For over 35 years, Fermentas led the industry world-wide in the discovery, manufacturing and marketing of quality molecular biology products. In July of 2010, Fermentas became a wholly-owned subsidiary of Thermo Fisher Scientific. In September of 2012, the new Molecular Biology Center of Excellence was opened in Vilnius. The new facilities provide molecular, protein and cellular biology products to better serve growing demand from life sciences customers globally. The 156,000-square-foot Molecular Biology Center of Excellence is currently home to more than 400 research, laboratory and manufacturing personnel, with room for expansion.
In 1975, the All-Union Research Institute of Applied Enzymology was established in Vilnius, Lithuania and in the years that followed delivered many “first” accomplishments. In 1978, the BcnI restriction enzyme was the first commercially manufactured restriction enzyme. The following year, scientists from Fermentas discovered their first restriction enzyme (CfrI). In 1985, the Eco47ll restriction enzyme was the first cloned by the Fermentas team. In 2006, Fermentas introduced FastDigest restriction enzymes – the new standard for DNA digestion. In 2011, the world's first genetically-engineered restriction enzyme (Eco57MI) and the world's first genetically-engineered DNA nicking enzyme (N.Bpu101) were created. During the 35-year history, Fermentas scientists have been responsible for the discovery of approximately 30% of all known restriction enzymes.
In 1996, Fermentas became one of the first manufacturers of molecular biology products to implement an ISO 9002 quality management system. The same year, PureExtreme® was introduced, representing the highest product quality and performance standards, and as of 2006, all products of enterprise carry this standard. In 2003, the Fermentas environmental protection management system was certified under ISO 14001. Since 2007, all Fermentas products are manufactured in class D clean room facilities, qualified and certified as per EU directives and ISPE guidelines, which are prerequisites for GMP manufacturing. In 2010, Fermentas implemented a quality management system in compliance with ISO 13485 for research, development and manufacturing of diagnostic medical devices.
- Purification of native and recombinant proteins
- Plasmid DNA preparation (pharmaceutical grade meeting FDA and EU guidelines, transfection grade & research grade)
- RNA production and purification
- Process development
- Protein, DNA and RNA ladders
- in vitro protein evolution (reverse transcriptases and DNA polymerases)
- Pilot-scale fermentation & production of biomass
- Processing of nucleic acids by enzymes
Petrusyte M, Janulaitis A.
Isolation and some properties of the restriction endonuclease BcnI from Bacillus centrosporus.
Eur J Biochem. 1982 Jan;121(2):377-81.
Janulaitis AA, Petrusyte MA, Jaskelavicene BP, Krayev AS, Skryabin KG, Bayev AA.
A new restriction endonuclease BcnI from Bacillus centrosporus RFL 1.
FEBS Lett. 1982 Jan 25;137(2):178-80.
Janulaitis AA, Stakenas PS, Lebedenko EN, Berlin YuA.
A new restriction endonuclease from Citrobacter freundii.
Nucleic Acids Res. 1982 Oct 25;10(20):6521-30.
Janulaitis A, Klimasauskas S, Petrusyte M, Butkus V.
Cytosine modification in DNA by BcnI methylase yields N4-methylcytosine.
FEBS Lett. 1983 Sep 5;161(1):131-4.
Janulaitis A, Kazlauskiene R, Lazareviciute L, Gilvonauskaite R, Steponaviciene D, Jagelavicius M, Petrusyte M, Bitinaite J, Vezeviciute Z, Kiuduliene E.
Taxonomic specificity of restriction-modification enzymes.
Gene. 1988 Dec 25;74(1):229-32.
Kulakauskas S, Lubys A, Ehrlich SD.
DNA restriction-modification systems mediate plasmid maintenance.
J Bacteriol. 1995, 177:3451-4.
Stankevicius K, Povilionis P, Lubys A, Menkevicius S, Janulaitis A.
