Core Facilities

The Protein Purification Facility

Tel: 02-6586920
 
The Protein Purification Facility provides support and assistance to researchers and students in the university, as well as to biotechnology and pharmaceutical companies.
We can provide the basis for project initiation and technical training, or perform the work ourselves as a collaboration or a service agreement. Using our facility can reduce the timeframe and cost of such projects.
The facility also serves as a training center through our workshops and courses.
 
We are highly experienced in developing protein purification strategies for both small and large scales, for all types of natural or recombinant proteins, and from different sources.
We are adept at overcoming problems of protein aggregation and low yield, and proficient in technical aspects such as protein refolding, and solubility.
 
Detailed information about the technologies and available support can be found in our website

 

דוא"ל טלפון פקס משרד
Dr. Hadar Amartely Dr. Hadar Amartely
Head of core facility 		02-65-86920 Silberman 3-228
Prof. Oded Livnah Prof. Oded Livnah
Academic director 		02-65-85191 Wolfson -10

The facility is equipped with five fully automated liquid chromatography systems (AKTA systems) designed for method development and research applications, for large and small scale production and for analytical tests of protein purity as well.
Aמ additional AKTA system ןד combined to a multi angle light scattering (MALS) and a refractometer systems, for mass and shape characterization, protein purity and post translation modification assessment.
In addition, we have gel electrophoresis and blotting equipment, a microfluidizer for cell disruption, ultrafiltration systems (such as AMICON and TFF), and a wide repertoire of columns and resins for protein purification according to size, charge, hydrophobicity, or specific affinity.
The facility is also equipped with Isothermal titration calorimeter (ITC) utilized for quantitative analysis of protein interactions (as well as of other biomolecular interactions including DNA and peptides), which provides calculation of the binding thermodynamic parameters, such as binding affinity (kd), binding energy and stoichiometry.