John M. Tomich - Ph.D. - Director
Ben Katz - BSE - Associate Director

Burt Hall, Rooms 201, 207, 211, 216
Telephone (785) 532-5956
Fax (785) 532-6297
E-mail: jtomich@ksu.edu

The Biotechnology Core Facility at Kansas State University was established in 1993 to provide a number of centralized services to plant and animal researchers at K-State and elsewhere. The goods and services provided by the facility give researchers the tools they need to identify new proteins, protein modifications, protein-protein interactions and enzyme substrates. The lab is located in space provided by the Department of Biochemistry and the facility is supported in part by fees for service and the K-State College of Arts and Sciences, The Vice President for Research and the Provost (Targeted Excellence Award). The laboratory functions in three distinct ways: synthesis, separations and bioanalysis. The lab synthesizes peptides, peptide libraries, chromophores, fluorophores and other organic molecules. It also serves as a broker for ordering oligonucleotides. Separations are performed using various chromatographic techniques and by mass spectrometry. Bioanalysis is performed to assess purity, size, composition and sequences of peptides, proteins and carbohydrates.

Our services include:
DNA/RNA Oligonucleotide Synthesis
Peptide/Protein Synthesis
Peptide/Protein Sequencing
Mass Spectrometry
Surface Plasmon Resonance

The Biotechnology component is equipped with more than $3 million worth of automated scientific instruments that enhance the biotechnology capabilities of the university. One piece of equipment, the Biacore, gives the core facility a new dimension, the quantification of molecular interactions. This instrument uses a treated gold slide that allows the covalent attachment and display of molecules, such as proteins or lipids, in a flow cell. Potential binding partners can be introduced in solution and subsequent binding to the bound molecule can be measured. Using this technique, accurate association constants can be determined. 

The Proteomics Component - The K-State Core lab has expanded the Proteomics Facility with funding from the National Science Foundation (MRI grant # 0521587) and the Kansas State University Targeting Excellence Program, Functional Genomics Consortium. The goal of the Functional Genomics Consortium is to facilitate utilization of functional genomics strategies aimed at both small and large biological problems, and, in particular, to enhance the ability of K-State scientists to analyze gene function at the protein and metabolite levels. To this end, a research associate at the Proteomics Core Facility is available to interact extensively with users, providing support and education. Means for users to acquire preliminary data without fees are also provided. We provide analysis of both purified proteins and isolated peptide fragments with our mass spectrometers. We have the ability to purify protein and peptides by both standard 2D-PAGE and 2D-nanoflow HPLC.

Specific capabilities include:
Mass Spectrometry
Protein/Peptide Isolation
2D LC (Ion exchange/RP)
Protein Fragmentation (chemical or enzymatic)
Protein/Peptide Sequencing
Consultations for designing of proteomic research

Instruments: Bruker Daltonics Ultraflex III MALDI TOF/TOF Mass Spectrometer, Finnigan Lasermat 2000 MALDI TOF Mass Spectrometer, Bruker Daltonics HCT Ultra ESI-Ion Trap Mass Spectrometer, Bruker Esquire 3000 plus ESI-Ion Trap Mass Spectrometer, 2D Capillary/Nano LC System (2), Bruker Daltonics Proteineer Digest and Prep Workstation (2), Bruker Daltonics Proteineer Automated Spot Picker (2), Beckman Gold HPLC system, Bio-Rad Protean 2D Gel Electropheresis System, Invitrogen 2D Gel Electropheresis System & IEF Zoom Fractionator, Biacore 3000 Surface Plasmon Resonance, GE Typhoon 9410 Phosphoimager, Applied Biosystem 492 Protein Sequencer, Cary Eclipse Spectrfluorimeter with microplate holder Software: Mascot and Phenyx / Aldente - Mass data base search engines, Melanie - 2D Gel analysis, Protein Scape - Sample handling and data analysis

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This page last updated: March 2016