found in PCa disease progression
    Pca Model, supplied by ATCC, 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/result/pca model/product/ATCC
    Average 90 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    pca model - by Bioz Stars, 2024-04
    90/100 stars
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    86
    EVJ Ltd evj 12315
    Project overview. a A list of proteins of interest in <t>PCa</t> was generated by extensive literature review, comparison of gene expression data, and in silico analysis of nearest neighbor in androgen receptor (AR) pathway. b To establish which proteins are identifiable in <t>the</t> <t>LNCaP</t> PCa model, cells were grown in a Petri dish and harvested. From the cell pellets the proteome was extracted and extensively fractionated using strong cation exchange (SCX) chromatography and off-gel electrophoresis (OGE). Fractions were purified and peptides identified using LC-MS/MS in discovery (or shotgun) mode. The MS/MS spectra were annotated to obtain a list of proteins identifiable in LNCaP cells. c Quantifying protein abundance following pharmacological treatment was done on undepleted lysate level. Peptides were quantified using targeted proteomics (SRM-MS) and resulting ion chromatograms were analyzed with the software tool Skyline. d Six clinically relevant drugs were chosen and all single plus double drug combinations were added to a PCa model. Proteins served as phenotypic readouts of drug response and were quantified using mass spectrometry in selected reaction monitoring (SRM) mode. Immediate protein abundance changes were analyzed across the dataset identifying a group of proteins consistently upregulated. Publicly available DNA alteration and transcriptomics data from PCa patients was analyzed to link immediate response to drug treatment with adaptations found in PCa disease progression
    Evj 12315, supplied by EVJ Ltd, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/evj 12315/product/EVJ Ltd
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    evj 12315 - by Bioz Stars, 2024-04
    86/100 stars
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    86
    Santa Cruz Biotechnology goat polyclonal antibody sc 12315
    Project overview. a A list of proteins of interest in <t>PCa</t> was generated by extensive literature review, comparison of gene expression data, and in silico analysis of nearest neighbor in androgen receptor (AR) pathway. b To establish which proteins are identifiable in <t>the</t> <t>LNCaP</t> PCa model, cells were grown in a Petri dish and harvested. From the cell pellets the proteome was extracted and extensively fractionated using strong cation exchange (SCX) chromatography and off-gel electrophoresis (OGE). Fractions were purified and peptides identified using LC-MS/MS in discovery (or shotgun) mode. The MS/MS spectra were annotated to obtain a list of proteins identifiable in LNCaP cells. c Quantifying protein abundance following pharmacological treatment was done on undepleted lysate level. Peptides were quantified using targeted proteomics (SRM-MS) and resulting ion chromatograms were analyzed with the software tool Skyline. d Six clinically relevant drugs were chosen and all single plus double drug combinations were added to a PCa model. Proteins served as phenotypic readouts of drug response and were quantified using mass spectrometry in selected reaction monitoring (SRM) mode. Immediate protein abundance changes were analyzed across the dataset identifying a group of proteins consistently upregulated. Publicly available DNA alteration and transcriptomics data from PCa patients was analyzed to link immediate response to drug treatment with adaptations found in PCa disease progression
    Goat Polyclonal Antibody Sc 12315, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/goat polyclonal antibody sc 12315/product/Santa Cruz Biotechnology
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    goat polyclonal antibody sc 12315 - by Bioz Stars, 2024-04
    86/100 stars
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    Image Search Results


    Project overview. a A list of proteins of interest in PCa was generated by extensive literature review, comparison of gene expression data, and in silico analysis of nearest neighbor in androgen receptor (AR) pathway. b To establish which proteins are identifiable in the LNCaP PCa model, cells were grown in a Petri dish and harvested. From the cell pellets the proteome was extracted and extensively fractionated using strong cation exchange (SCX) chromatography and off-gel electrophoresis (OGE). Fractions were purified and peptides identified using LC-MS/MS in discovery (or shotgun) mode. The MS/MS spectra were annotated to obtain a list of proteins identifiable in LNCaP cells. c Quantifying protein abundance following pharmacological treatment was done on undepleted lysate level. Peptides were quantified using targeted proteomics (SRM-MS) and resulting ion chromatograms were analyzed with the software tool Skyline. d Six clinically relevant drugs were chosen and all single plus double drug combinations were added to a PCa model. Proteins served as phenotypic readouts of drug response and were quantified using mass spectrometry in selected reaction monitoring (SRM) mode. Immediate protein abundance changes were analyzed across the dataset identifying a group of proteins consistently upregulated. Publicly available DNA alteration and transcriptomics data from PCa patients was analyzed to link immediate response to drug treatment with adaptations found in PCa disease progression

    Journal: NPJ Systems Biology and Applications

    Article Title: Systems pharmacology using mass spectrometry identifies critical response nodes in prostate cancer

    doi: 10.1038/s41540-018-0064-1

    Figure Lengend Snippet: Project overview. a A list of proteins of interest in PCa was generated by extensive literature review, comparison of gene expression data, and in silico analysis of nearest neighbor in androgen receptor (AR) pathway. b To establish which proteins are identifiable in the LNCaP PCa model, cells were grown in a Petri dish and harvested. From the cell pellets the proteome was extracted and extensively fractionated using strong cation exchange (SCX) chromatography and off-gel electrophoresis (OGE). Fractions were purified and peptides identified using LC-MS/MS in discovery (or shotgun) mode. The MS/MS spectra were annotated to obtain a list of proteins identifiable in LNCaP cells. c Quantifying protein abundance following pharmacological treatment was done on undepleted lysate level. Peptides were quantified using targeted proteomics (SRM-MS) and resulting ion chromatograms were analyzed with the software tool Skyline. d Six clinically relevant drugs were chosen and all single plus double drug combinations were added to a PCa model. Proteins served as phenotypic readouts of drug response and were quantified using mass spectrometry in selected reaction monitoring (SRM) mode. Immediate protein abundance changes were analyzed across the dataset identifying a group of proteins consistently upregulated. Publicly available DNA alteration and transcriptomics data from PCa patients was analyzed to link immediate response to drug treatment with adaptations found in PCa disease progression

    Article Snippet: As PCa model we chose the hormone sensitive LNCaP clone FGC (ATCC® CRL-1740™).

