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seldi-tof ms proteinchip system  (Bio-Rad)


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    Bio-Rad seldi-tof ms proteinchip system
    Seldi Tof Ms Proteinchip System, supplied by Bio-Rad, 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/proteinchip+seldi+system/proteinchip+seldi+system/pmc09960765-153-6-10
    Average 90 stars, based on 1 article reviews
    seldi-tof ms proteinchip system - by Bioz Stars, 2026-09
    90/100 stars

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    Related Articles

    other:

    Article Title: Cystatin C in Cerebrospinal Fluid is Upregulated in Elderly Patients With Chronic Osteoarthritis Pain and Modulated Through Matrix Metalloproteinase 9–Specific Pathway
    Article Snippet: Methods: Samples of CSF were obtained from 8 elderly patients (65 y and above) with OA with lower limb pain for at least 6 months (OA group) and 8 sex-matched and age-matched relatively healthy elderly individuals without any pain problems (control group).. The intrathecal CysC, MMP2, and MMP9 were examined by Western blotting.. The analysis of CysC cleavage under different conditions was performed through silver staining and using massspectroscopy (SELDI-TOF) on 2 groups.

    Article Title: Gamma secretase modulators
    Article Snippet: After briefly drying up the array surface, energy absorbing molecule (EAM, saturated alpha-cyano-4-hydroxycinnamic acid in 50% acetonitrile, 0.1% TFA) is added to the spots and the array is analyzed using ProteinChip SELDI system (Bio-Rad).

    Article Title: Identifying polyglutamine protein species in situ that best predict neurodegeneration
    Article Snippet: PolyQ (K 2 Q 39 K 2 ) or PACAP peptide (basic peptide) was spotted on a PS10 ProteinChip Array (Bio-Rad) and loaded into a ProteinChip SELDI System (Bio-Rad) for data collection.

    Article Title: Characterization of the Ubiquinone Binding Site in Alternative NADH-Quinone Oxidoreductase of Saccharomyces cerevisiae by Photoaffinity Labeling
    Article Snippet: The digested peptides were extracted with 0.6% TFA in 10% acetonitrile, and analyzed by the ProteinChip SELDI system (Bio-Rad) on a NP 20 chip.

    Article Title: Optimization of furin inhibitors to protect against the activation of influenza hemagglutinin H5 and Shiga toxin.
    Article Snippet: Proprotein convertases (PCs) are crucial in the processing and entry of viral or bacterial protein precursors and confer increased infectivity of pathogens bearing a PC activation site, which results in increased symptom severity and lethality.. Previously, we developed a nanomolar peptide inhibitor of PCs to prevent PC activation of infectious agents.. Herein, we describe a peptidomimetic approach that increases the stability of this inhibitor for use in vivo to prevent systemic infections and cellular damage, such as that caused by influenza H5N1 and Shiga toxin.

    Article Title: Identifying polyglutamine protein species in situ that best predict neurodegeneration
    Article Snippet: PolyQ (K2Q39K2) or PACAP peptide (basic peptide) was spotted on a PS10 ProteinChip Array (Bio-Rad) and loaded into a ProteinChip SELDI System (Bio-Rad) for data collection.

    Purification:

    Article Title: Design, synthesis, and structure-activity relationship studies of a potent PACE4 inhibitor.
    Article Snippet: PACE4 plays an important role in the progression of prostate cancer and is an attractive target for the development of novel inhibitor-based tumor therapies.. We previously reported the design and synthesis of a novel, potent, and relatively selective PACE4 inhibitor known as a Multi-Leu (ML) peptide.. In the present work, we examined the ML peptide through detailed structure−activity relationship studies.

    Extraction:

    Article Title: Design, synthesis, and structure-activity relationship studies of a potent PACE4 inhibitor.
    Article Snippet: PACE4 plays an important role in the progression of prostate cancer and is an attractive target for the development of novel inhibitor-based tumor therapies.. We previously reported the design and synthesis of a novel, potent, and relatively selective PACE4 inhibitor known as a Multi-Leu (ML) peptide.. In the present work, we examined the ML peptide through detailed structure−activity relationship studies.