Cloning and characterization of the unusual restriction-modification system comprising two restriction endonucleases and one methyltransferase.
Gene. 1995, 19;157:49-53.
Siksnys V, Timinskas A, Klimasauskas S, Butkus V, Janulaitis A.
Sequence similarity among type-II restriction endonucleases, related by their recognized 6-bp target and tetranucleotide-overhang cleavage.
Gene. 1995, 19;157:311-4.
Lubys A, Janulaitis A.
Cloning and analysis of the plasmid-borne genes encoding the Bsp6I restriction and modification enzymes.
Gene. 1995, 19;157:25-9.
Lubys A, Lubienè J, Kulakauskas S, Stankevicius K, Timinskas A, Janulaitis A.
Cloning and analysis of the genes encoding the type IIS restriction-modification system HphI from Haemophilus parahaemolyticus.
Nucleic Acids Res. 1996, 15;24:2760-6.
Vitkute J, Maneliene Z, Petrusyte M, Janulaitis A.
BplI, a new BcgI-like restriction endonuclease, which recognizes a symmetric sequence.
Nucleic Acids Res. 1997, 15;25:4444-6.
Lagunavicius A, Grazulis S, Balciunaite E, Vainius D, Siksnys V.
DNA binding specificity of MunI restriction endonuclease is controlled by pH and calcium ions: involvement of active site carboxylate residues.
Biochemistry. 1997, 16;36:11093-9.
Lagunavicius A, Siksnys V.
Site-directed mutagenesis of putative active site residues of MunI restriction endonuclease: replacement of catalytically essential carboxylate residues triggers DNA binding specificity.
Biochemistry. 1997, 16;36:11086-92.
Skirgaila R, Grazulis S, Bozic D, Huber R, Siksnys V.
Structure-based redesign of the catalytic/metal binding site of Cfr10I restriction endonuclease reveals importance of spatial rather than sequence conservation of active centre residues.
J Mol Biol. 1998, 5;279:473-81.
Skirgaila R, Siksnys V.
Ca2+-ions stimulate DNA binding specificity of Cfr10I restriction enzyme.
Biol Chem. 1998, 379(4-5):595-8.
Vitkute J, Maneliene Z, Janulaitis A.
AbeI, a restriction endonuclease from Azotobacter beijerinckii, which recognizes the asymmetric heptanucleotide sequence 5'-CCTCAGC-3'(-5/-2).
Nucleic Acids Res. 1998, 1;26:4917-8.
Vitkute J, Maneliene Z, Petrusyte M, Janulaitis A.
BfiI, a restriction endonuclease from Bacillus firmus S8120, which recognizes the novel non-palindromic sequence 5'-ACTGGG(N)5/4-3'.
Nucleic Acids Res. 1998, 15;26:3348-9.
Lubys A, Jurenaite S, Janulaitis A.
Structural organization and regulation of the plasmid-borne type II restriction-modification system Kpn2I from Klebsiella pneumoniae RFL2.
Nucleic Acids Res. 1999, 1;27:4228-34.
Steponaviciene D, Maneliene Z, Petrusyte M, Janulaitis A.
BseSI, a restriction endonuclease from Bacillus stearothermophilus Jo 10-553, which recognizes the novel hexanucleotide sequence 5'-G(G/T)GC(A/C)C-3'.
Nucleic Acids Res. 1999, 1; 27:2644-5.
Siksnys V, Skirgaila R, Sasnauskas G, Urbanke C, Cherny D, Grazulis S, Huber R.
The Cfr10I restriction enzyme is functional as a tetramer.
J Mol Biol. 1999, 3;291:1105-18.
Sapranauskas R, Sasnauskas G, Lagunavicius A, Vilkaitis G, Lubys A, Siksnys V.
Novel subtype of type IIs restriction enzymes. BfiI endonuclease exhibits similarities to the EDTA-resistant nuclease Nuc of Salmonella typhimurium.
