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Sally Schwarz, M.S., Research Associate Professor of Radiology and Co-Director of the Cyclotron facility at Washington University in St. Louis, will present "USP chapter and 21 CFR part 212. Relevant differences and similarities" as part of the Cyclotron and Radiochemistry program seminar series.

FAQs Q: Why are your services so expensive?! A: They aren’t! Our rates are comparable to, or cheaper than, the majority of other academic proteomics facilities. We will work hard to maximize our sample throughput, and automate our procedures, so that we do not have to raise prices. Proteomics is expensive – MS instrumentation costs several hundreds of thousands of dollars, and must be replaced often to keep up with the state-of-the-art. Some processes are labor-intensive, and we must cover staff

Staff Andy Lemoff, Ph.D. – Core Director Associate Professor, Department of Biochemistry Faculty Profile & Publications Room: Y4.310D Email: andrew.lemoff@utsouthwestern.edu Xuemei Luo, Ph.D. Instructor, Department of Biochemistry Room: Y4.306 Email: xuemei.luo@utsouthwestern.edu Joe Otto, Ph.D. Senior Research Scientist, Department of Biochemistry Room: Y4.306 Email: joseph.otto@utsouthwestern.edu Songyue Shi, Ph.D. Senior Research Associate, Department of Biochemistry Room: Y4.306 Email

Cutting Gels Introduction Many proteomics samples are well suited for SDS-PAGE, including protein identification and PTM identification. We recognize that a gel approach may not be compatible with all samples, so please contact us if you have concerns about running your sample into a gel. We require that: Precast SDS-PAGE gels are used whenever possible to reduce contamination. The advice on this page must be followed to avoid keratin and detergent/polymer contamination. All gels should be

Intact Mass What do we use to measure the mass of intact proteins? We do LC/MS analysis of intact proteins using a Q-TOF mass spectrometer with electrospray ionization. This means that samples must be free of detergents. An ideal solvent is 5% acetonitrile in water containing 1-5% formic acid or acetic acid, though many standard biological buffers and salts are acceptable (see below). What are some limitations of your intact mass analysis? We are not able to look at native or non-covalent

TMT Quantitation Introduction Tandem Mass Tag (TMT) technology is a powerful technique for comparing protein (and peptide) amounts between six to eighteen conditions. This technique involves labeling samples after digestion, meaning this technique can be used on in vivo samples, unlike SILAC. TMT or TMTpro samples are to be submitted in solution or on-bead, not in gel. It is the responsibility of the customer to ensure that similar amounts of protein is present in each sample and that the

Charging Policy What is our policy for charging users? The Proteomics Core has a simple charging policy: No samples will be prepared or run until the information has been entered into our sample submission site. We charge for every sample run , regardless of whether an expected result is obtained. The only exception to this rule is where processing or instrument problems in the core have caused the lack of result. Why do I have to pay for samples that deliver no useful result? Many users are

Gel Band ID Introduction Identification of proteins from visible bands excised from Coomassie or silver-stained gels using mass-spectrometry is generally very successful. Almost all visible Coomassie bands contain enough protein for MS identification. Most silver-stain bands can be identified on our instruments. Sequence coverage achieved is dependent on the sequence of the unknown protein (does it produce observable tryptic peptides), and the amount of protein in the band. Silver stained bands

General Limitations MS proteomics is a powerful tool for the analysis of protein samples, but there are some limits to the techniques we employ in the Proteomics Core. Knowing the limitations of the services we provide can help to ensure your experiment is a success, and you do not incur costs for unsuccessful analyses. Detection Limits & Protein Requirement For Protein Identification Generally the instrumentation we use for service work can easily identify Coomassie-stained bands, will identify

Contact Us T. Boone Pickens Biomedical Building 11th floor, Room 200 6001 Forest Park Road Dallas, TX 75235 Please use our intake form below to send us details about your project and sample submission for using our services. Intake Form For additional details or inquiries, you can contact us via email. Email Funding This core facility is funded by Grant number RP250571 awarded to Dr. Kevin Dean from the Cancer Prevention & Research Institute of Texas (CPRIT). Back-to top