Quality Control
Cultures are screened for the presence of bacteria, yeast, fungi and mycoplasma (DNA amplification). NBCS used in the culture medium is certified from New Zealand origin.

HeLa Nuclear Extracts Production
HeLa cells are grown in sonoperfused fedbatch (cytostat) mode at a constant concentration of 5×10⁶ cells/ml (cell viability: 93%-99%) under GLP conditions in our facility in Mons, Belgium. Cells are harvested in exponential phase.

The Nuclear Extracts are prepared according to:
Dignam, J. D., Lebovitz, R. M., and Roeder, R. G. (1983) Nucleic Acids Res. 11, 1475-1489

Conc. Protein (Bradford) = +/- 6 mg/ml

No dialysis is performed during the preparation of this product. The preparation stopped after the ultra-centrifugation step. Buffer composition is then the same as the extraction buffer.

Research Use
Our HeLa Nuclear Extracts are used by research or production entities worldwide for the study of biochemical processing, high throughput screening or purification of biological material from human origin.

Source of HDAC activity, transcription factors, chromatin proteins and histones.

Also suitable for use in:

• separation by SDS-PAGE;
• Gel Shift assays used for protein-DNA interactions studies;
• HDAC assays;
• positive control for Western Blot assays;
• in vitro splicing;
• transcription factors studies;
• cell division cycle and apoptosis studies;
• spliceosome and other proteome studies (DNA ends, snRNP’s, DNA PKcs, …).