    Techniques: Generated, Expressing, In Silico, Chromatography, Nucleic Acid Electrophoresis, Purification, Liquid Chromatography with Mass Spectroscopy, Tandem Mass Spectroscopy, Software, Mass Spectrometry

    Development of SRM assays and initial drug testing. a Total proteome was isolated from LNCaP cells and fractionated using strong anion exchange (LN_SAE ). Separately, the LNCaP proteome was fractionated using strong cation exchange and off-gel electrophoresis (LN_OGE). In both cases, all fractions were analyzed using mass spectrometry (LC-MS/MS) and protein abundances calculated (iBAQ units ). The limit of detection (LoD) is indicated by a horizontal dashed red line. A quarter of the 490 proteins of interest in prostate cancer (Prot_PCa) are detectable in LNCaP cells using current mass spectrometry equipment. b For detectable proteins in LNCaP cell lysate SRM assays were developed. Examples of ion chromatograms show four co-eluting transitions with base line separation for peptides corresponding to KLK3 (prostate-specific antigen), RASK (GTPase KRas), and MP2K1 (MAP kinase kinase 1). c LNCaP cells were incubated with a caspase 3/7 fluorescent probe and six clinically relevant drugs (BEZ: NVP-Bez235, DAS: dasatinib, DOC: docetaxel, ENZ: enzalutamide, MK2: MK2206, TEM: temsirolimus). As a function of time the fluorescent signal corresponding to the degree of apoptosis was quantified by an automated fluorescent microscope. The ratio of treated to untreated apoptosis signal shows a large dynamic range at 24 h, a time point we chose for subsequent perturbation experiments

    Journal: NPJ Systems Biology and Applications

    Article Title: Systems pharmacology using mass spectrometry identifies critical response nodes in prostate cancer

    doi: 10.1038/s41540-018-0064-1

    Figure Lengend Snippet: Development of SRM assays and initial drug testing. a Total proteome was isolated from LNCaP cells and fractionated using strong anion exchange (LN_SAE ). Separately, the LNCaP proteome was fractionated using strong cation exchange and off-gel electrophoresis (LN_OGE). In both cases, all fractions were analyzed using mass spectrometry (LC-MS/MS) and protein abundances calculated (iBAQ units ). The limit of detection (LoD) is indicated by a horizontal dashed red line. A quarter of the 490 proteins of interest in prostate cancer (Prot_PCa) are detectable in LNCaP cells using current mass spectrometry equipment. b For detectable proteins in LNCaP cell lysate SRM assays were developed. Examples of ion chromatograms show four co-eluting transitions with base line separation for peptides corresponding to KLK3 (prostate-specific antigen), RASK (GTPase KRas), and MP2K1 (MAP kinase kinase 1). c LNCaP cells were incubated with a caspase 3/7 fluorescent probe and six clinically relevant drugs (BEZ: NVP-Bez235, DAS: dasatinib, DOC: docetaxel, ENZ: enzalutamide, MK2: MK2206, TEM: temsirolimus). As a function of time the fluorescent signal corresponding to the degree of apoptosis was quantified by an automated fluorescent microscope. The ratio of treated to untreated apoptosis signal shows a large dynamic range at 24 h, a time point we chose for subsequent perturbation experiments

    Article Snippet: As PCa model we chose the hormone sensitive LNCaP clone FGC (ATCC® CRL-1740™).

    Techniques: Isolation, Nucleic Acid Electrophoresis, Mass Spectrometry, Liquid Chromatography with Mass Spectroscopy, Incubation, Microscopy

    Protein centric view of abundance ratio across conditions. a Predominantly upregulated proteins such as enzymes (e.g., KLK2) and chaperons (e.g., 14-3-3 proteins) as short-term response to pharmacological conditions tested in LNCaP cells. b Frequently investigated proteins in PCa (e.g., KLK3 [PSA] or HSP90) show little change in protein abundance across the tested pharmacological perturbations in LNCaP cells. c Predominantly down-regulated proteins as short-term response to pharmacological conditions tested. Proteins such as PAK1 and HN1 are poorly characterized in PCa

    Journal: NPJ Systems Biology and Applications

    Article Title: Systems pharmacology using mass spectrometry identifies critical response nodes in prostate cancer

    doi: 10.1038/s41540-018-0064-1

    Figure Lengend Snippet: Protein centric view of abundance ratio across conditions. a Predominantly upregulated proteins such as enzymes (e.g., KLK2) and chaperons (e.g., 14-3-3 proteins) as short-term response to pharmacological conditions tested in LNCaP cells. b Frequently investigated proteins in PCa (e.g., KLK3 [PSA] or HSP90) show little change in protein abundance across the tested pharmacological perturbations in LNCaP cells. c Predominantly down-regulated proteins as short-term response to pharmacological conditions tested. Proteins such as PAK1 and HN1 are poorly characterized in PCa

    Article Snippet: As PCa model we chose the hormone sensitive LNCaP clone FGC (ATCC® CRL-1740™).

    Techniques: