BioMediTech Research Infrastructure

Protein Services

The facility offers protein expression, purification and characterization. Proteins are expressed in bacterial, insect and mammalian cells, which supply the expression and modification requirements for a comprehensive variety of proteins for wide variety of biological assays.


Protein Service (PS) offers recombinant protein expression, protein purification and biophysical characterization for drug discovery and life science research. The proteins may be used in structural biology, protein-ligand and protein-protein interaction studies, and in development of diagnostics.

The facility offers hands-on counselling concerning protein expression methods and expression vectors, but customer is typically responsible for the preparation of the expression vector. Synthetic genes of interest can be directly ordered by the service on the behalf of the customer. Typical workflow includes pilot scale protein production and purification, scale-up to liter scale, protein isolation and purification and finally, protein characterization by various biochemical and biophysical methods including interaction assays.

Note: Protein Service is capable only work with Biosafety level 1 products.

Order Form

Protein Service Order Form including:

  • Research Agreement – Business Operations (University of Tampere)
  • General terms and conditions – Business Operations (University of Tampere)

Protein Expression Service

Three expression systems (bacteria, insect and mammalian cells) are currently available and they offer potential for large variety of different types of proteins. Potential customer is asked to contact the coordinator of the facility for further information in case the selection of the suitable expression system is not straightforward.

Customer provides expression vector and the expression will be first confirmed utilizing bottle or plate cultures (makes it also possible to optimize growth media). After positive results the production may be performed by using bottles in shakers or with small scale fermentor.

The bioreactor laboratory service offers protein production in bacterial host in 4.5 l batches using Labfors Infors 3 fermentor. The accurately controlled growth conditions enable higher cell densities and better product quality than by using conventional bottle cultures.

PS sends the final products to the customer and reports SDS-PAGE and Western Blot results (customer is asked to provide antibodies for WB if not usual antibody is available).

Customer provides the desired insert in plasmid donor vector and is asked to confirm the clone by DNA sequencing. If necessary, DNA sequencing can be done also in the University of Tampere.

Note! PS kindly asks to measure and label the concentration of the plasmid provided (min 5 ng, V=25 µl).

The donor plasmid is used to prepare three to six bacmids, which are confirmed by PCR and then three of them are transfected to the Sf9 insect cells (optionally HighFiveTM cells). Volume of secondary virus (P2) is typically 50 ml and expression of protein is confirmed by Western Blot from cell pellet and medium (antibodies against possible purification tag or provided by customer). Virus is stock up for one month and can be used to optimize the expression or for possible production scale-up up to 4.5 L in aliquots of 500 ml. Moreover, protein purification with His-tag or Strept-tag is also possible.

Customer provides the desired cDNA in suitable plasmid vector and is asked to confirm the clone by sequencing. If necessary, DNA sequencing can be done also in the University of Tampere.

Expression vector is transfected to the mammalian cells (CHO-S or HEK 293F) prior to four weeks long cell line selection. SDS-PAGE and Western blot is done from pilot scale expression to confirm protein expression. Cell lines are stored for four months so they can be used to the further expression. Decision of scale-up is asked to give in a month. In scale up, cells are first adapted to the suspension growth, and protein expression is confirmed with SDS-PAGE and Western blot from 50 ml patch. This step takes about two weeks, and then scale up to the 5 L is possible.

Protein Isolation, Purification, and Characterization

Host cells are collected by centrifugation and lysed by using either a high-power sonicator or high-pressure homogenizator Emulsiflex. Protein isolation and purification is typically done by chromatographic methods. The protein quality can be evaluated by several methods, including analytical gel filtration, SDS-PAGE, 2-D electrophoresis, dynamic light scattering, calorimetric methods and biosensors. Proteins can be delivered either in solution or as freeze-dried.

Equipment tab provides a brief summary of the methods and instrumentation available.


All the users of the Protein Services (PS) facility are obligated to acknowledge the facility in publications:

“The authors acknowledge the Tampere facility of Protein Services (PS) for their service.”