References

• Laggerbauer, B., Lauber, J. and Lührmann, R. (1996). Identification of an RNA-dependent ATPase activity in mammalian U5 SnRNPs. Nucl. Ac. Res. 24, 868-875.
• Sirand-Pugnet, P., Durosay, P., Clouet d’Orval, B., Brody, E., Marie, J. (1995). R-Tropomyosin pre-mRNA folding around a muscle-specific exon interferes with several steps of spliceosome assembly. J. Mol. Biol. 251, 591-602.
• Gell, D. and Jackson, S. P. (1999). Mapping of protein-protein interactions within the DNA-dependent protein kinase complex. Nucl. Ac. Res. 27, 3494-3502.
• Izzard, R.A., Jackson, S.P. and Smith, G.C.M. (1999). Competitive and non-competitive inhibition of the DNA-dependent protein kinase. Cancer Res. 59, 2581-2586.
• Lakin, N.D., Hann, B.C. and Jackson, S.P. (1999) The ataxia-telangiectasia related protein ATR mediates DNA-dependent phosphorylation of P53. Oncogene 68, 3989-3995.
• Smith, G.C., Cary, R.B., Lakin, N.D., Hann, B.C., Teo, S._H., Chen, D.J. and Jackson, S.P. (1999) Purification and DNA binding properties of the ataxia-telangiectasia gene product ATM. Proc. Natl. Acad. Sci. USA 96, 11134-11139.
• Smith, G.C., d’Adda di Fagagna, F., Lakin, N.D. and Jackson, S.P. (1999) Cleavage and inactivation of ATM during apoptosis. Molec. Cell. Biol. 19, 6076-6084.
• Chew, S.L., Baginsky, L., Eperon, I.C. (2000) An exonic splicing silencer in the testes-specific DNA ligase III B exon. Nucleic Acid Res. 28, 402-410.
• Deplus, R., Brenner, C., Burgers, W.A., Putmans, P., Kouzarides, T., de Launoit, Y., Fuks, F. (2002) Dnmt3L is a transcriptional repressor that recruits histone deacetylase. Nucleic Acid Res. 30, n°17, 3831-3838.
• Hallay, H., Locker, N., Ayadi, L., Ropers, D., Guittet, E. and Branlant, C. (2006) Biochemical and NMR study on the competition between proteins SC35, SRp40 and hnRNP A1 at the HIV-1 Tat exon 2 splicing site. J. Biol. Chem., Vol. 281, Issue 48, 37159-37174
• Hanna, C., Gjerde, D., Nguyen, L., Dickman, M., Brown, P. and Hornby, D. (2006) Micro-scale open-tube capillary separations of functional proteins. Analytical Biochemistry 350, 128-137.
• Jacquenet, S., Méreau, A., Bilodeau, P.S., Damier, L., Martin Stoltzfus, C. and Branlant, C. (2001) A Second Exon Splicing Silencer within Human Immunodeficiency Virus Type 1 tat Exon 2 Represses Splicing of Tat mRNA and Binds Protein hnRNP H*. J. Biol. Chem., 276, No 44, Issue of November 2, 40464-40475
• Roche,K.C., Wiechens,N., Owen-Hughes,T and Perkins, N.D. (2004) The FHA domain protein SNIP1 is a regulator of the cell cycle and cyclin D1 expression. Oncogene 23, 8185-8195
• Brandt, D., Marion, S., Griffiths, G., Watanabe, T., Kaibuchi, K. and Grosse, R. (2007) Dia 1 and IQGAP1 interact in cell migration and phagocytic cup formation. Journal of Cell Biology 178, 193-200
• Ropers, D., Ayadi, L., Gattoni, R., Jacquenet, S., Damier, L., Branlant, C. and Stévenin, J. (2004) Differential effects of the SR proteins 9G8, SC35, ASF/SF2 and SRp40 on the utilization of the A1 to A5 splicing sites of HIV-1 RNA. J. Biol. Chem., 279, 29963-29973
• Gehring, N.H., Lamprinaki, S., Kulozik, A.E. and Hentze, M. (2009) Disassembly of exon junction complexes by PYM. Cell 137, 536-548
• Gehring, N.H., Lamprinaki, S., Hentze, M. and Kulozik, A.E. (2009) The hierarchy of exon-junction complex assembly by the spliceosome explains key features of mammalian nonsense-mediated mRNA decay. Plos Biology 7 (5) e 1000120
• Rivera-Calzada, A., Spagnolo, L., Laurence H., P., Llorca, O. (2007) Structural model of full-lengh human Ku70-Ku80 heterodimer and its recognition of DNA and DNA-PKcs. EMBO reports 8, 56-62
• Stefan Reber, Jolanda Stettler1, Giuseppe Filosa, Martino Colombo Daniel Jutzi, Silvia C Lenzken, Christoph Schweingruber, Rémy Bruggmann, Angela Bachi, Silvia ML Barabino, Oliver Mühlemann & Marc-David Ruepp (2016) Minor intron splicing is regulated by FUS and affected by ALS-associated FUS mutants. The EMBO Journal 35: 1504–1521
• JiwenYang, Lee-HsuehHung, ThomasLicht, SawaKostin, MarioLooso, EkaterinaKhrameeva, AlbrechtBindereif, AndreSchneider, ThomasBraun. (2014) RBM24 Is a Major Regulator of Muscle-Specific Alternative Splicing. Developmental Cell Volume 31, Issue 1, 13 October 2014, Pages 87-99
• Vivien Berthelot, Gildas Mouta-Cardoso, Nadia Hégarat, François Guillonneau, Jean-Christophe François, Carine Giovannangeli, Danièle Praseuth, Filippo Rusconi. (2016) The human DNA ends proteome uncovers an unexpected entanglement of functional pathways. Nucleic Acids Research, Volume 44, Issue 10, 2 June 2016, Pages 4721–4733
• Katarzyna Dorota Raczynska Marc-David Ruepp Aleksandra Brzek Stefan Reber Valentina Romeo Barbara Rindlisbacher Manfred Heller Zofia Szweykowska-Kulinska Artur Jarmolowski Daniel Schümperli. (2015) FUS/TLS contributes to replication-dependent histone gene expression by interaction with U7 snRNPs and histone-specific transcription factors. Nucleic Acids Research, Volume 43, Issue 20, 16 November 2015, Pages 9711–9728
• Tim Schneider, Lee-Hsueh Hung, Silke Schreiner, Stefan Starke, Heinrich Eckhof , Oliver Rossbach, Stefan Reich, Jan Medenbach, and Albrecht Bindereif. (2016) CircRNA-protein complexes: IMP3 protein component defines subfamily of circRNPs. Nature Sci Rep. 2016; 6: 31313.
• Andri Christodoulou and Hideki Yokoyama. (2015) Purification of nuclear localization signal-containing proteins and its application to investigation of the mechanisms of the cell division cycle. Small GTPases. 2015 Jan-Mar; 6(1): 20–27
• Lorenzo Lafranchi, Harmen R de Boer, Elisabeth GE de Vries, Shao-En Ong, Alessandro A Sartori and Marcel ATM van Vugt. (2014) APC/CCdh1 controls CtIP stability during the cell cycle and in response to DNA damage. EMBO J. 2014 Dec 1; 33(23): 2860–2879.
• Takashi Ochi, Andrew N. Blackford, Julia Coates, Satpal Jhujh, Shahid Mehmood, Naoka Tamura, Jon Travers, Qian Wu, Viji M. Draviam, Carol V. Robinson, Tom L. Blundell, and Stephen P. Jackson (2015) PAXX, a paralog of XRCC4 and XLF, interacts with Ku to promote DNA double-strand break repair. Science. 2015 Jan 9; 347(6218): 185–188.
• Andrew N. Blackford, Jadwiga Nieminuszczy, Rebekka A. Schwab, Yaron Galanty, Stephen P. Jackson, and Wojciech Niedzwiedz (2015) TopBP1 Interacts with BLM to Maintain Genome Stability but Is Dispensable for Preventing BLM Degradation. Mol Cell. 2015 Mar 19; 57(6): 1133–1141

Quality Control
Cultures are screened for the presence of bacteria, yeast, fungi and mycoplasma (DNA amplification). NBCS used in the culture medium is certified from New Zealand origin.

HeLa Mitochondria Production
HeLa cells are grown in sonoperfused fedbatch (cytostat) mode at a constant concentration of 5×10⁶ cells/ml (cell viability: 93%-99%) under GLP conditions in our facility in Mons, Belgium. Cells are harvested in exponential phase.

Research Use
Our Hela Mitochondria are used by research or production entities worldwide for the study of biochemical processing, high throughput screening or purification of biological material from human origin.

Also suitable for use in:

• human mitochondrial processes studies;
• purification of mitochondrial DNA;
• purification and isolation of mitochondrial proteins (ERK1/2, mitochondrial ribosomes, …).

For published papers reporting the use of our extract, please check out our references list.

Downloads – Documents

Quality Control
Cultures are screened for the presence of bacteria, yeast, fungi and mycoplasma (DNA amplification). NBCS used in the culture medium is certified from New Zealand origin.

HeLa S100 Cytoplasmic Extracts Production
HeLa cells are grown in sonoperfused fedbatch (cytostat) mode at a constant concentration of 5×10⁶ cells/ml (cell viability: 93%-99%) under GLP conditions in our facility in Mons, Belgium. Cells are harvested in exponential phase.

Ipracell, provider of high quality HeLa Nuclear Extract (HNE) expands its activities by making available the cytoplasm prepared from exponentially growing HeLa cells (HeLa Cytoplasmic Extract: HCE).
HCE is a rich source of:

• complexes (40S, 60S ribosomal subunits and 80S ribosomes etc…)
• Factors involved in translation (eIFs’, IRES- and PolyA binding proteins).
• Factors which play a role on different parts of the mRNA molecule (5′- and 3′ UTRs’).

It can be used to study the regulation of muRNA processing, mRNA polymorphism etc…
Preliminary data suggest that HCE compares favorably with the rabbit reticulocyte lysate for cell-free protein expression.
HCE production automation makes it possible to offer this subcellular fraction of high and reproducible quality at very competitive prices.

Research Use
Our HeLa S100 Cytoplasmic Extracts are used by research or production entities worldwide for the study of biochemical processing, high throughput screening or purification of biological material from human origin.

Also suitable for use in:

• in vitro splicing;
• protein-DNA/RNA and protein-protein interactions;
• source of individual splicing factors and other regulatory proteins.

Downloads – Documents

References

• Plessel, G., Fischer, U. and Lührmann, R, (1994). m3G cap hypermethylation of U1 small nuclear ribonucleoprotein (SnRNP) in vitro: evidence that the U1 small nuclear RNA-(guanosine-N2)­methyltransferase is a non-SnRNP cytoplasmic protein that requires a binding site on the Sm core domain. Molecular and Cellular Biology 14, 4160-4172.

Quality Control
Cultures are screened for the presence of bacteria, yeast, fungi and mycoplasma (DNA amplification). NBCS used in the culture medium is certified from New Zealand origin.

HeLa Cytoplasmic Extracts Production
HeLa cells are grown in sonoperfused fedbatch (cytostat) mode at a constant concentration of 5×10⁶ cells/ml (cell viability: 93%-99%) under GLP conditions in our facility in Mons, Belgium. Cells are harvested in exponential phase.

