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http://www.ebi.ac.uk/genomes

The EBI genomes pages give access to a large number of complete genomes including bacteria, archaea, viruses, phages, plasmids, viroids and eukaryotes. Methods using whole genome shotgun data are used to gain a large amount of genome coverage for an organism. WGS data for a growing number of organisms are being submitted to DDBJ/EMBL/GenBank. Genome entries have been listed in their appropriate category which may be browsed using the website navigation tool bar on the left. While organelles are all listed in a separate category, any from Eukaryota with chromosome entries are also listed in the Eukaryota page. Within each page, entries are grouped and sorted at the species level with links to the taxonomy page for that species separating each group. Within each species, entries whose source organism has been categorized further are grouped and numbered accordingly. Links are made to: * taxonomy * complete EMBL flatfile * CON files * lists of CON segments * Project * Proteomes pages * FASTA file of Proteins * list of Proteins

Proper citation: EBI Genomes (RRID:SCR_002426) Copy   

•   Source: SciCrunch Registry

https://ki.mit.edu/sbc/biopolymers

Facility provides integrated synthetic and analytical capabilities for biological materials, including proteins, peptides, and nanoparticles, range of technical expertise and instrumentation. Access is available to all members of MIT community. Priority access is given to KI members, NCI-funded research projects and other contributing user groups in recognition of funding support. In special circumstances, access may be available to non-MIT users.

Proper citation: MIT KIICR Biopolymers and Proteomics Core Facility (RRID:SCR_017737) Copy   

•   Source: SciCrunch Registry

https://fgcz.ch/working_with_us/service.html

Laboratory performs services in proteomics, genomics and metabolomics by FGCZ personnel without need for user to access labs. Services include Proteomics:Protein identification,quantification,characterization,Glycan/glycoprotein analyses, Analysis of Biomolecules, Fractionation; Genomics:DNA sequencing, RNA sequencing; Metabolomics/Biophysics services.

Proper citation: Zurich University Functional Genomics Center Core Facility (RRID:SCR_017742) Copy   

•   Source: SciCrunch Registry

https://web.uri.edu/riinbre/mic/

Core provides sequencing and bioinformatics support for INBRE and non-INBRE researchers. Provides data science services adjacent to traditional bioinformatics; access to computational and software resources for INBRE network institutions, particularly primarily undergraduate institutions; training for students and faculty in data science methods. Maintains professional network with other core and user facilities in Rhode Island and beyond to maximize resources available to our users.Utilizes novel technologies such as virtual/augmented reality for use in teaching and research.

Proper citation: Rhode Island INBRE Molecular Informatics Core Facility (RRID:SCR_017685) Copy   

•   Source: SciCrunch Registry

https://www.mdanderson.org/research/research-resources/core-facilities/proteomics-facility.html

Facility provides mass spectrometry analysis of proteins. Provides access to mass spectrometry based proteomics technologies and services including Protein Identification, Molecular Weight Determination, Quantitative Protein Analysis, Post-translational Modification Analysis, LC or LC-MS Analysis, Equipment Usage, Additional Data Analysis:Bioinformatics, statistics, pathway analysis and Assistance preparing materials for manuscripts or grants.Consultations for custom assays for other MS Services are also available.

Proper citation: University of Texas MD Anderson Cancer Center Proteomics Core Facility (RRID:SCR_017731) Copy   

•   Source: SciCrunch Registry

http://mmcri.org/ns/?page_id=230

Core provides protein and small molecule structural and functional analysis, and quantitation using technologies and software applications. Services in Nano-liquid chromatography,Protein identification and quantitation using SWATH,Protein post translational modification identification,Lipid profiling and identification (MS/MSALL),Targeted multiple reaction monitoring (MRM) for lipids.

Proper citation: Maine Medical Center Research Institute Proteomics and Lipidomics Analysis Core Facility (RRID:SCR_017730) Copy   

•   Source: SciCrunch Registry

https://www.albany.edu/repr/

Resource offers range of mass spectrometry instrumentation, expertise in analysis of RNA, RNA modifications, and proteins involved in RNA metabolism/regulation, supports projects involving analysis of biomolecules, metabolites, and small synthetic molecules, provides consulting on experimental design, sample preparation and data interpretation, whole project development and grant writing contributions.

Proper citation: Albany University RNA Epitranscriptomics and Proteomics Resource Core Facility (RRID:SCR_017695) Copy   

•   Source: SciCrunch Registry

https://www.unr.edu/proteomics

Core offers mass spectral proteomic analysis. Assists with qualitative and quantitative characterization of proteins in biological matrices such as plasma/serum, tissue, cell lines and other biological material to gain understanding of physiological pathways, molecular interactions and regulatory signaling.