J Biol Chem. 2000, 6;275:30878-85.
Kesminiene A, Maneliene Z, Vitkute J, Petrusyte M, Janulaitis A.
A unique type II restriction endonuclease FspAI, that recognizes the octanucleotide sequence 5'-RTGC/GCAY-3'.
Nucleic Acids Res. 2001, 15;29:E120.
Vitkute J, Maneliene Z, Janulaitis A.
Two new thermostable type II restriction endonucleases from Thermus aquaticus: TatI and TauI, which recognize the novel nucleotide sequences 5'-W (downward arrow)GTACW-3' and 5'-GCSG (downward arrow)C-3' respectively.
FEMS Microbiol Lett. 2001, 13;204:253-7.
Cesnaviciene E, Petrusyte M, Kazlauskiene R, Maneliene Z, Timinskas A, Lubys A, Janulaitis A.
Characterization of AloI, a restriction-modification system of a new type.
J Mol Biol. 2001, 23;314:205-16.
Padegimiene E, Maneliene Z, Petrusyte M, Janulaitis A.
OliI, a unique restriction endonuclease that recognizes the discontinuous sequence 5'-CACNN NGTG-3'.
Nucleic Acids Res. 2001, 15;29:E30.
Jurenaite-Urbanaviciene S, Kazlauskiene R, Urbelyte V, Maneliene Z, Petrusyte M, Lubys A, Janulaitis A.
Characterization of BseMII, a new type IV restriction-modification system, which recognizes the pentanucleotide sequence 5'-CTCAG(N)(10/8)/.
Nucleic Acids Res. 2001,15;29:895-903.
Vitkute J, Stankevicius K, Tamulaitiene G, Maneliene Z, Timinskas A, Berg DE, Janulaitis A.
Specificities of eleven different DNA methyltransferases of Helicobacter pylori strain 26695.
J Bacteriol. 2001, 183:443-50.
Rimseliene R, Janulaitis A.
Mutational analysis of two putative catalytic motifs of the type IV restriction endonuclease Eco57I.
J Biol Chem. 2001, 30;276:10492-7.
Grigaite R, Maneliene Z, Janulaitis A.
AarI, a restriction endonuclease from Arthrobacter aurescens SS2-322, which recognizes the novel non-palindromic sequence 5'-CACCTGC(N)4/8-3'.
Nucleic Acids Res. 2002, 1;30:e123.
Gaigalas M, Maneliene Z, Kazlauskiene R, Petrusyte M, Janulaitis A.
PfoI, a unique type II restriction endonuclease that recognises the sequence 5'-T downward arrow CCNGGA-3'.
Nucleic Acids Res. 2002, 1;30:e98.
Bitinaite J, Mitkaite G, Dauksaite V, Jakubauskas A, Timinskas A, Vaisvila R, Lubys A, Janulaitis A.
Evolutionary relationship of Alw26I, Eco31I and Esp3I, restriction endonucleases that recognise overlapping sequences.
Mol Genet Genomics. 2002, 267:664-72.
Vilkaitis G, Lubys A, Merkiene E, Timinskas A, Janulaitis A, Klimasauskas S.
Circular permutation of DNA cytosine-N4 methyltransferases: in vivo coexistence in the BcnI system and in vitro probing by hybrid formation.
Nucleic Acids Res. 2002, 1;30:1547-57.
Roberts RJ, Belfort M, Bestor T, Bhagwat AS, Bickle TA, Bitinaite J, Blumenthal RM, Degtyarev SKh, Dryden DT, Dybvig K, Firman K, Gromova ES, Gumport RI, Halford SE, Hattman S, Heitman J, Hornby DP, Janulaitis A, Jeltsch A, Josephsen J, Kiss A, Klaenhammer TR, Kobayashi I, Kong H, Krüger DH, Lacks S, Marinus MG, Miyahara M, Morgan RD, Murray NE, Nagaraja V, Piekarowicz A, Pingoud A, Raleigh E, Rao DN, Reich N, Repin VE, Selker EU, Shaw PC, Stein DC, Stoddard BL, Szybalski W, Trautner TA, Van Etten JL, Vitor JM, Wilson GG, Xu SY.