    Mass Spectrometry:

    Article Title: Effective capture of proteins inside living cells by antibodies indirectly linked to a novel cell-penetrating polymer-modified protein A derivative.
    Article Snippet: .. From the surface-enhanced laser desorption/ionization (SELDI) time-of-flight mass spectrometer (TOF-MS) analysis using the ProteinChip SELDI System (Bio-Rad Laboratories, Tokyo, Japan) of the resulting materials, a major peak was observed at m/z 12 576.1, which corresponds to the sum of the molecular masses of [free CPP + H] (m/z 4629.6) and [free pAd + H] (m/z 7803.2) including the molecular mass of the linker (Fig. 1B), although the peak at m/z 12 576.1 was very small due to low ionization of the resulting material. ..



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    Analysis of proteomic profiles in mouse serum using SELDI-TOF-MS. Serum samples from fasting wild-type (+m/+m) mice were loaded onto the spots of CM10 (a cationic exchanger, pH4) ProteinChip arrays. The spots were analyzed using the SELDI ProteinChip system on three different ranges: m/z 3000 – 10000, m/z 10000 – 20000 and m/z 20000 – 100000. The y-axis of the spectra indicates the mass-to-charge ratio (m/z) of protonated proteins, and the x-axis indicates the relative intensities of mass spectral signals. Note: The intensity of each peak is directly proportional to the amount of protein, but the peak intensities could not be comparable among the different proteins because of the difference in ionization.

    Journal: BMC Pharmacology

    Article Title: Effect of green tea on blood glucose levels and serum proteomic patterns in diabetic (db/db) mice and on glucose metabolism in healthy humans

    doi: 10.1186/1471-2210-4-18

    Figure Lengend Snippet: Analysis of proteomic profiles in mouse serum using SELDI-TOF-MS. Serum samples from fasting wild-type (+m/+m) mice were loaded onto the spots of CM10 (a cationic exchanger, pH4) ProteinChip arrays. The spots were analyzed using the SELDI ProteinChip system on three different ranges: m/z 3000 – 10000, m/z 10000 – 20000 and m/z 20000 – 100000. The y-axis of the spectra indicates the mass-to-charge ratio (m/z) of protonated proteins, and the x-axis indicates the relative intensities of mass spectral signals. Note: The intensity of each peak is directly proportional to the amount of protein, but the peak intensities could not be comparable among the different proteins because of the difference in ionization.

    Article Snippet: The spots were analyzed using the SELDI ProteinChip system (PBS-IIc, Ciphergen Biosystems).

    Techniques:

    Proteomic analyses demonstrating the differences in protein profiles of sera from diabetic and wild-type mice. Serum samples from fasting diabetic (db+/db+) mice and fasting wild-type (+m/+m) mice were loaded onto ProteinChip arrays. (A) List of peaks of proteins and/or peptides with indicated m/z values, the peak intensities of which were significantly changed in the diabetic state. Relative peak intensities were averaged (n = 8). The fold changes are presented as ratios of the peak intensities at indicated m/z values in db+/db+ to those in the +m/+m mice. Peaks at m/z 4203, 4576, 8515, 9291, 17406 and 18678 were obtained using CM10 ProteinChip (pH4). Peaks at 8733 and 9311 m/z were obtained using CM10 ProteinChip (pH7). Peaks at m/z 3933, 4119, 4206, 4369, 4566, 4579, 4637, 8523, 8827, 8915, 9283, 13075, 17407, 17418, 17622, 18431, 18691, 22334 and 26100 were obtained using Q10 ProteinChip. Peak at m/z 4211 was obtained using IMAC30. The chips were analyzed by SELDI-TOF-MS. (B) and (C) Typical data of relative peak intensities in +m/+m and db+/db+ mouse sera (upper, representative of 4–8 independent observations) and the peak intensity averages at m/z 4206 and 26100 (lower, n = 4 for +m/+m, n = 8 for db+/db+). The analyzed peak is indicated by arrows in the data of mass spectral signals. **P < 0.01; significantly different from the peak in wild-type mice, by unpaired t -test.