Ipracell, provider of high quality HeLa Nuclear Extract (HNE) expands its activities by making available the cytoplasm prepared from exponentially growing HeLa cells (HeLa Cytoplasmic Extract: HCE).
HCE is a rich source of:

• complexes (40S, 60S ribosomal subunits and 80S ribosomes etc…)
• Factors involved in translation (eIFs’, IRES- and PolyA binding proteins).
• Factors which play a role on different parts of the mRNA molecule (5′- and 3′ UTRs’).

It can be used to study the regulation of muRNA processing, mRNA polymorphism etc…
Preliminary data suggest that HCE compares favorably with the rabbit reticulocyte lysate for cell-free protein expression.
HCE production automation makes it possible to offer this subcellular fraction of high and reproducible quality at very competitive prices.

Research Use
Our HeLa Cytoplasmic Extracts are used by research or production entities worldwide for the study of biochemical processing, high throughput screening or purification of biological material from human origin.

Also suitable for use in:

• purification and isolation of cytoplasmic protein;
• translatome analysis;
• circRNAs studies;
• ribosomal subunits studies;
• replication studies.

Downloads – Documents

References

• Angulo J, Ulryck N, Deforges J, Chamond N, Lopez-Lastra M, Masquida B, Sargueil B (2016) LOOP IIId of the HCV IRES is essential for the structural rearrangement of the 40S-HCV IRES complex. Nucleic Acids Res 44: 1309-1325
• Chamond N, Deforges J, Ulryck N, Sargueil B (2014) 40S recruitment in the absence of eIF4G/4A by EMCV IRES refines the model for translation initiation on the archetype of Type II IRESs. Nucleic Acids Res 42: 10373-10384
• King, Helen A., El-Sharif, Hazim F., Matia-González, Ana M., Iadevaia, Valentina, Fowotade, Adeola, Reddy, Subrayal M and Gerber, André P. (2017) Generation of ribosome imprinted polymers for sensitive detection of translational responses. Scientific Reports, 7 (1). ISSN 2045-2322
• Alexander R. Langley, Stefan Graf, James C. Smith, and Torsten Krude. (2016) Genome-wide identification and characterisation of human DNA replication origins by initiation site sequencing (ini-seq). Nucleic Acids Research, 2016 doi: 10.1093/nar/gkw760

Quality Control
Cultures are screened for the presence of bacteria, yeast, fungi and mycoplasma (DNA amplification). NBCS used in the culture medium is certified from New Zealand origin.

HeLa Nuclear Extracts Production
HeLa cells are grown in sonoperfused fedbatch (cytostat) mode at a constant concentration of 5×10⁶ cells/ml (cell viability: 93%-99%) under GLP conditions in our facility in Mons, Belgium. Cells are harvested in exponential phase.

The Nuclear Extracts are prepared according to:
Dignam, J. D., Lebovitz, R. M., and Roeder, R. G. (1983) Nucleic Acids Res. 11, 1475-1489

Conc. Protein (Bradford) = +/- 6 mg/ml

Buffer used for dialysis of our Nuclear Extracts is:

• HEPES 20mM
• KCl 100mM
• EDTA 0.2mM
• Glycerol 20%
• PMSF 0.2mM
• DTT 0.5mM

Research Use
Our HeLa Nuclear Extracts are used by research or production entities worldwide for the study of biochemical processing, high throughput screening or purification of biological material from human origin.

Source of HDAC activity, transcription factors, chromatin proteins and histones.

Also suitable for use in:

• separation by SDS-PAGE;
• Gel Shift assays used for protein-DNA interactions studies;
• HDAC assays;
• positive control for Western Blot assays;
• in vitro splicing;
• transcription factors studies;
• cell division cycle and apoptosis studies;
• spliceosome and other proteome studies (DNA ends, snRNP’s, DNA PKcs, …).