A nomenclature for restriction enzymes, DNA methyltransferases, homing endonucleases and their genes.
Nucleic Acids Res. 2003, 1;31:1805-12.
Rimseliene R, Maneliene Z, Lubys A, Janulaitis A.
Engineering of restriction endonucleases: using methylation activity of the bifunctional endonuclease Eco57I to select the mutant with a novel sequence specificity.
J Mol Biol. 2003, 21;327:383-91.
Lagunavicius A, Sasnauskas G, Halford SE, Siksnys V.
The metal-independent type IIs restriction enzyme BfiI is a dimer that binds two DNA sites but has only one catalytic centre.
J Mol Biol. 2003, 28;326:1051-64.
Cesnaviciene E, Mitkaite G, Stankevicius K, Janulaitis A, Lubys A.
Esp1396I restriction-modification system: structural organization and mode of regulation.
Nucleic Acids Res. 2003, 15;31:743-9.
Földesi A, Keller A, Stura A, Zigmantas S, Kwiatkowski M, Knapp D, Engels JW.
The fluoride cleavable 2-(cyanoethoxy)methyl (CEM) group as reversible 3'-O-terminator for DNA sequencing-by-synthesis - synthesis, incorporation, and cleavage.
Nucleosides Nucleotides Nucleic Acids. 2007, 26:271-5.
Knapp, D.C., Keller, A., D'Onofrio, J., Lubys, A., Serva, S., Kurg, A., Remm, M., Kwiatkowski, M., Engels, J.W.
Synthesis of four colors fluorescently labelled 3'-O-blocked nucleotides with fluoride cleavable blocking group and linker for array based Sequencing-by-Synthesis applications.
Nucleic Acids Symp. Ser. (Oxf). 2008, v. 52, 345-346.
Lagunavicius A, Kiveryte Z., Zimbaite-Ruskuliene, V, Radzvilavicius T & Janulaitis A.
Duality of polynucleotide substrates for Phi29 DNA polymerase: 3’→5’ RNase activity of the enzyme.
RNA. 2008, 14:503-13.
Lagunavicius, A, Merkiene, E, Kiveryte, Z, Savaneviciute, A, Zimbaite-Ruskuliene, V, Radzvilavicius, T & Janulaitis, A.
Novel application of Phi29 DNA polymerase: RNA detection and analysis in vitro and in situ by target RNA-primed RCA.
RNA. 2009, 15:765-71.
Gaidamaviciute, E., Tauraite, D., Gagilas, J. & Lagunavicius, A.
Site-directed chemical modification of archaeal Thermococcus litoralis Sh1B DNA polymerase: Acquired ability to read through template-strand uracils.
Biochim. Biophys. Acta. 2010, 1804: 1385-1393.
Merkiene, E., Gaidamaviciute, E., Riauba, L., Janulaitis, A. & Lagunavicius, A.
Direct detection of RNA in vitro and in situ by target-primed RCA: The impact of E.coli RNase III on the detection efficiency of RNA sequences distanced far from the 3'-end.
RNA. 2010, 16: 1508-1515.
Zaliauskiene, L., Bernadisiute, U., Vareikis, A., Makuska, R., Volungeviciene, I., Petuskaite, A., Riauba, L., Lagunavicius, A. & Zigmantas, S.
Efficient gene transfection using novel cationic polymers poly(hydroxylalkylene imines).
Bioconjug. Chem. 2010, 21: 1602-1611.
Tubeleviciute A, Skirgaila R.
Compartmentalized self-replication (CSR) selection of Thermococcus litoralis Sh1B DNA polymerase for diminished uracil binding
Protein Eng Des Sel. 2010, 23(8):589-97.