    Journal: BMC Pharmacology

    Article Title: Effect of green tea on blood glucose levels and serum proteomic patterns in diabetic (db/db) mice and on glucose metabolism in healthy humans

    doi: 10.1186/1471-2210-4-18

    Figure Lengend Snippet: Proteomic analyses demonstrating the differences in protein profiles of sera from diabetic and wild-type mice. Serum samples from fasting diabetic (db+/db+) mice and fasting wild-type (+m/+m) mice were loaded onto ProteinChip arrays. (A) List of peaks of proteins and/or peptides with indicated m/z values, the peak intensities of which were significantly changed in the diabetic state. Relative peak intensities were averaged (n = 8). The fold changes are presented as ratios of the peak intensities at indicated m/z values in db+/db+ to those in the +m/+m mice. Peaks at m/z 4203, 4576, 8515, 9291, 17406 and 18678 were obtained using CM10 ProteinChip (pH4). Peaks at 8733 and 9311 m/z were obtained using CM10 ProteinChip (pH7). Peaks at m/z 3933, 4119, 4206, 4369, 4566, 4579, 4637, 8523, 8827, 8915, 9283, 13075, 17407, 17418, 17622, 18431, 18691, 22334 and 26100 were obtained using Q10 ProteinChip. Peak at m/z 4211 was obtained using IMAC30. The chips were analyzed by SELDI-TOF-MS. (B) and (C) Typical data of relative peak intensities in +m/+m and db+/db+ mouse sera (upper, representative of 4–8 independent observations) and the peak intensity averages at m/z 4206 and 26100 (lower, n = 4 for +m/+m, n = 8 for db+/db+). The analyzed peak is indicated by arrows in the data of mass spectral signals. **P < 0.01; significantly different from the peak in wild-type mice, by unpaired t -test.

    Article Snippet: The spots were analyzed using the SELDI ProteinChip system (PBS-IIc, Ciphergen Biosystems).

    Techniques:

    Changes in serum protein profiles in db+/db+ mice by administration of green tea. Serum samples from fasting diabetic (db+/db+) mice 2 h after administration of green tea suspension were loaded onto ProteinChip Arrays. The chips were analyzed using SELDI-TOF-MS. (A) List of peaks of proteins and/or peptides with indicated m/z values, the peak intensities of which were significantly changed by the green tea administration. Relative peak intensities were averaged (n = 4). The fold changes are presented as ratios of the peak intensities at indicated m/z values 2 h after to before green tea administration. Peaks at m/z 7495, 7595, 7808, 7920, 14983, 15612 and 15614 were obtained using CM10 ProteinChip (pH4), whereas those at m/z 7503, 7611, 7823, 7926, 11651, 11664, 11863, 15004 and 15638 were obtained using CM10 ProteinChip (pH7). Peaks at m/z 4212, 4226, 7499, 11637, 11846, 13711, 13831, 14974, 15180, 31204 and 65906 were obtained using IMAC30 ProteinChip. (B) Typical data of relative peak intensities (upper, representative of 4 independent observations) and the peak intensity average at m/z 11863 (lower, n = 4) after green tea administration and saline control. The analyzed peak is indicated by arrows in the data of mass spectral signals. **P < 0.01; significantly different from the peak obtained before the administration, by unpaired t -test.

    Journal: BMC Pharmacology

    Article Title: Effect of green tea on blood glucose levels and serum proteomic patterns in diabetic (db/db) mice and on glucose metabolism in healthy humans

    doi: 10.1186/1471-2210-4-18

    Figure Lengend Snippet: Changes in serum protein profiles in db+/db+ mice by administration of green tea. Serum samples from fasting diabetic (db+/db+) mice 2 h after administration of green tea suspension were loaded onto ProteinChip Arrays. The chips were analyzed using SELDI-TOF-MS. (A) List of peaks of proteins and/or peptides with indicated m/z values, the peak intensities of which were significantly changed by the green tea administration. Relative peak intensities were averaged (n = 4). The fold changes are presented as ratios of the peak intensities at indicated m/z values 2 h after to before green tea administration. Peaks at m/z 7495, 7595, 7808, 7920, 14983, 15612 and 15614 were obtained using CM10 ProteinChip (pH4), whereas those at m/z 7503, 7611, 7823, 7926, 11651, 11664, 11863, 15004 and 15638 were obtained using CM10 ProteinChip (pH7). Peaks at m/z 4212, 4226, 7499, 11637, 11846, 13711, 13831, 14974, 15180, 31204 and 65906 were obtained using IMAC30 ProteinChip. (B) Typical data of relative peak intensities (upper, representative of 4 independent observations) and the peak intensity average at m/z 11863 (lower, n = 4) after green tea administration and saline control. The analyzed peak is indicated by arrows in the data of mass spectral signals. **P < 0.01; significantly different from the peak obtained before the administration, by unpaired t -test.