Downloads – Documents

References

• Laggerbauer, B., Lauber, J. and Lührmann, R. (1996). Identification of an RNA-dependent ATPase activity in mammalian U5 SnRNPs. Nucl. Ac. Res. 24, 868-875.
• Sirand-Pugnet, P., Durosay, P., Clouet d’Orval, B., Brody, E., Marie, J. (1995). R-Tropomyosin pre-mRNA folding around a muscle-specific exon interferes with several steps of spliceosome assembly. J. Mol. Biol. 251, 591-602.
• Gell, D. and Jackson, S. P. (1999). Mapping of protein-protein interactions within the DNA-dependent protein kinase complex. Nucl. Ac. Res. 27, 3494-3502.
• Izzard, R.A., Jackson, S.P. and Smith, G.C.M. (1999). Competitive and non-competitive inhibition of the DNA-dependent protein kinase. Cancer Res. 59, 2581-2586.
• Lakin, N.D., Hann, B.C. and Jackson, S.P. (1999) The ataxia-telangiectasia related protein ATR mediates DNA-dependent phosphorylation of P53. Oncogene 68, 3989-3995.
• Smith, G.C., Cary, R.B., Lakin, N.D., Hann, B.C., Teo, S._H., Chen, D.J. and Jackson, S.P. (1999) Purification and DNA binding properties of the ataxia-telangiectasia gene product ATM. Proc. Natl. Acad. Sci. USA 96, 11134-11139.
• Smith, G.C., d’Adda di Fagagna, F., Lakin, N.D. and Jackson, S.P. (1999) Cleavage and inactivation of ATM during apoptosis. Molec. Cell. Biol. 19, 6076-6084.
• Chew, S.L., Baginsky, L., Eperon, I.C. (2000) An exonic splicing silencer in the testes-specific DNA ligase III B exon. Nucleic Acid Res. 28, 402-410.
• Deplus, R., Brenner, C., Burgers, W.A., Putmans, P., Kouzarides, T., de Launoit, Y., Fuks, F. (2002) Dnmt3L is a transcriptional repressor that recruits histone deacetylase. Nucleic Acid Res. 30, n°17, 3831-3838.
• Hallay, H., Locker, N., Ayadi, L., Ropers, D., Guittet, E. and Branlant, C. (2006) Biochemical and NMR study on the competition between proteins SC35, SRp40 and hnRNP A1 at the HIV-1 Tat exon 2 splicing site. J. Biol. Chem., Vol. 281, Issue 48, 37159-37174
• Hanna, C., Gjerde, D., Nguyen, L., Dickman, M., Brown, P. and Hornby, D. (2006) Micro-scale open-tube capillary separations of functional proteins. Analytical Biochemistry 350, 128-137.
• Jacquenet, S., Méreau, A., Bilodeau, P.S., Damier, L., Martin Stoltzfus, C. and Branlant, C. (2001) A Second Exon Splicing Silencer within Human Immunodeficiency Virus Type 1 tat Exon 2 Represses Splicing of Tat mRNA and Binds Protein hnRNP H*. J. Biol. Chem., 276, No 44, Issue of November 2, 40464-40475
• Roche,K.C., Wiechens,N., Owen-Hughes,T and Perkins, N.D. (2004) The FHA domain protein SNIP1 is a regulator of the cell cycle and cyclin D1 expression. Oncogene 23, 8185-8195
• Brandt, D., Marion, S., Griffiths, G., Watanabe, T., Kaibuchi, K. and Grosse, R. (2007) Dia 1 and IQGAP1 interact in cell migration and phagocytic cup formation. Journal of Cell Biology 178, 193-200
• Ropers, D., Ayadi, L., Gattoni, R., Jacquenet, S., Damier, L., Branlant, C. and Stévenin, J. (2004) Differential effects of the SR proteins 9G8, SC35, ASF/SF2 and SRp40 on the utilization of the A1 to A5 splicing sites of HIV-1 RNA. J. Biol. Chem., 279, 29963-29973
• Gehring, N.H., Lamprinaki, S., Kulozik, A.E. and Hentze, M. (2009) Disassembly of exon junction complexes by PYM. Cell 137, 536-548
• Gehring, N.H., Lamprinaki, S., Hentze, M. and Kulozik, A.E. (2009) The hierarchy of exon-junction complex assembly by the spliceosome explains key features of mammalian nonsense-mediated mRNA decay. Plos Biology 7 (5) e 1000120
