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http://www.antibodypedia.com/

Open-access database of antibodies against human proteins developed through collaboration between Antibodypedia AB and the Nature Publishing Group. It aims to provide the scientific community and antibody distributors alike with information on the effectiveness of specific antibodies in specific applications--to help scientists select the right antibody for the right application. Antibodypedia's mission is to promote the functional understanding of the human proteome and expedite analysis of potential biomarkers discovered through clinical efforts. To this end, they have developed an open-access, curated, searchable database containing annotated and scored affinity reagents to aid users in selecting antibodies tailored to specific biological and biomedical assays. They envisage Antibodypedia as a virtual repository of validated antibodies against all human, and ultimately most model-organism, proteins. Such a tool will be exploitable to identify affinity reagents to document protein expression patterns in normal and pathological states and to purify proteins alone and in complex for structural and functional analyses. They hope to promote characterization of the roles and interplay of proteins and complexes in human health and disease. They encourage commercial providers to submit information regarding their inventory of antibodies with links to quality control data. Independent users can submit their own application-specific experimental data using standard validation criteria (supportive or non-supportive) developed with the assistance of an international advisory board recruited from academic research institutions. Users can also comment on specific antibodies without submitting validation data.

Proper citation: Antibodypedia (RRID:SCR_012782) Copy   

•   Source: SciCrunch Registry

http://www.informatics.jax.org/

Community model organism database for laboratory mouse and authoritative source for phenotype and functional annotations of mouse genes. MGD includes complete catalog of mouse genes and genome features with integrated access to genetic, genomic and phenotypic information, all serving to further the use of the mouse as a model system for studying human biology and disease. MGD is a major component of the Mouse Genome Informatics.Contains standardized descriptions of mouse phenotypes, associations between mouse models and human genetic diseases, extensive integration of DNA and protein sequence data, normalized representation of genome and genome variant information. Data are obtained and integrated via manual curation of the biomedical literature, direct contributions from individual investigators and downloads from major informatics resource centers. MGD collaborates with the bioinformatics community on the development and use of biomedical ontologies such as the Gene Ontology (GO) and the Mammalian Phenotype (MP) Ontology.

Proper citation: Mouse Genome Database (RRID:SCR_012953) Copy   

•   Source: SciCrunch Registry

http://www.syfpeithi.de/

SYFPEITHI is a database comprising more than 7000 peptide sequences known to bind class I and class II MHC molecules. The entries are compiled from published reports only. It contains a collection of MHC class I and class II ligands and peptide motifs of humans and other species, such as apes, cattle, chicken, and mouse, for example, and is continuously updated. Searches for MHC alleles, MHC motifs, natural ligands, T-cell epitopes, source proteins/organisms and references are possible. Hyperlinks to the EMBL and PubMed databases are included. In addition, ligand predictions are available for a number of MHC allelic products. The database is based on previous publications on T-cell epitopes and MHC ligands. It contains information on: -Peptide sequences -anchor positions -MHC specificity -source proteins, source organisms -publication references Since the number of motifs continuously increases, it was necessary to set up a database which facilitates the search for peptides and allows the prediction of T-cell epitopes. The prediction is based on published motifs (pool sequencing, natural ligands) and takes into consideration the amino acids in the anchor and auxiliary anchor positions, as well as other frequent amino acids. The score is calculated according to the following rules: The amino acids of a certain peptide are given a specific value depending on whether they are anchor, auxiliary anchor or preferred residue. Ideal anchors will be given 10 points, unusual anchors 6-8 points, auxiliary anchors 4-6 and preferred residues 1-4 points. Amino acids that are regarded as having a negative effect on the binding ability are given values between -1 and -3. Sponsors: SYFPEITHI is supported by DFG-Sonderforschungsbereich 685 and theEuropean Union: EU BIOMED CT95-1627, BIOTECH CT95-0263, and EU QLQ-CT-1999-00713.