    Article Snippet: The spots were analyzed using the SELDI ProteinChip system (PBS-IIc, Ciphergen Biosystems).

    Techniques:

    Hemoglobin-related multiple SELDI-TOF-MS signals in db+/db+ mice. Samples of sera from nontreated db+/db+ mice in the fasting state were loaded onto ProteinChip arrays. Left panel: hemoglobin-related multi-MS signals. From the average of 8 data, the signals were detected from m/z 14974 to 15638 (+H) using CM10 ProteinChip (pH7). The double-charged m/z values appear to be observed from m/z 7495 to 7823 (+2H). These values may correspond to hemoglobin α- and β-chains, and other hemoglobin-related proteins. Right panel: multi-MS signals observed at approximately double the single-charged m/z values for the hemoglobin-related signals, using IMAC ProteinChip. These signals may correspond to the dimers of hemoglobin α- and β-chains.

    Journal: BMC Pharmacology

    Article Title: Effect of green tea on blood glucose levels and serum proteomic patterns in diabetic (db/db) mice and on glucose metabolism in healthy humans

    doi: 10.1186/1471-2210-4-18

    Figure Lengend Snippet: Hemoglobin-related multiple SELDI-TOF-MS signals in db+/db+ mice. Samples of sera from nontreated db+/db+ mice in the fasting state were loaded onto ProteinChip arrays. Left panel: hemoglobin-related multi-MS signals. From the average of 8 data, the signals were detected from m/z 14974 to 15638 (+H) using CM10 ProteinChip (pH7). The double-charged m/z values appear to be observed from m/z 7495 to 7823 (+2H). These values may correspond to hemoglobin α- and β-chains, and other hemoglobin-related proteins. Right panel: multi-MS signals observed at approximately double the single-charged m/z values for the hemoglobin-related signals, using IMAC ProteinChip. These signals may correspond to the dimers of hemoglobin α- and β-chains.

    Article Snippet: The spots were analyzed using the SELDI ProteinChip system (PBS-IIc, Ciphergen Biosystems).

    Techniques:

    CART analysis using peaks obtained by SELDI-TOF-MS to discriminate between patients with MMD and control patients. The decision tree was constructed using CSF samples from 32 patients with MMD and control patients. The classification is determined starting at the roof node, following by appropriate splitting decisions based on the peak intensity at each node. If the peak intensity is lower than the cutoff intensity value, the left node is selected. This splitting process is continued until no further classification is achieved and terminal nodes are produced. Using m/z 4473, 2406 and 6338 peaks (pH 5), m/z 4588 and 7250 peaks (pH 7), and m/z 4746 and 1044 peaks (pH 9), CART for Q10 ProteinChip was applied to identify patients with MMD and control patients. The analysis correctly classified all 20 patients with MMD under pH 5 condition and 19 of 20 under the pH 7 and 9 conditions; all 12 control patients were classified under all pH conditions.

    Journal: BMC Neurology

    Article Title: Identification of novel biomarker candidates by proteomic analysis of cerebrospinal fluid from patients with moyamoya disease using SELDI-TOF-MS

    doi: 10.1186/1471-2377-10-112

    Figure Lengend Snippet: CART analysis using peaks obtained by SELDI-TOF-MS to discriminate between patients with MMD and control patients. The decision tree was constructed using CSF samples from 32 patients with MMD and control patients. The classification is determined starting at the roof node, following by appropriate splitting decisions based on the peak intensity at each node. If the peak intensity is lower than the cutoff intensity value, the left node is selected. This splitting process is continued until no further classification is achieved and terminal nodes are produced. Using m/z 4473, 2406 and 6338 peaks (pH 5), m/z 4588 and 7250 peaks (pH 7), and m/z 4746 and 1044 peaks (pH 9), CART for Q10 ProteinChip was applied to identify patients with MMD and control patients. The analysis correctly classified all 20 patients with MMD under pH 5 condition and 19 of 20 under the pH 7 and 9 conditions; all 12 control patients were classified under all pH conditions.

    Article Snippet: The protein mass spectral data was generated with ProteinChip System 4000 SELDI-TOF mass spectrometer (Enterprise version; Bio-Rad Laboratories) using automated data collection protocol with Ciphergen Express version 3.0.6 software interface (Bio-Rad Laboratories).

    Techniques: Construct, Produced