Chromatography systems. The facility has three complete ÄKTA chromatography systems installed for preparative chromatography work and they all include UV/VIS and conductivity detectors and are equipped with fraction collectors. One of the instruments is equipped with sample pump and pH electrode. We have also Shimadzu/Malver instrument especially suitable for analytical chromatography. This instrument has gradient pump, autosampler and fraction collector, and it is equipped with UV/VIS, fluorescence, DLS and SLS detectors.

Dynamic light scattering (DLS) allows study of particle size from hydrodynamic diameter of 1 nm (size of sucrose molecule) and particle size distribution (homogeneity) in soluble samples. In addition, it is possible to measure Zeta potential which is a measure of the magnitude of the repulsion or attraction between particles. The significance of zeta potential is that it can be related to the stability of particle dispersions and allows one to find suitable conditions for samples (proteins, virus particles, nanoparticles etc). DLS is thus efficient method both in protein characterization and in protein formulation.

Differential scanning calorimetry (DSC) is primarily used to characterize stability and folding of macromolecules such as proteins. In addition, it can be used to screen protein-ligand interactions, because when a ligand preferentially binds to the native form of a protein, the protein is stabilized and the thermal transition midpoint (Tm) of the protein-ligand complex is higher than that of the protein in the absence of ligand. Therefore, DSC can be used for ligands with ultra-tight binding constants (1020 M-1) that cannot be measured by other methods, as well as a high throughput screening assay for drug discovery (up to 50 samples per day). The DSC instrument is equipped with refrigerated autosampler, enabling large sample sets.

Isothermal titration calorimetry (ITC) is a thermodynamic technique that directly measures the heat released or absorbed during a biomolecular binding event. Measurement of this heat allows accurate determination of binding constants (KB), reaction stoichiometry (n), enthalpy (ΔH) and entropy (ΔS), thereby providing a complete thermodynamic profile of the molecular interaction in a single experiment. With ITC, it is possible to directly measure sub-millimolar to nanomolar binding constants (10-2 to 10-9 M) and nanomolar to picomolar binding constants (10-9 to 10-12 M) by using the competitive binding technique. Moreover, ITC is true in-solution technique and therefore no labeling or immobilization is required.

Biolayer interferometry (BLI) is technique, which is used to measure real-time, label-free analysis of biomolecular interactions and to provide information on affinity, kinetics and concentration. BLI technology monitors the binding of proteins and other biomolecules to their partners in real time. The binding interaction is continuously monitored by measuring the change in thickness of the protein layer on the biosensor tip. The method has no need to label the protein with fluorescent or chromogenic tags, thus eliminating interference issues. In addition, instrument uses 96 or 384 plates and 16 parallel sensors enabling high throughput assays.

Surface plasmon resonance (SPR) use an optical method to measure the refractive index near a sensor surface in order to detect an interaction of one molecule that is immobilised onto the sensor’s surface. Method is used e.g. to search for binding partners or most commonly to measure kinetics of an interaction, i.e. the rates of complex formation (ka) and dissociation (kd). The previous parameters can be determined from the information in a sensorgram.


E. coli expression and characterization
Transformation per plasmid 20 €
Production of a pre-culture from a tested clone 20 €
5 L Bacterial expression culture from pre-culture* 300 €
Affinity Chromatography** 150 €
Concentration and buffer change of protein sample 25 €
SDS-PAGE with Coomassie staining 50 €
SDS-PAGE with Oriole staining 70 €
SDS-PAGE with Silver staining 80 €
Immunoblotting*** 100 €
ITC analysis per sample 50 €
ITC equipment usage per day**** 100 €
DSC analysis per sample (Minimum charge 3 samples) 20 €
DLS analysis per sample 20 €
SPR analysis per run*** 50 €
Freeze drying per sample 10 €
Octet BLI measurement (sensors do not include) 25 €
Bacmid production (20 € x 6) 120 €
Transfection Sf9 (HighFive 60 €) 50 €
Optimization of the production by post infection follow up 60 €
Pilot purification assay 40 €
Scale up 1st 500 ml 125 €
Scale up 2nd and following 500 mls 75 €
Mammalian cell expression system
Transfection and selection 150 €
Cell adaptation 100 €
Scale up 1 L 200 €
Concentration 350 €

Protein Service reserves the right to price adjustments.

