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origin data analysis software  (Malvern Panalytical)


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    Structured Review

    Malvern Panalytical origin data analysis software
    Origin Data Analysis Software, supplied by Malvern Panalytical, 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/product/origin+analysis+software/pm41803151-368-5-9
    Average 86 stars, based on 1 article reviews
    origin data analysis software - by Bioz Stars, 2026-11
    86/100 stars

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    Related Articles

    Titration:

    Article Title: Structural basis of EZH2 recognition by EED.
    Article Snippet: .. The titration data, collected at 25 C, were analyzed using ORIGIN data analysis software (MicroCal Software). ..

    Software:

    Article Title: Structural basis of EZH2 recognition by EED.
    Article Snippet: .. The titration data, collected at 25 C, were analyzed using ORIGIN data analysis software (MicroCal Software). ..

    Article Title: Structural Basis for the Interaction between the Potato Virus X Resistance Protein (Rx) and Its Cofactor Ran GTPase-activating Protein 2 (RanGAP2)
    Article Snippet: .. Datawere collected at 30 °C and analyzed using Origin data analysis software (MicroCal). ..

    Article Title: The MST4–MOB4 complex disrupts the MST1–MOB1 complex in the Hippo–YAP pathway and plays a pro-oncogenic role in pancreatic cancer
    Article Snippet: .. Data were analyzed using the ORIGIN data analysis software (MicroCal Software). by guest on A ugust 4, 2018 http://w w w .jbc.org/ D ow nloaded from ..

    Article Title: Selective Inhibition of STRN3-Containing PP2A Phosphatase Restores Hippo Tumor-Suppressor Activity in Gastric Cancer.
    Article Snippet: .. Data were analyzed using the ORIGIN data analysis software (MicroCal Software). ..

    Article Title: NPM3 functions as a lactyltransferase to promote necroptosis in male diabetic cardiomyopathy mice models via FASN transcription modulation.
    Article Snippet: .. The data were analysed using ORIGIN data analysis software (MicroCal Software). .. ATP, PPi and AMP levels in the in vitro lactylation system were measured using an Enhanced ATP Assay Kit (S0027; Beyotime, China), a Pyrophosphate Assay Kit (ab234040; Abcam, Cambridge, UK), and an AMP Assay Kit (ab273275; Abcam, Cambridge, UK) in accordance with the manufacturers’ instructions.

    Article Title: NHE3 Activity Is Dependent on Direct Phosphoinositide Binding at the N Terminus of Its Intracellular Cytosolic Region
    Article Snippet: .. Na /H exchange rates (H efflux) were calculated as the product of buffering capacity at each pHi and Na -dependent change in pHi and were analyzed using data analysis software Origin (Microcal), by which data are fit to a general allosteric model as described by the Hill equation. ..

    Immunoprecipitation:

    Article Title: The MST4–MOB4 complex disrupts the MST1–MOB1 complex in the Hippo–YAP pathway and plays a pro-oncogenic role in pancreatic cancer
    Article Snippet: .. Data were analyzed using the ORIGIN data analysis software (MicroCal Software). by gest on A uust 4, 2018 hp://w w w .jb.org/ D ow nladed from MST4–MOB4 antagonizes MST1–MOB1 in PC 11 Immunoprecipitation and immunoblot analysis For immunoprecipitation experiments, whole-cell extracts of HEK293FT cells were collected 24 h after transfection or stimulation, and cells were lysed with RIPA buffer (150 mM NaCl, 100 mM Tris, pH8.0, 1% Triton X-100, 5 mM EDTA and 10 mM NaF) supplemented with 1mM PMSF and the protease inhibitor cocktail. .. After centrifugation at 12,000 rpm for 20 min at 4°C, supernatants were collected and incubated overnight with indicated antibodies together with Protein A/G beads (Santa Cruz).