Proper citation: SYFPEITHI: A Database for MHC Ligands and Peptide Motifs (RRID:SCR_013182) Copy   

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http://epsf.bmad.bii.a-star.edu.sg/cube/db/html/home.html

Cube-DB is a database of pre-evaluated conservation and specialization scores for residues in paralogous proteins belonging to multi-member families of human proteins. Protein family classification follows (largely) the classification suggested by HUGO Gene Nomenclature Committee. Sets of orhtologous protein sequences were generated by mutual-best-hit strategy using full vertebrate genomes available in Ensembl. The scores, described on documentation page, are assigned to each individual residue in a protein, and presented in the form of a table (html or downloadable xls formats) and mapped, when appropriate, onto the related structure (Jmol, Pymol, Chimera).

Proper citation: Cube-DB (RRID:SCR_013233) Copy   

•   Source: SciCrunch Registry

http://www.alzforum.org/res/com/ant/

The Alzheimer Research Forum is the web''s most dynamic scientific community dedicated to understanding Alzheimer''s disease and related disorders. It also contains a database of providers of antibodies directed against several hundred molecules and proteins of relevant to research on Alzheimer and other neurodegenerative diseases. The web site reports on the latest scientific findings, from basic research to clinical trials; creates and maintains public databases of essential research data and reagents, and produces discussion forums to promote debate, speed the dissemination of new ideas, and break down barriers across the numerous disciplines that can contribute to the global effort to cure Alzheimer''s disease. The ARF team of professional science writers and editors, information technology experts, web developers and producers all work closely with our distinguished and diverse Advisory Board to ensure a high-quality of information and services. We very much welcome our readers'' participation in all aspects of the web site. Sponsors: The Alzheimer Research Forum is an independent nonprofit organization. It is supported by grants and individual donations.

Proper citation: Alzforum Antibody Directory for Neuroscience Research (RRID:SCR_013601) Copy   

•   Source: SciCrunch Registry

http://web.mit.edu/glycomics/gt/gtdb.shtml

A pathway-based graphical interface for navigating the glycoenzyme database. The goal of the project is to define the paradigms by which carbohydrate binding proteins function in cellular communication. These pages are divided into six categories: -Glycosphingolipid: Sub-categories are Isogloboseries, Globoseries, Neo-lactoseries, Lactoseries and Ganglioseries - N-linked: Sub-categories are High-mannose, Hybrid and Complex -Mucin -Terminal Core 1 -Other O-linked -Terminal All: Includes all potential terminal structures for each glycan category

Proper citation: Glycosylation Pathways Database (RRID:SCR_013486) Copy   

•   Source: SciCrunch Registry

http://xin.cz3.nus.edu.sg/group/trmp/trmp.asp

The Therapeutically Relevant Multiple Pathways Database is designed to provide information about such multiple pathways and related therapeutic targets described in the literatures, the targeted disease conditions, and the corresponding drugs/ligands directed at each of these targets. This database currently contains 11 entries of multiple pathways, 97 entries of individual pathways, 120 targets covering 72 disease conditions along with 120 sets of drugs directed at each of these targets. Each entry can be retrieved through multiple methods including multiple pathway name, individual pathway name and disease name. Additional information provided include protein name, synonyms, Swissprot AC number, species, gene name and location, protein sequence (AASEQ) and gene sequence (NTSEQ) as well as potential therapeutic implications while applicable. Cross-links to other databases are provided which include Genecard, GDB, Locuslink, NCBI, KEGG, OMIM, SwissProt to facilitate the access of more detailed information about various aspects of the particular target or non-target protein. Queries can be submitted by entering or selecting the required information in any one or combination of the fields in the form. User can specify full name or any part of the name in a text field, or choose one item from an selection field. Sponsors: TRMP is supported by the National University of Singapore.

Proper citation: Therapeutically Relevant Multiple Pathways Database (RRID:SCR_013471) Copy   

•   Source: SciCrunch Registry

http://research.bioinformatics.udel.edu/iptmnet/

A protein database which connects multiple disparate bioinformatics tools and systems text mining, data mining, analysis and visualization tools, and databases and ontologies.

Proper citation: iPTMnet (RRID:SCR_014416) Copy   

•   Source: SciCrunch Registry

https://pharos.nih.gov/idg/index#

Database of ligands and diseases. Its goal is to develop a knowledge-base for the Druggable Genome (DG) in order to illuminate the uncharacterized and/or poorly annotated portion of the genome. DG, focusing on four of the most commonly drug-targeted protein families: G-protein-coupled receptors (GPCRs); nuclear receptors (NRs); ion channels (ICs); and kinases.