• Rivera-Calzada, A., Spagnolo, L., Laurence H., P., Llorca, O. (2007) Structural model of full-lengh human Ku70-Ku80 heterodimer and its recognition of DNA and DNA-PKcs. EMBO reports 8, 56-62
• Stefan Reber, Jolanda Stettler1, Giuseppe Filosa, Martino Colombo Daniel Jutzi, Silvia C Lenzken, Christoph Schweingruber, Rémy Bruggmann, Angela Bachi, Silvia ML Barabino, Oliver Mühlemann & Marc-David Ruepp (2016) Minor intron splicing is regulated by FUS and affected by ALS-associated FUS mutants. The EMBO Journal 35: 1504–1521
• JiwenYang, Lee-HsuehHung, ThomasLicht, SawaKostin, MarioLooso, EkaterinaKhrameeva, AlbrechtBindereif, AndreSchneider, ThomasBraun. (2014) RBM24 Is a Major Regulator of Muscle-Specific Alternative Splicing. Developmental Cell Volume 31, Issue 1, 13 October 2014, Pages 87-99
• Vivien Berthelot, Gildas Mouta-Cardoso, Nadia Hégarat, François Guillonneau, Jean-Christophe François, Carine Giovannangeli, Danièle Praseuth, Filippo Rusconi. (2016) The human DNA ends proteome uncovers an unexpected entanglement of functional pathways. Nucleic Acids Research, Volume 44, Issue 10, 2 June 2016, Pages 4721–4733
• Katarzyna Dorota Raczynska Marc-David Ruepp Aleksandra Brzek Stefan Reber Valentina Romeo Barbara Rindlisbacher Manfred Heller Zofia Szweykowska-Kulinska Artur Jarmolowski Daniel Schümperli. (2015) FUS/TLS contributes to replication-dependent histone gene expression by interaction with U7 snRNPs and histone-specific transcription factors. Nucleic Acids Research, Volume 43, Issue 20, 16 November 2015, Pages 9711–9728
• Tim Schneider, Lee-Hsueh Hung, Silke Schreiner, Stefan Starke, Heinrich Eckhof , Oliver Rossbach, Stefan Reich, Jan Medenbach, and Albrecht Bindereif. (2016) CircRNA-protein complexes: IMP3 protein component defines subfamily of circRNPs. Nature Sci Rep. 2016; 6: 31313.
• Andri Christodoulou and Hideki Yokoyama. (2015) Purification of nuclear localization signal-containing proteins and its application to investigation of the mechanisms of the cell division cycle. Small GTPases. 2015 Jan-Mar; 6(1): 20–27
• Lorenzo Lafranchi, Harmen R de Boer, Elisabeth GE de Vries, Shao-En Ong, Alessandro A Sartori and Marcel ATM van Vugt. (2014) APC/CCdh1 controls CtIP stability during the cell cycle and in response to DNA damage. EMBO J. 2014 Dec 1; 33(23): 2860–2879.
• Takashi Ochi, Andrew N. Blackford, Julia Coates, Satpal Jhujh, Shahid Mehmood, Naoka Tamura, Jon Travers, Qian Wu, Viji M. Draviam, Carol V. Robinson, Tom L. Blundell, and Stephen P. Jackson (2015) PAXX, a paralog of XRCC4 and XLF, interacts with Ku to promote DNA double-strand break repair. Science. 2015 Jan 9; 347(6218): 185–188.
• Andrew N. Blackford, Jadwiga Nieminuszczy, Rebekka A. Schwab, Yaron Galanty, Stephen P. Jackson, and Wojciech Niedzwiedz (2015) TopBP1 Interacts with BLM to Maintain Genome Stability but Is Dispensable for Preventing BLM Degradation. Mol Cell. 2015 Mar 19; 57(6): 1133–1141
• Pia-Amata Leimbacher, Samuel E.Jones, Ann-Marie K.Shorrocks, Marade Marco Zompit, Matthew Day, Jordy Blaauwendraad, Diana Bundschuh, Sarah Bonham, Roman Fischer, Daniel Fink, Benedikt M.Kessler, Antony W.Oliver, Laurence H.Pearl, Andrew N.Blackford, ManuelStucki (2019) MDC1 Interacts with TOPBP1 to Maintain Chromosomal Stability during Mitosis. Mol Cell. 2019 May 2; 74(3): 571-583.e8

