ClonaCell™ Media for Hybridoma and CHO Cell Line Development
ClonaCell™ for Hybridoma and Cell Line Development
Liquid and Semi-Solid Media for Efficient Cell Cloning and Generation
Develop CHO cell line, hybridomas, and other cell types using the ClonaCell™ portfolio of innovative cell line-specific media, designed to provide optimal culture conditions. Available in both methylcellulose-based (semi-solid) and liquid form, ClonaCell™-CHO and ClonaCell™-HY formulations help you achieve a high probability of monoclonality and clonal diversity in just one step.
View all ClonaCell™ media and supplements, and download our brochure to help you choose the right product for your needs.
Use ClonaCell™ to:
- Save time and resources with a proven semi-solid cloning method that overcomes the challenges of traditional limiting dilution cloning
- Nurture and save finicky hybridomas generated from mouse, rat, human, rabbit and hamster cells
- Increase subcloning efficiency during CHO cell line development
Research-stage biotechnology companies and antibodies service companies use ClonaCell™-HY to complete antibody development projects faster and deliver the best antibodies for each application.
Dr. M. Javad Aman, President and CSO, Integrated BioTherapeutics, Inc.
Why Use ClonaCell™?
- Save time with semi-solid cloning. Don’t waste resources on empty cloning wells.
- Superior cloning efficiency and growth of CHO and other cell lines, hybridomas and myelomas.
- Base methylcellulose medium is easily customized for your cell type. Custom formulations, packaging, and additional sizes are available upon request.
- Rigorous performance testing, ensuring lot-to-lot reproducibility.
- Industry-recognized manufacturing expertise and unparalleled technical support.
Try ClonaCell™ in your own lab.
ClonaCell™ for Hybridoma Generation and Expansion
ClonaCell™-HY Hybridoma Kit
Components (Available Separately):
Recommended Applications:
All steps of mouse monoclonal antibody production: cell fusion, semi-solid cloning/selection and expansion of hybridomas
Advantages:
- Combines the hybridoma selection and cloning into one step
- Single-cell derived hybridomas form visible discrete colonies in semi-solid medium for easy picking and screening
- Rare clones not lost through overgrowth
Resources:
ClonaCell™FLEX
Size:
45 mL
Format:
Semi-solid
Formulation:
- Serum-free
- Chemically defined
- Animal component-free
- Protein-free
- Methylcellulose
- DHFR and GS compatible
Recommended Applications:
- Creating customized semi-solid media for selection and cloning of suspension-adapted CHO cells and hybridomas
- Converting a liquid medium into semi-solid medium for selection and cloning of a wide variety of cell types
- Recloning of established, suspension-adapted CHO cells
Advantages:
- Allows users to create a customized semi-solid medium optimized for a variety of cell types
- Allows users to convert an existing liquid cloning method into a semi-solid cloning method
Resources:
ClonaCell™-HY Liquid HAT Selection Medium
Size:
500 mL
Format:
Liquid
Formulation:
- DMEM
- Pre-selected serum
- L-Glutamine
- Gentamycin
- Supplements
- Hypoxanthine
- Aminopterin
- Thymidine
- 2-Mercaptoethanol
Recommended Applications:
- Selection of hybridomas following cell fusion
- Cloning of individual hybridomas by limiting dilution
Advantages:
Simplifies hybridoma selection in liquid suspension cultures.
Resources:
ClonaCell™-HY Medium D without HAT
Size:
90 mL
Format:
Semi-solid
Formulation:
- DMEM
- Pre-selected serum
- L-Glutamine
- Gentamycin
- Supplements
- Hypoxanthine
- Aminopterin
- Thymidine
- 2-Mercaptoethanol
Recommended Applications:
- One-step selection (if appropriate selective agent is added) and semi-solid cloning of hybridomas
- Used after cell fusion
Advantages:
- Combines the hybridoma selection and cloning into one step
- Single-cell derived hybridomas form visible discrete colonies in semi-solid medium for easy picking, screening, and expanding
- Rare clones not lost through overgrowth
Resources:
ClonaCell™-HY AOF Expansion Medium
Size:
500 mL
Format:
Liquid
Formulation:
- Hypoxanthine
- Thymidine
- Gentamicin
- L-Glutamine
- Recombinant proteins
Recommended Applications:
- Growth and expansion of hybridomas (mouse, rat) and myelomas (mouse, rat, human)
Advantages:
- Animal origin-free
- Reduces performance variability in the medium
- Simplifies downstream clone screening and antibody purification (no serum-derived IgG)
Resources:
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ClonaCell™-HY Hybridoma Kit Media
ClonaCell™-HY Medium A
Size:
500 mL
Format:
Liquid
Ingredients:
- DMEM
- Pre-selected serum
- L-Glutamine
- Gentamycin
- Supplements
- 2-Mercaptoethanol
Application:
Supports the growth of myeloma cells prior to fusion
ClonaCell™-HY Medium B
Size:
500 mL
Format:
Liquid
Ingredients:
- DMEM
- L-Glutamine
- Gentamycin
- 2-Mercaptoethanol
Application:
Used during the fusion process
ClonaCell™-HY Medium C
Size:
100 mL
Format:
Liquid
Ingredients:
- DMEM
- Pre-selected serum
- L-Glutamine
- Gentamycin
- Supplements
- 2-Mercaptoethanol