Proper citation: PHAROS (RRID:SCR_016258) Copy   

•   Source: SciCrunch Registry

https://www.moffitt.org/research-science/shared-resources/proteomics-and-metabolomics/

Provides instrumentation for proteomics and metabolomics studies, including protein, peptide and metabolite separations, MS instrumentation for protein, peptide and metabolite analysis, and data systems, software, and bioinformatics tools for data archiving and analysis. Proteomics Core performs routine analytical proteomics services, including target discovery, identification and quantitation, and also provides platforms for functional proteomics using variety of strategies for protein separation, sub-proteome enrichment, post-translational modification analysis, and quantitation.

Proper citation: Moffitt Cancer Center Proteomics and Metabolomics Core Facility (RRID:SCR_012168) Copy   

•   Source: SciCrunch Registry

https://www.mcgill.ca/cian/

Core facility at Biology Department in McGill Faculty of Science. Expertise in Light Microscopy and Image Analysis. Provides light microscopes, ranging from Point Scanning and Spinning Disc Confocals to Multi-Photon, TIRF, Light Sheet and Super-Resolution microscopes. Provides services in Automation/High throughput screening (liquid handler, pinning robot), Protein expression and antibody production. Users get training.

Proper citation: McGill Cell Imaging and Analysis Network Core Facility (RRID:SCR_012623) Copy   

•   Source: SciCrunch Registry

http://blanco.biomol.uci.edu/membrane_proteins_xtal.html

Table providing information about integral membrane proteins whose crystallographic, or sometimes NMR, structures have been determined to a resolution sufficient to identify TM helices of helix-bundle membrane proteins (typically 4 - 4.5 angstroms). It is based upon Preusch et al. (1998) as revised by White & Wimley (1999). Reference is made to all of the protein types whose structures have been determined. They have attempted to make the database as inclusive as possible.

Proper citation: Mpstruct (RRID:SCR_013284) Copy   

•   Source: SciCrunch Registry

http://www.glycosciences.de/glycocd/

Manually curated, comprehensive repository of clusters of differentiation (CDs) which are a) defined as distinct oligosaccharide sequences as part of either glycoproteins and/or glycosphingolipids and b) defined as proteins which have carbohydrate recognition sites (CRDs) or as carbohydrate binding lectins. The data base is generated by exhaustive search of literature and other online data banks related to carbohydrates and proteins. This data bank is the beginning of an effort to provide concise, relevant information of carbohydrate-related CDs in a user- friendly manner. For users convenience the data bank under menu browse of GlycoCD is arranged in two section namely carbohydrate recognition CDs (CRD CD) and glycan CD. The carbohydrate recognition CD part is the collection of proteins which recognize glycan structures by means of the CRDs. Glycan CD is the part in which CDs are summarized which characterize specific oligosaccharide structures. The GlycoCD databank has been developed with the aim to assist the immunologist, cell biologist as well as the clinician who wants to keep up with the present knowledge in this field of glycobiology.

Proper citation: Glyco-CD (RRID:SCR_001574) Copy   

•   Source: SciCrunch Registry

https://www.tamuk.edu/agriculture/institutes-and-other-units/nntrc/Products-Services.html

Center to provide global research, training, and resources that will lead to the discovery of medically important toxins found in venoms. The Viper Resource Center (VRC) is located in the Natural Toxins Research Center at Texas A&M University-Kingsville.