    Western Blot:

    Article Title: The MST4–MOB4 complex disrupts the MST1–MOB1 complex in the Hippo–YAP pathway and plays a pro-oncogenic role in pancreatic cancer
    Article Snippet: .. Data were analyzed using the ORIGIN data analysis software (MicroCal Software). by gest on A uust 4, 2018 hp://w w w .jb.org/ D ow nladed from MST4–MOB4 antagonizes MST1–MOB1 in PC 11 Immunoprecipitation and immunoblot analysis For immunoprecipitation experiments, whole-cell extracts of HEK293FT cells were collected 24 h after transfection or stimulation, and cells were lysed with RIPA buffer (150 mM NaCl, 100 mM Tris, pH8.0, 1% Triton X-100, 5 mM EDTA and 10 mM NaF) supplemented with 1mM PMSF and the protease inhibitor cocktail. .. After centrifugation at 12,000 rpm for 20 min at 4°C, supernatants were collected and incubated overnight with indicated antibodies together with Protein A/G beads (Santa Cruz).

    Transfection:

    Article Title: The MST4–MOB4 complex disrupts the MST1–MOB1 complex in the Hippo–YAP pathway and plays a pro-oncogenic role in pancreatic cancer
    Article Snippet: .. Data were analyzed using the ORIGIN data analysis software (MicroCal Software). by gest on A uust 4, 2018 hp://w w w .jb.org/ D ow nladed from MST4–MOB4 antagonizes MST1–MOB1 in PC 11 Immunoprecipitation and immunoblot analysis For immunoprecipitation experiments, whole-cell extracts of HEK293FT cells were collected 24 h after transfection or stimulation, and cells were lysed with RIPA buffer (150 mM NaCl, 100 mM Tris, pH8.0, 1% Triton X-100, 5 mM EDTA and 10 mM NaF) supplemented with 1mM PMSF and the protease inhibitor cocktail. .. After centrifugation at 12,000 rpm for 20 min at 4°C, supernatants were collected and incubated overnight with indicated antibodies together with Protein A/G beads (Santa Cruz).

    Protease Inhibitor:

    Article Title: The MST4–MOB4 complex disrupts the MST1–MOB1 complex in the Hippo–YAP pathway and plays a pro-oncogenic role in pancreatic cancer
    Article Snippet: .. Data were analyzed using the ORIGIN data analysis software (MicroCal Software). by gest on A uust 4, 2018 hp://w w w .jb.org/ D ow nladed from MST4–MOB4 antagonizes MST1–MOB1 in PC 11 Immunoprecipitation and immunoblot analysis For immunoprecipitation experiments, whole-cell extracts of HEK293FT cells were collected 24 h after transfection or stimulation, and cells were lysed with RIPA buffer (150 mM NaCl, 100 mM Tris, pH8.0, 1% Triton X-100, 5 mM EDTA and 10 mM NaF) supplemented with 1mM PMSF and the protease inhibitor cocktail. .. After centrifugation at 12,000 rpm for 20 min at 4°C, supernatants were collected and incubated overnight with indicated antibodies together with Protein A/G beads (Santa Cruz).



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    Image Search Results


    ITC traces of CP titrated with CBR126 wt (panel A) or CBR126 mut (panel B). Upper panels are raw traces of thermograms, with differential power for each injection of CBR. Lower panels are binding isotherms, with integrated enthalpy vs molar ratio. Fitted values for K D , with a stoichiometry of one, are listed.

    Journal: bioRxiv

    Article Title: Biochemical Functions of the Membrane-Binding Domain of CARMIL

    doi: 10.64898/2026.01.05.697744

    Figure Lengend Snippet: ITC traces of CP titrated with CBR126 wt (panel A) or CBR126 mut (panel B). Upper panels are raw traces of thermograms, with differential power for each injection of CBR. Lower panels are binding isotherms, with integrated enthalpy vs molar ratio. Fitted values for K D , with a stoichiometry of one, are listed.

    Article Snippet: Binding constants were determined by fitting the change in enthalpy to a single site binding model using MicroCal ITC Origin analysis software.

    Techniques: Injection, Binding Assay

    H3Q5ser stabilizes Taf3-PHD/H3K4me2 and Taf3-PHD/H3K4me3 complexes. ( A ) Experimental (blue) and fitted (red) spectra of free, ∼50% bound, and fully bound TAF3-PHD resonances E862 and C896 for H3K4me3/H3K4me3Q5ser complex. Transfer peaks indicated with *. Experimental spectrum of E862 is also shown separately for clarity. ( B ) ITC analysis of GST-tagged Taf3-PHD binding to H3K4me3 in yellow and H3K4me3Q5ser in navy blue. Top panel displays the raw heat change per injection of H3 peptide. Bottom panel represents the binding isotherm. The solid line represents the best fit to the one-set-of-sites model using MicroCal-ITC Origin 7 software.