Šiurkus J, Panula-Perälä J, Horn U, Kraft M, Rimšeliene R, Neubauer P.
Novel Approach of High Cell Density Recombinant Bioprocess Development: Optimization and Scale up from microlitre to pilot scales, with maintenance of fed-batch cultivation mode of E. coli Cultures.
Microb Cell Fact. 2010, 9:35.
Radzvilavicius, T. & Lagunavicius, A.
Selective inactivation of M-MuLV RT RNase H activity by site-directed PEGylation: an improved ability to synthesize long cDNA molecules.
N. Biotechnology 2012, 29(3):285-92.
Knapp DC, Serva S, D'Onofrio J, Keller A, Lubys A, Kurg A, Remm M, Engels JW.
Fluoride-cleavable, fluorescently labelled reversible terminators: synthesis and use in primer extension.
Chemistry. 2011, 17(10):2903-15.
Šiurkus J, Neubauer P. Reducing conditions are the key for efficient production of active ribonuclease inhibitor in Escherichia coli.
Microb Cell Fact. 2011 May 10;10:31.
Šiurkus J, Neubauer P.
Heterologous production of active ribonuclease inhibitor in Escherichia coli by redox state control and chaperonin coexpression.
Microb Cell Fact. 2011 Aug 8;10:65.
Ukanis M., Sapranauskas R., Lubys A.
Screening for catalytically active Type II restriction endonucleases using segregation-induced methylation deficiency.
Nucleic Acids Res. 2012 Oct 1; 40(19): e149.
Baranauskas A, Paliksa S, Alzbutas G, Vaitkevicius M, Lubiene J, Letukiene V, Burinskas S, Sasnauskas G, Skirgaila R.
Generation and characterization of new highly thermostable and processive M-MuLV reverse transcriptase variants.
Protein Eng Des Sel. 2012 Jun 12 2012 Oct;25(10):657-68.
DNA/RNA Modifying Enzymes: Extremely Pure Quality Guarantee
All Thermo Scientific DNA/RNA modifying enzymes and other proteins are produced under the ISO 9001:2000 quality management system and are subjected to extensive quality control. As a result of these stringent conditions of product analysis, the entire Thermo Scientific product line meets the industry's highest quality and performance. Our products are monitored for the accuracy of their activity units, the absence of contaminant activities (nucleases, phosphatases and proteases) and for their performance in specific functional tests. A warranty is assigned and an expiry date is listed both on the product label and in the Product Information insert supplied with each product. Product lots are monitored regularly to ensure that they continue to meet the quality control specifications right up to their expiry date.
The stringent quality control procedures at Thermo Scientific consistently guarantee the highest quality of DNA/RNA modifying enzymes and other proteins.
Activity unit definitions for Thermo Scientific DNA/RNA modifying enzymes are those commonly used in molecular biology. Activity unit definitions and descriptions of reaction conditions are provided in the catalog entry for each product. Reaction conditions may differ for specific research applications.
Labeled Oligonucleotide Test (LO)
The assay is performed in reaction buffer containing a particular enzyme or other protein of interest and 5'-[32P]-labeled synthetic oligonucleotides (single-stranded and double-stranded). After incubation under the appropriate conditions, see Table 1, reaction products are separated on a polyacrylamide gel and then analyzed by phosphoimaging. The product passes this quality control test if there is no degradation of both the single-stranded oligonucleotide and double-stranded oligonucleotide, see Fig. 1 below.
Figure 1. Labeled Oligonucleotide (LO) Test.
ss – single-stranded radiolabeled oligonucleotide
ds – double-stranded radiolabeled oligonucleotide
Pure enzyme – Thermo Scientific NotI restriction enzyme
Contaminated enzyme – competitor's NotI restriction enzyme
Double-stranded Endodeoxyribonuclease Assay (dsEndo)
The assay is performed in 50µl of reaction mixture containing reaction buffer, enzyme and 1µg of covalently closed circular (supercoiled) DNA (either pUC19 DNA or phiX174 RF1 DNA). After incubation under the appropriate conditions,see Table 1, the DNA is analyzed on a 1% agarose gel. The product passes this quality control test if neither nicked DNA nor linear DNA is detected.