Proper citation: National Natural Toxins Research Center (RRID:SCR_002824) Copy   

•   Source: SciCrunch Registry

http://www.uniprot.org/program/Chordata

Data set of manually annotated chordata-specific proteins as well as those that are widely conserved. The program keeps existing human entries up-to-date and broadens the manual annotation to other vertebrate species, especially model organisms, including great apes, cow, mouse, rat, chicken, zebrafish, as well as Xenopus laevis and Xenopus tropicalis. A draft of the complete human proteome is available in UniProtKB/Swiss-Prot and one of the current priorities of the Chordata protein annotation program is to improve the quality of human sequences provided. To this aim, they are updating sequences which show discrepancies with those predicted from the genome sequence. Dubious isoforms, sequences based on experimental artifacts and protein products derived from erroneous gene model predictions are also revisited. This work is in part done in collaboration with the Hinxton Sequence Forum (HSF), which allows active exchange between UniProt, HAVANA, Ensembl and HGNC groups, as well as with RefSeq database. UniProt is a member of the Consensus CDS project and thye are in the process of reviewing their records to support convergence towards a standard set of protein annotation. They also continuously update human entries with functional annotation, including novel structural, post-translational modification, interaction and enzymatic activity data. In order to identify candidates for re-annotation, they use, among others, information extraction tools such as the STRING database. In addition, they regularly add new sequence variants and maintain disease information. Indeed, this annotation program includes the Variation Annotation Program, the goal of which is to annotate all known human genetic diseases and disease-linked protein variants, as well as neutral polymorphisms.

Proper citation: UniProt Chordata protein annotation program (RRID:SCR_007071) Copy   

•   Source: SciCrunch Registry

http://www.jhugicc.org/GIConteCenter/pages/cores/proteomicsCore.html

Core facility that uses mass spectrometry coupled to one (1D) and two (2D) dimensional separations by column chromatography or gel electrophoresis to identify, quantify or characterize proteins and their post-translational modifications, that are expressed in well characterized protein fractions from the small intestine, colon, kidney, liver and pancreas. Techniques such as difference gel electrophoresis (DIGE), isobaric tag for relative and absolute quantitation (iTRAQ), tandem mass tags (TMT) and stable isotope labeling of amino acids in cell culture (SILAC) as well as non-labeling methods (MudPIT, multi-dimensional protein identification technology) are available for quantifying relative differences in protein expression and post-translational modifications, such as acetylation, glycosylation, phosphorylation, nitrosation, ubiquitination and novel cleavage sites.

Proper citation: Hopkins Conte Digestive Diseases Basic and Translational Research Core Center Proteomics Core (RRID:SCR_015597) Copy   

•   Source: SciCrunch Registry

https://www.cimr.cam.ac.uk/about/facilities/bioinformatics

Core provides biological data handling and analysis in differential expression analysis, next generation sequencing, networks, protein architecture, and motif searching for in house researchers.

Proper citation: Cambridge Institute for Medical Research Bioinformatics Core Facility (RRID:SCR_017186) Copy   

•   Source: SciCrunch Registry

http://www.uvm.edu/sbb/cxx/cxx.html

Core for high resolution structural biology at the University of Vermont. X-ray crystallography allows biological and biomedical researchers to visualize proteins, RNA, DNA and their complexes at atomic resolution. The molecular details of specimens as small as DNA binding domains and as large as the ribosome have been elucidated via this powerful method. The CXX provides resources for all stages of macromolecular structure determination.

Proper citation: Vermont University Center for X-Ray Crystallography Core Facility (RRID:SCR_017688) Copy   

•   Source: SciCrunch Registry

http://biophysics.fsu.edu/facilities/protein-expression-facility/

Core to facilitate the large scale expression of recombinant proteins in bacterial, insects, and mammalian cells. Serves primarily faculty and students from the laboratories in the Kasha Laboratory Building and laboratories in Biology, Biochemistry, Chemistry and Nutrition at Florida State University, Tallahassee, FL.

Proper citation: Florida State University Protein Expression Core Facility (RRID:SCR_016757) Copy   

•   Source: SciCrunch Registry

https://www.rockefeller.edu/sbrc/

Core for protein expression and purification as well as all equipment needed for determination of three dimensional structures of biological macromolecules via X-ray crystallography. Houses Rigaku/MSC microMax 007HF generator for X-ray diffraction data collection, equipped with Varimax optics, X-stream 2000 cryosystems and two RaxisIV++ detectors.Also available is stereomicroscope, Nikon SMZ18, for crystal tray observations and crystal mounting., THIS RESOURCE IS NO LONGER IN SERVICE. Documented on September 16,2025.

Proper citation: Rockefeller University Structural Biology Resource Center Core Facility (RRID:SCR_017732) Copy   

•   Source: SciCrunch Registry