Ms grade modified trypsin

Manufactured by Promega

Sourced in United States

MS-grade modified trypsin is a proteolytic enzyme used for the digestion of proteins in mass spectrometry analysis. It is specifically designed and processed to ensure high purity and consistent performance in mass spectrometry applications.

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Lab products found in correlation

Total akt, by Cell Signaling Technology (1 mentions) Phospho akt, by Cell Signaling Technology (1 mentions) Phosphatase inhibitor cocktail, by Cell Signaling Technology (1 mentions) Dimethyl sulfoxide (dmso), by Merck Group (1 mentions) Normal rabbit igg, by Thermo Fisher Scientific (1 mentions) Protein a g plus agarose immunoprecipitation reagent, by Santa Cruz Biotechnology (1 mentions) Leupeptin, by Avantor (1 mentions) Bca protein assay kit, by Thermo Fisher Scientific (1 mentions) Mem per eukaryotic membrane protein extraction reagent kit, by Thermo Fisher Scientific (1 mentions) Phospho mapk erk, by Cell Signaling Technology (1 mentions) Ltq lc ms ms, by Thermo Fisher Scientific (1 mentions) Htc pal autosampler, by CTC Analytics (1 mentions) Ltq orbitrap xl mass spectrometer, by Thermo Fisher Scientific (1 mentions) Paradigm ms4 hplc pump, by Bruker (1 mentions) Gelcode blue stain reagent, by Thermo Fisher Scientific (1 mentions) Ammonium acetate, by Merck Group (1 mentions) Chloramine t, by Merck Group (1 mentions) Guaiacol, by Merck Group (1 mentions)

Spelling variants of this product

Trypsin (3007 citations) Modified trypsin (165 citations) MS-grade trypsin (67 citations)

6 protocols using ms grade modified trypsin

Protein Extraction and Analysis Methods

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Dulbecco's modified Eagle's medium (DMEM), penicillin, streptomycin, and fetal bovine serum were purchased from Hyclone (Logan, UT). MS-grade modified trypsin was from Promega (Madison, WI). Dimethylsulfoxide (DMSO) was purchased from Sigma (St. Louis, MO). Rabbit polyclonal antibodies against total MAPK/ERK, phospho-MAPK/ERK, total-Akt, phospho-Akt, and phosphatase inhibitor cocktail were obtained from Cell Signaling Technology (Boston, MA). 3-(4,5-Dimethylthiazol)-2,5-diphenyltetra-zolium bromide (MTT), aprotinin, and leupeptin were from Amresco (Solon, OH). A Mem-PER mammalian protein extraction reagent, Mem-PER eukaryotic membrane protein extraction reagent kit, and BCA protein assay kit were purchased from Thermo Fisher Scientific (Rockford, IL).
Protein A/G PLUS-Agarose Immunoprecipitation Reagent, monoclonal mouse antibody against human actin, or GAPDH was purchased from Santa Cruz Biotechnology (Santa Cruz, CA). Normal rabbit IgG was purchased from PeproTech (Rocky Hill, NJ). FAM172A recombinant proteins were preserved in our laboratory.

Zhao H., Wang Y., Liu Y., Hao X., Wei H, & Xie W. (2019). The Effect of Protein FAM172A on Proliferation in HepG2 Cells and Investigation of the Possible Molecular Mechanism. Analytical Cellular Pathology (Amsterdam), 2019, 5901083.

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Co-IP Mass Spectrometry Analysis

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Co-IP samples of sGFP and CjWRKY1-sGFP proteins were obtained as described above. Co-immunoprecipitated samples were separated by SDS-PAGE and silver stained (Supplementary Fig. S2). Protein bands were extracted, and proteins were digested in-gel with MS grade modified trypsin (Promega). The extracted peptides were subjected to LTQ LC/MS/MS (Thermo Fisher Scientific). The collected ion spectrum data were analysed with the help of Mr. Y. Watanabe (Proteomic Facility Lab., Grad. Sch. Biostudies, Kyoto Univ.) using MassMatrix version 2.4.2 (www.massmatrix.net/)38 (link).

Yamada Y, & Sato F. (2016). Tyrosine phosphorylation and protein degradation control the transcriptional activity of WRKY involved in benzylisoquinoline alkaloid biosynthesis. Scientific Reports, 6, 31988.