Proper citation: University of Nevada at Reno Nevada Proteomics Center Core Facility (RRID:SCR_017761) Copy   

•   Source: SciCrunch Registry

http://chemistry.vcu.edu/research/facilities/chemical-and-proteomic-mass-spectrometry-core-facility/

Core provides mass spectrometric services, from basic mass measurement to complex proteome analyses.Services include basic mass measurement, ESI-MS/MS,LC-MS,Exact mass measurement,Protein identification.

Proper citation: Virginia Commonwealth University Chemical and Proteomic Mass Spectrometry Core Facility (RRID:SCR_017806) Copy   

•   Source: SciCrunch Registry

http://nmr.uthscsa.edu/contact.shtml

Core offers high field NMR instrumentation for structural studies of biological macromolecules. Instrumentation includes four-channel Bruker Avance 500, 600, and 700 MHz NMR spectrometers, ultra high sensitivity 5mm 1H-13C-15N triple-resonance cold probe for 600 MHz spectrometers. Service include acquisition and analysis of required spectra for elucidation of small molecule structures (includes synthetic molecules, natural products, cofactors, lipids, and short peptides (30 amino acids or less)). Types of projects conducted collaboratively include determination of three-dimensional structures of biological macromolecules, including proteins and nucleic acids, both alone and as complexes with various ligands.

Proper citation: Texas University Health Science Center at San Antonio Biomolecular NMR Core Facility (RRID:SCR_017775) Copy   

•   Source: SciCrunch Registry

http://biochem.slu.edu/proteincore/coreindex.shtml

Core facility that supports expression, purification, and analysis of reagent and preclinical proteins by providing instrumentation and consultation for protein production from small to large scale. Available equipment includes shaking incubators, 5 L fermentor, high pressure cell disruptor, hollow fiber concentrator, Maxwell16 magnetic bead purification system, AKTA Purifier chromatograph, analytical ultracentrifuge, analytical HPLC, and MALDI-QIT-TOF mass spectrometer.

Proper citation: Saint Louis University School of Medicine Protein Core Facility (RRID:SCR_017811) Copy   

•   Source: SciCrunch Registry

http://psf.cobre.ku.edu/cores/ppg/about

Core focuses on cloning, expression and purification of prokaryotic and eukaryotic proteins for COBRE and other investigators in Kansas and region. Laboratory maintains equipment to support production of properly folded proteins in quantities suitable for structural studies (X-ray and NMR), functional studies (catalytic or biological), label-free binding studies (SPR) and/or high throughput (HTP) screening studies.

Proper citation: Kansas University at Lawrence Protein Production Group Core Facility (RRID:SCR_017749) Copy   

•   Source: SciCrunch Registry

http://mgm.ku.edu/services

Research oriented service laboratory providing informatics support to research community. Services include data analysis and mining in proteomics, genomics and chemistry, systems biology approaches such as pathway, network and interaction analyses, large scale statistical and machine learning studies, protein structure, function and stability prediction, sequence and domain analyses,d esign and implementation of relational databases and software programs, consultation on experimental design involving data acquisition, management and analysis, report, grant, and manuscript preparation.

Proper citation: Kansas University at Lawrence Applied Bioinformatics Laboratory Core Facility (RRID:SCR_017751) Copy   

•   Source: SciCrunch Registry

http://www.kumc.edu/mspc.html/

Core provides access to mass spectrometry based proteomics applications, customizes mass spectrometry designs that fit individual needs. Used for general proteomics evaluations and protein identification designs, quantitation techniques, hydrogen/deuterium exchange, and oxidative footprinting. Equipment includes Orbitrap Fusion Lumos.

Proper citation: Kansas University Medical Center Mass Spectrometry/Proteomics Core Facility (RRID:SCR_017818) Copy   

•   Source: SciCrunch Registry

http://www.protein.iastate.edu

Core offers protein/peptide sequencing, large and small scale peptide synthesis (Fmoc), matrix assisted laser desorption/ionization (MALDI) mass spectrometry, SDS-PAGE/electroblotting, 2-D gel electrophoresis, isoelectric focusing (IEF), in-gel and solution digestion, tandem mass spectrometry (LC-MS/MS), ion mobility mass spectrometry (IM-MS), digital image acquisition and analysis using Typhoon imaging system and 2D gel documentation/analysis system, and semi-preparative, analytical and micro-analytical high performance liquid chromatography (HPLC). MALDI, HPLC, SDS-PAGE/blotting, IEF, 2D gel electrophoresis, 2D gel documentation/analysis and Typhoon imaging system are all available for user operation after appropriate training.