Single-stranded Endodeoxyribonuclease Assay (ssEndo)
The assay is performed in 50µl of reaction mixture containing reaction buffer, enzyme and 1µg of covalently closed circular single-stranded DNA of M13mp19. After incubation under appropriate conditions, see Table 1, the DNA is analyzed on a 1% agarose gel. The product passes this quality control test if no decrease in the amount of closed circular DNA is observed.
Exodeoxyribonuclease Assay I (Exo I)
The assay is performed in 50µl of reaction mixture containing reaction buffer, enzyme and 1µg of sonicated [3H]-labeled DNA from E.coli. After incubation under the appropriate conditions, see Table 1, the DNA is precipitated with trichloroacetic acid and the radioactivity of the supernatant is determined. Exodeoxyribonuclease activity is expressed as the percent of total DNA radioactivity released into the acid soluble fraction. The product passes this quality control test if less than 0.5% of the DNA is degraded.
Exodeoxyribonuclease Assay II (Exo II)
The assay is performed in 50µl of reaction mixture containing reaction buffer, enzyme and 1µg of either the lambda DNA or plasmid DNA fragments. After incubation under appropriate conditions, see Table 1, the DNA is analyzed on an agarose gel. The product passes this quality control test if DNA fragments are not degraded.
Ribonuclease Assay (RNase)
The assay is performed in 50µl of reaction mixture containing reaction buffer, enzyme and 1µg of [3H]-labeled RNA. After incubation under the appropriate conditions, see Table 1, the RNA is precipitated with trichloroacetic acid and the radioactivity of the supernatant is determined. Ribonuclease activity is expressed as a percent of the total RNA radioactivity released into the acid soluble fraction. Details of the assay are provided in the Product Information insert supplied with each product.
The assay is performed in 200µl of reaction mixture containing 10mM Tris-HCl buffer (pH7.5), enzyme and 200µg of azocasein. After incubation under the appropriate conditions, see Table 1, the reaction is terminated with trichloroacetic acid and the absorbance of the supernatant is measured at 400nm. The product passes this quality control test if azocasein is not degraded.
Assays performed for a particular modifying enzyme or other protein are indicated both in the product entry and in the Product Information insert supplied with each product.
Table 1. Conditions for Quality Control Assays.
|Enzyme||Amount per assay||Incubation temp., °C||Incubation time, hour||QC performed|
|T4 DNA Ligase||200 U||37||4||dsEndo, LO, B/W, RNase|
|T4 RNA Ligase||50 U||37||4||dsEndo, LO, RNase|
|FastAP™ Thermosensitive Alkaline Phosphatase||10 U||37||4||dsEndo, Exo I, RNase|
|T4 Polynucleotide Kinase (T4 PNK)||50 U||37||4||dsEndo, Exo I, RNase|
|phi29 DNA Polymerase||100 U||30||4||ds-, ssEndo|
|DNA Polymerase I, E.coli||20 U||37||4||dsEndo|
|Klenow Fragment||20 U||37||4||dsEndo|
|Klenow Fragment, exo-||20 U||37||4||dsEndo, Exo I, LO|
|T4 DNA Polymerase||10 U||37||4||ds-, ssEndo|
|T7 DNA Polymerase||10 U||37||4||dsEndo|
|Terminal Deoxynucleotidyl Transferase (TdT)||60 U||37||4||dsEndo, LO, RNase|
|T7 RNA Polymerase||200 U||37||1||dsEndo, Exo I, RNase|
|SP6 RNA Polymerase||200 U||37||1||dsEndo, Exo I, RNase|
|T3 RNA Polymerase||200 U||37||1||dsEndo, Exo I, RNase|
|RiboLock™ RNase Inhibitor||200 U||37||4||dsEndo, LO, RNase|
|DNase I, RNase-free||10 U||37||4||RNase, Protease|
|Endonuclease IV, E.coli (Endo IV)||20 U||37||1||dsEndo, Exo I, RNase|
|Endonuclease V, T.maritima (Endo V)||25 U||37||4||dsEndo, Exo I, LO, RNase|
