Description

HeLa cell
The HeLa cell line was established from an adenocarcinoma of the cervix in 1952. It is the first continuous human cell line.

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