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Nucleoid Protein Identification by SDS-PAGE and MS

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The nucleoid proteins were separated by sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE) and subjected to in-gel digestion with mass spectrometry (MS) grade modified trypsin (Promega). The peptides were extracted as described previously (26 (link)) and loaded onto a column (100-µm internal diameter, 15-cm length; L-Column, CERI) using a Paradigm MS4 HPLC pump (Michrom BioResources) and an HTC-PAL autosampler (CTC Analytics) and eluted over 26 min with a gradient of 5 to 45% (vol/vol) acetonitrile in 0.1% (vol/vol) formic acid. The eluted peptides were introduced directly into an LTQ-Orbitrap XL mass spectrometer (Thermo Fisher Scientific) with a flow rate of 500 nL-⋅-min⁻¹ and a spray voltage of 2.0 kV. The obtained spectra were compared to those in a protein database (Chlamydomonas genomic information 2.4) using the in-house MASCOT server (version 2.3, Matrix Science) (54 (link)). MASCOT search parameters were set as follows: threshold of the ion score cutoff, 0.05; peptide tolerance, 10 ppm; MS/MS tolerance, 0.5 Da; and peptide charge, +1, +2, or +3. The search was also set to allow one missed cleavage by trypsin, carboxymethylation modification of Cys residues, and variable oxidation of Met residues.

Takusagawa M., Kobayashi Y., Fukao Y., Hidaka K., Endo M., Sugiyama H., Hamaji T., Kato Y., Miyakawa I., Misumi O., Shikanai T, & Nishimura Y. (2021). HBD1 protein with a tandem repeat of two HMG-box domains is a DNA clip to organize chloroplast nucleoids in Chlamydomonas reinhardtii. Proceedings of the National Academy of Sciences of the United States of America, 118(20), e2021053118.

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Comparative Proteomic Analysis of Sera

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Sera from pGIA mice, control mice, patients with RA, and HS were separated by 2D-PAGE, and gels were stained with GelCode Blue Stain Reagent (Thermo Fisher Scientific) for Coomassie brilliant blue staining. Gel slices were incubated overnight with MS-grade modified trypsin (6.7 ng/μl; Promega, Madison, WI, USA) at 37 °C. The resultant peptides were analyzed with the nanoACQUITY ultrahigh-performance LC (UPLC) system (Waters, Milford, MA, USA). Data were collected in centroid mode from mass-to-charge ratios (m/z) 50 to 1990. All analyses were acquired with an independent reference. BiopharmLynx version 1.2 software (Waters) was used for baseline subtraction and smoothing, de-isotoping, de novo peptide sequence identification, and database searches.

Kawaguchi H., Matsumoto I., Osada A., Kurata I., Ebe H., Tanaka Y., Inoue A., Umeda N., Kondo Y., Tsuboi H., Shinkai Y., Kumagai Y., Ishigami A, & Sumida T. (2018). Identification of novel biomarker as citrullinated inter-alpha-trypsin inhibitor heavy chain 4, specifically increased in sera with experimental and rheumatoid arthritis. Arthritis Research & Therapy, 20, 66.

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Acetylation Site Identification of TFEB

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To identify the acetylation site of TFEB by mass spectrometry, the gel band of acetylated TFEB was cut off. In‐gel digestion of TFEB was performed with MS‐grade modified trypsin (Promega) at 37°C overnight. The digested peptides were loaded on an in‐house packed capillary reverse‐phase C18 column (15 cm in length, 3 mm particle size, 100 mm ID 3 360 mm OD, 100 A˚ pore diameter) connected to an Easy LC 1000 system. The samples were analyzed with a 180 min‐HPLC gradient from 0% to 100% buffer B (0.1% formic acid in acetonitrile) at 300 nl/min. The eluted peptides were ionized and directly introduced into a Q‐Exactive or Fusion mass spectrometer (Thermo) using a nano‐spray source. Survey full‐scan MS spectra (m/z 300–1,800) were acquired in the Orbitrap analyzer with resolution r = 70,000 at m/z 400.

Wang Y., Huang Y., Liu J., Zhang J., Xu M., You Z., Peng C., Gong Z, & Liu W. (2019). Acetyltransferase GCN5 regulates autophagy and lysosome biogenesis by targeting TFEB. EMBO Reports, 21(1), e48335.

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Spectrophotometric Determination of Peroxidase Activity

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Horse heart ferri-cyt c, H₂O₂, guaiacol (o-methoxyphenol), ammonium acetate, and chloramine-T (N-chloro-4-toluol-sulfonamide), were from Sigma Aldrich (St. Louis, MO). Solvents were from Fisher Scientific (Nepean, ON). Potassium phosphate was supplied by Caledon Laboratories (Georgetown, ON), and MS-grade modified trypsin was from Promega (Madison, WI). All experiments were conducted at 22 ± 2 °C.

Yin V., Mian S.H, & Konermann L. (2019). Lysine carbonylation is a previously unrecognized contributor to peroxidase activation of cytochrome c by chloramine-T †Electronic supplementary information (ESI) available. See DOI: 10.1039/c8sc03624a. Chemical Science, 10(8), 2349-2359.

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