|Exonuclease I, E.coli (Exo I)||100 U||37||16||ds-, ssEndo, Exo II, RNase|
|Exonuclease III, E.coli (Exo III)||25 U||37||4||dsEndo|
|Lambda Exonuclease||100 U||37||4||dsEndo|
|RNase A, DNase and protease-free||5 µg
|RNase T1||1000 U
|RNase A/T1 Mix||2 µl
|RNase I, E.coli||80 U||37||4||dsEndo, Exo I, LO|
|RNase H, E.coli||10 U||37||1||dsEndo, Exo I, RNase|
|Agarase||5 U||37||4||dsEndo, LO, B/W, RNase|
|Proteinase K (recombinant), PCR grade||200 µg
|dsEndo, Exo I,
|Pyrophosphatase, Inorganic (from yeast)||1 U||37||24||dsEndo, Exo I, LO, RNase|
|Uracil-DNA Glycosylase (UDG)||50 U||37||4||dsEndo, LO, RNase|
"Thermo Fisher Scientific" (Vilnius Site) develops, produces and sells molecular biology products, which are recognized as high quality product in the global market. "Thermo Fisher Scientific" (Vilnius Site) personnel aims that all processes and products are safe and have minimal negative impact on the environment. The Company's Management is committed to support Environmental Management System and support it, by allocating adequate human, financial and technical resources.
Priority directions of the Company's environmental protection improvement:
- Safe management of chemicals
- Ensure the safe use of potentially infected biological materials
- Reduce chemical inputs to the sewage
- Properly monitor that genetically modified micro-organisms do not release to the environment
- Reduce waste and improve their management
"Thermo Fisher Scientific" (Vilnius Site) undertakes:
- Maintain and regularly improve the Environmental Management System, ensuring the compliance with ISO 14001 requirements
- Determining environmental objectives and tasks, refer to the commitments undertaken in the present Environmental Policy
- Comply with the applicable legal requirements relating to the Company's environmental aspects and other requirements, which the Company assumes
- Achieve continual improvement in the fields of environmental effectiveness and pollution prevention
- Combine the Environmental Policy with the Company's Quality Policy
- Use rationally non-renewable nature resources
- Observe the environmental impact of the Company, if possible
- Obtain state-of-art technologies and equipment, if possible
- Improve workers awareness of environmental issues related to the activities of the Company
- By implementing new projects to assess their impact on the environment
- Inform the public, current and newly hired personnel, people working on behalf of the Company (distributors), suppliers (contractors) and customers about this policy.
This policy is consistent with the Environmental, Health and Safety Policy of Thermo Fisher Scientific.
Fermentas, now part of Thermo Fisher Scientific, was the first restriction enzyme manufacturer to implement the ISO9001 quality management system in 1996.
In 2008, we became the first molecular biology company to manufacture in class D clean-room facilities qualified and certified according to EU directives and ISPE guidelines.
Our quality assurance is carried out according to ISO9001 quality and ISO14001 environmental management systems, guaranteeing batch-to-batch reproducibility. See our Environmental Policy for more details.
Manufacturing in Class D clean-room facilities, together with ISO9001 and ISO14001 management systems, guarantees lot-to-lot consistency.
Additionally, in 2010, the company has obtained and continues to maintain ISO13485 certification covering such activities as "Research and Developement, Manufacturing and Sales of in vitro diagnostic medical devices".
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