    Journal: Nucleic Acids Research

    Article Title: Molecular determinants for recognition of serotonylated chromatin

    doi: 10.1093/nar/gkaf612

    Figure Lengend Snippet: H3Q5ser stabilizes Taf3-PHD/H3K4me2 and Taf3-PHD/H3K4me3 complexes. ( A ) Experimental (blue) and fitted (red) spectra of free, ∼50% bound, and fully bound TAF3-PHD resonances E862 and C896 for H3K4me3/H3K4me3Q5ser complex. Transfer peaks indicated with *. Experimental spectrum of E862 is also shown separately for clarity. ( B ) ITC analysis of GST-tagged Taf3-PHD binding to H3K4me3 in yellow and H3K4me3Q5ser in navy blue. Top panel displays the raw heat change per injection of H3 peptide. Bottom panel represents the binding isotherm. The solid line represents the best fit to the one-set-of-sites model using MicroCal-ITC Origin 7 software.

    Article Snippet: ITC data were subsequently analysed and fitted with the one-site binding model in the MicroCal ITC Origin Analysis software 7.0 (Table , Figs and , , and ).

    Techniques: Binding Assay, Injection, Software

    Taf3-PHD P881 and W894 form key interaction surface with the serotonin group. ( A ) ITC analysis of GST-tagged Taf3-PHD mutants, BPTF-PHD , PHF2-PHD, or PHF8-PHD with the peptides H3K4me3 (in yellow) and H3K4me3Q5ser (in blue). Top panels display the raw heat change per injection of H3 peptide. Bottom panels represent the binding isotherm. The solid line represents the best fit to the one-set-of-sites model using MicroCal-ITC Origin 7 software. ( B ) Multiple sequence alignment (MSA) of human PHD fingers for which high-resolution structures in complex with H3K4me3 are available (ASH1L PDB: 8VLF; BPTF(2) PDB: 2FUU; DIDO1 PDB: 4L7X; ING1 PDB: 2QIC; ING4 PDB: 2PNX/2VNF; ING5 PDB: 3C6W; KMT2E PDB: 4L58; PHF2 PDB: 3KQI; PHF13 PDB: 3O7A; UHRF1 PDB: 3SOW). Consensus Cys4–His–Cys3 positions are highlighted in grey and indicated on top. Locations of the secondary structure elements of TAF3-PHD are indicated on top. S880 and A902 are highlighted in purple, while P881 and W894 are highlighted in yellow.

    Journal: Nucleic Acids Research

    Article Title: Molecular determinants for recognition of serotonylated chromatin

    doi: 10.1093/nar/gkaf612

    Figure Lengend Snippet: Taf3-PHD P881 and W894 form key interaction surface with the serotonin group. ( A ) ITC analysis of GST-tagged Taf3-PHD mutants, BPTF-PHD , PHF2-PHD, or PHF8-PHD with the peptides H3K4me3 (in yellow) and H3K4me3Q5ser (in blue). Top panels display the raw heat change per injection of H3 peptide. Bottom panels represent the binding isotherm. The solid line represents the best fit to the one-set-of-sites model using MicroCal-ITC Origin 7 software. ( B ) Multiple sequence alignment (MSA) of human PHD fingers for which high-resolution structures in complex with H3K4me3 are available (ASH1L PDB: 8VLF; BPTF(2) PDB: 2FUU; DIDO1 PDB: 4L7X; ING1 PDB: 2QIC; ING4 PDB: 2PNX/2VNF; ING5 PDB: 3C6W; KMT2E PDB: 4L58; PHF2 PDB: 3KQI; PHF13 PDB: 3O7A; UHRF1 PDB: 3SOW). Consensus Cys4–His–Cys3 positions are highlighted in grey and indicated on top. Locations of the secondary structure elements of TAF3-PHD are indicated on top. S880 and A902 are highlighted in purple, while P881 and W894 are highlighted in yellow.

    Article Snippet: ITC data were subsequently analysed and fitted with the one-site binding model in the MicroCal ITC Origin Analysis software 7.0 (Table , Figs and , , and ).

    Techniques: Injection, Binding Assay, Software, Sequencing