Proper citation: Iowa State University Office of Biotechnology Protein Core Facility (RRID:SCR_017780) Copy   

•   Source: SciCrunch Registry

http://proteomics.rockefeller.edu/

Core provides analysis of proteins, peptides, lipids, polar metabolites and small molecules by high resolution/high mass spectrometry. Targeted and hypothesis free analysis are offered combined with relative quantitation based on either label free, tandem mass tags or metabolic labelling. Acquisition tools include Data Dependent (DDA) and Data Independent (DIA).

Proper citation: The Rockefeller University Proteomics Resource Center Core Facility (RRID:SCR_017797) Copy   

•   Source: SciCrunch Registry

https://biophysics.fsu.edu/facilities/x-ray-crystallography-facility

Shared macromolecular x-ray crystallography facility provides instruments and expertise for screening, optimizing, imaging, growing, and storing crystals of biological macromolecules. The X-Ray Facility coordinates single crystal x-ray diffraction data collection at third generation synchrotron x-ray source using FSU's membership at the National Synchrotron Light Source II at Brookhaven National Lab, Upton, NY. XRF also offers custom buffer preparation, optimization, and crystal set-up using multi-well format crystallization blocks and plates.XRF has ARI Crystal Gryphon robot, Formulatrix Rock Imager, Formulator 16, Rock Maker software, RUMED incubator, Cryo storage and shipping dewars, Leica S8 AP0 Zoom microscope and other amenities.

Proper citation: Florida State University X-Ray Crystallography Core Facility (RRID:SCR_017922) Copy   

•   Source: SciCrunch Registry

http://proteomics.northwestern.edu/collaborate

Core offers multiple types of experiments from simple protein identification to protein quantitation. Performs traditional bottom-up proteomics, where proteins are digested with enzyme prior to analysis and intact, top-down proteomics analyses. Services include proteins identification after in-gel or in-solution digestion, top-down mass spectrometry to preserve post-translationally modified forms of proteins present in vivo by measuring them intact, IP-MS Pulldown,BioID service to identify target of biotin ligase that has been tagged onto their protein via traditional cloning methods,Untargeted Quantitative Peptide Proteomics,Targeted Quantitative Peptide Proteomics,Epiproteomic Histone Modification Panel A,Epiproteomic Histone Modification Panel B,Untargeted Metabolomics,Phosphoproteomics,PTM Scan,ChIP-MS.

Proper citation: Northwestern University Proteomics Core Facility (RRID:SCR_017945) Copy   

•   Source: SciCrunch Registry

http://prospector.ucsf.edu

A package of over twenty mass spectrometry-based tools primarily geared toward proteomic data analysis and database mining. It can be run from the command line, but is primarily used through a web browser, and there is a public website that allows anyone to use the software without local installation. Tandem mass spectrometry analysis tools are used for database searching and identification of peptides, including post-translationally modified peptides and cross-linked peptides. Support for isotope and label-free quantification from this type of data is provided. MS-Viewer software allows sharing and displaying of annotated spectra from many different tandem mass spectrometry data analysis packages. Other tools include software for analyzing peptide mass fingerprinting data (MS-Fit); prediction of theoretical fragmentation of peptides (MS-Product); theoretical chemical or enzymatic digestion of proteins (MS-Digest); and theoretical modeling of the isotope distribution of any chemical, including peptides (MS-Isotope). Searches using amino acid sequence can be used to identify homologous peptides in a database (MS-Pattern); the use of the combination of amino acid sequence and masses can be used for homologous peptide and protein identification using MS-Homology. Tandem mass spectrometry peak list files can be filtered for the presence of certain peaks or neutral losses using MS-Filter. Given a list of proteins, MS-Bridge can report all potential cross-linked peptide combinations of a specified mass. Given a precursor peptide mass and information about known amino acid presence, absence, or modifications, MS-Comp can report all amino acid combinations that could lead to the observed mass.

Proper citation: Protein Prospector (RRID:SCR_014558) Copy   

•   Source: SciCrunch Registry

http://gps.biocuckoo.org/

Software that detects kinase-specific phosphorylation sites. GPS provides a platform able to perform its prediction based on a group-based phosphorylation scoring algorithm. It allows users to query multiple protein sequences through a batch prediction mode.

Proper citation: GPS (RRID:SCR_016374) Copy   

•   Source: SciCrunch Registry