Quality Control
Cultures are screened for the presence of bacteria, yeast, fungi and mycoplasma (DNA amplification). NBCS used in the culture medium is certified from New Zealand origin.

HeLa cells Production
HeLa cells are grown in sonoperfused fedbatch (cytostat) mode at a constant concentration of 5×10⁶ cells/ml (cell viability: 93%-99%) under GLP conditions in our facility in Mons, Belgium. Cells are harvested in exponential phase.

Cell pellets are prepared by low speed centrifugation, rinsed with phosphate-buffered saline, snap frozen in liquid nitrogen and stored at -85°C.

The cell pellets are not prepared in aseptic conditions and are not intended to be used as seed for a new culture.

Research Use
Our HeLa cell pellets are used by research or production entities worldwide for the study of biochemical processing, high throughput screening or purification of biological material from human origin.

Also suitable for use in:

• entities production and purification of biological material from human origin used in many other applications;

• biochemical processing;

• isolation of gDNA and RNA;

• fixation of the pellet;

• production of whole cell lysates;

• histochemistry.

Downloads – Documents

References

• Barabino, S.M.L., Sproat, B.S. and Lamond, A.I. (1992). Antisense probes targeted to an internal domain in U2 snRNP specifically inhibit the second step of pre-mRNA splicing. Nucl. Ac. Res. 20, 4457-4464.
• Calvio, C., Neubauer, G., Mann, M. and Lamond, A.I. (1995). Identification of hnRNP P2as TLS/FUS using electrospray mass spectrometry. RNA 1, 724-733.
• Fabrizio, P., Laggerbauer, B., Lauber, J., Lane, W.S. and Lührmann, R. (1997). An evolutionary conserved U5 SnRNP-specific protein is a GTP-binding factor closely related to the ribosomal translocase EF-2. EMBO Journal 16, 4092-4106.
• Hackl, W., Fischer, V. and Lührmann, R. (1994). A 69 kD protein that associates reversibly with the Sm core domain of several spliceosomal SnRNP species. J. Cell Biol. 124, 261-272.
• Kreivi, J.P., Trinkle-Mulcahy, L., Lyon, C.E., Morrice, N.A., Cohen, P., Lamond, A.I. (1997). Purification and characterisation of p99, a nuclear modulator of protein phosphatase 1 activity FEBS Letters 420, 57­62.
• Lamm, G.M., Blencowe, B.J., Sproat, B.S., Iribarren, A.M., Ryder, U. and Lamond, A.I. (1991). Antisense probes containing 2-aminoadenosine allow efficient depletion of U5 snRNP from HeLa splicing extracts. Nucl. Ac. Res. 19, 3193-3198.
• Lauber, J., Fabrizio, P., Teigelkamp, S., Lane, W.S., Hartmann, E. and Lührmann, R. (1996). The HeLa 200 kDa U5 SnRNP-specific protein and its homologue in Saccharomyces cerevisiae are members of the DEXH-box protein family of putative RNA helicases. EMBO Journal 15, 4001-4015.
• Lauber, J., Plessel, G., Prehn, S., Will, C.L., Fabrizio, P., Grôning, K., Lane, W.S. and Lührmann, R. (1997). The human U4/U6 SnRNP contains 60 and 90 kD proteins that are structurally homologous to the yeast splicing factors Prp4p and Prp3p. RNA. 3, 926-941.
• Mermoud, J.E., Cohen, P. and Lamond, A.I. (1992). Ser/Thr-specific protein phosphatases are required for both catalytic steps of pre-mRNA splicing. Nucl. Ac. Res. 20, 5263-5269.
• Rossmanith, W., Tullo, A., Potuschak, T., Karwan, R. (1995). Human mitochondrial tRNA processing. J. Biol. Chem. 270, 12885-12891.
• Ryder, U., Sproat, B.S. and Lamond, A.I. (1990). Sequence-specific affinity selection of mammalian splicing complexes. Nucl. Ac. Res. 18, 7373-7379.
• Ségault, V., Will, C.L., Sproat, B.S. and Lührmann, R. (1995). In vitro reconstitution of mammalian U2 and U5 snRNPs active in splicing : Sm proteins are essential for the formation of functional U2 and U5 SnRNPs. EMBO Journal 14, 7010-4021.
• Will, C.L., Rümpler, S., Gunnewiek, J.K., Van Venrooij, W. and Lührmann, R. (1996). In vitro reconstitution of mammalian U1 SnRNPs active in splicing : the U1:C protein enhances the formation of early (E) spliceosomal complexes. Nucl. Ac. Res. 24, 4614-4623.
• Cairns, C.A. and White, R.J. (1998) p53 is a general repressor of RNA polymerase III transcription. EMBO Journal 17, 3112-3123.
• Agranat, L., Sperling, J. and Sperling, R. (2010) A novel tissue-specific alternatively spliced form of the A-to-I RNA editing enzyme ADAR2. RNA Biology 7, 1-10