* Includes basic reagents and cell collection
** Affinity matrix will be charged separately
*** Customer provides / pays for the antibody or SPR sensors
**** User must attain tutoring for usage before starting experiments


Head of the facility:
Vesa Hytönen, Ph.D., Associate Professor
Tel: +358 40 190 1517
Room: ARVO F331

Juha Määttä, Ph.D.
Tel: +358 50 318 5814
Room: ARVO F303

Street address:
Arvo Ylpön katu 34
33520 Tampere

Reference Publications

Auer S, Azizi L, Faschinger F, Blazevic V, Vesikari T, Gruber HJ, Hytönen VP
Stable immobilisation of His-tagged proteins on BLI biosensor surface using cobalt
Sensors and Actuators B: Chemical. 2017 May 243:104-113

Agrawal N, Määttä JAE, Kulomaa MS, Hytönen VP, Johnson MS, Airenne TT
Structural characterization of core-bradavidin in complex with biotin
PLoS One. 2017 Apr 20;12(4):e0176086

Kalliokoski S, Piqueras VO, Frías R, Sulic AM, Määttä JA, Kähkönen N, Viiri K, Huhtala H, Pasternack A, Laurila K, Sblattero D, Korponay-Szabó IR, Mäki M, Caja S, Kaukinen K, Lindfors K
Transglutaminase 2-specific coeliac disease autoantibodies induce morphological changes and signs of inflammation in the small-bowel mucosa of mice
Amino Acids. 2017 Mar;49(3):529-540

Lehtonen SI, Tullila A, Agrawal N, Kukkurainen S, Kähkönen N, Koskinen M, Nevanen TK, Johnson MS, Airenne TT, Kulomaa MS, Riihimäki TA, Hytönen VP
Artificial Avidin-Based Receptors for a Panel of Small Molecules
ACS Chem Biol. 2016 11(1):211-21

Pawlowski A, Moilanen AM, Rissanen IA, Määttä JA, Hytönen VP, Ihalainen JA, Bamford JK
The Minor Capsid Protein VP11 of Thermophilic Bacteriophage P23-77 Facilitates Virus Assembly by Using Lipid-Protein Interactions
J Virol. 2015 Aug;89(15):7593-603


The modern infrastructure for macromolecular X-ray crystallography and protein characterization is available for European researchers through Instruct, an EU-ESFRI program. Instruct aims at fostering the development of structural biology in Europe. It is coordinated by the Instruct office in Oxford, UK.

Instruct logo

Biocenter Finland Structural Biology network formed the framework for an Instruct National Affiliate Center (NAC) established in 2014. The Finnish Instruct-NAC has nodes at the Universities of Helsinki, Oulu, Tampere, Turku, Eastern Finland, and at the Åbo Academi University.

Participation in Instruct through the Instruct-NAC provides access to other European centers of the Instruct network for the researchers in Tampere and it makes the infrastructure and expertise at the BioMediTech institute available for European researchers. Instruct also supports organization of international courses in Tampere.

Structural biology in Tampere

Protein Service in Tampere offers variety of possibilities to express recombinant proteins for structural biology groups. Tampere has a strong background in manufacturing proteins for structural biology as well as many other purposes for example VLPs and antigens. In addition, we provide characterization and interaction analysis for the proteins with experimental methods such as ITC, DSC, DLS and OctetRed.

Equipment available in Tampere: see the Equipment tab.

Contact person

Juha Määttä, juha.maatta(at)

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