Application:
Promotes hybridoma viability after fusion prior to HAT selection
ClonaCell™-HY Medium D
Size:
90 mL
Format:
Semi-solid
Ingredients:
- DMEM
- Pre-selected serum
- L-Glutamine
- Gentamycin
- Supplements
- Hypoxanthine
- Aminopterin
- Thymidine
- 2-Mercaptoethanol
Application:
Used for selection and cloning of hybridomas in one step
ClonaCell™-HY Medium E
Size:
500 mL
Format:
Liquid
Ingredients:
- DMEM
- Pre-selected serum
- L-Glutamine
- Gentamycin
- Supplements
- Hypoxanthine
- Thymidine
- 2-Mercaptoethanol
Application:
Supports hybridoma growth and expansion after HAT selection
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ClonaCell™ for CHO Cell Line Development
ClonaCell™-CHO CD Medium
Size:
90 mL
Format:
Semi-solid
Formulation:
- Serum-free
- Chemically defined
- Animal component-free
- Protein-free
- DHFR and GS compatible
Ingredients:
- Methylcellulose
- Kolliphor P188 / Pluronic F68
Recommended Applications:
- Selection and cloning of suspension-adapted CHO cells
- Recloning of established, suspension-adapted CHO cells
Advantages:
Enables single-cell cloning in a chemically defined, animal component-free, protein-free medium
Resources:
ClonaCell™ FLEX
Size:
45 mL
Format:
Semi-solid
Formulation:
- Serum-free
- Chemically defined
- Animal component-free
- Protein-free
- DHFR and GS compatible
Ingredients:
Methylcellulose
Recommended Applications:
- Creating customized semi-solid media for selection and cloning of suspension-adapted CHO cells and hybridomas
- Converting a liquid medium into semi-solid medium for selection and cloning of a wide variety of cell types
- Recloning of established, suspension-adapted CHO cells
Advantages:
- Allows users to create a customized semi-solid medium optimized for a variety of cell types
- Allows users to convert an existing liquid cloning method into a semi-solid cloning method
ClonaCell™-CHO CD Liquid
Size:
500 mL
Format:
Liquid
Formulation:
- Serum-free
- Chemically defined
- Animal component-free
- Protein-free
- DHFR and GS compatible
Ingredients:
Kolliphor P188 / Pluronic F68
Recommended Applications:
- Culture of suspension-adapted CHO cells
- Adaptation of CHO cells for selection and cloning
- Expanding CHO cells following semi-solid cloning
- Limiting dilution cloning of CHO cells when used with ClonaCell™-CHO ACF Supplement
- Cryopreservation of CHO cells when combined with DMSO
Advantages:
- Supports expansion of CHO cells in a chemically defined, animal component-free, protein-free medium
- Compatible with all other ClonaCell™ products
ClonaCell™-CHO ACF Medium
Size:
90 mL
Format:
Semi-solid
Formulation:
- Serum-free
- Animal component-free
- DHFR and GS compatible
Ingredients:
- Methylcellulose
- Supplements
- Kolliphor P188 / Pluronic F68
Recommended Applications:
- Selection and cloning of transfected suspension-adapted CHO cells where serum-free or animal component-free media is required
- Recloning of established, suspension-adapted CHO cells
Advantages:
- Contains only recombinant proteins and synthetic components
- Greater single cell cloning efficiency of CHO cells compared with chemically defined, protein-free media (particularly at low plating densities)
Resources:
ClonaCell™-CHO ACF Supplement
Size:
2.5 mL
Format:
Liquid
Formulation:
- Serum-free
- Animal component-free
- DHFR and GS compatible
Ingredients:
Supplements
Recommended Applications:
- Supplementing chemically defined, protein-free media or semi-solid media to promote growth of CHO cells during single-cell cloning and expansion
- Supporting CHO cell expansion
Advantages:
- Contains only recombinant proteins and chemically defined components at 40X
- Does not contain serum or hydrolysates
ClonaCell™-TCS Medium
Size:
80 mL
Format:
Semi-solid
Formulation:
Serum-containing
Ingredients:
- Methylcellulose
- 2-Mercaptoethanol
- L-Glutamine
Recommended Applications:
- Selection, cloning, and recloning of suspension-adapted or adherent CHO cells and other cell lines
- Applications where high cloning efficiency and robust colony formation is important
Advantages:
Supports high cloning efficiency and robust colony formation for a variety of cell lines such as: CHO-K1, CHO-S, HEK-293, B16F-10, BaF/3, BHK-1, FD-5, Jurkat Daudi, Molt-4, UT-7
Resources:
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Scientific Resources
Protocol
How to Prepare and Plate Semi-Solid Methylcellulose Medium for Cell Culture
Brochure
Increase the Efficiency of Your Hybridoma Workflow with EasySep™ and ClonaCell™
Brochure
ClonaCell™ Media for Hybridoma and Cell Line Development
Tech Tip
Achieving Monoclonality in Hybridoma Cultures
Key Applications
Cell Line Development:
Ling SSM et al. (2015) Instrumental Role of Helicobacter Pylori γ-Glutamyl Transpeptidase in VacA-Dependent Vacuolation in Gastric Epithelial Cells. PLoS One 10(6): e0131460.
Rodríguez L et al. (2015) Generation of Monoclonal Antibodies Specific of The Postfusion Conformation of The Pneumovirinae Fusion (F) Protein. J Virol Methods.
Young J et al. (2015) A Novel Immunoassay to Measure Total Serum Lymphotoxin-α Levels in The Presence of An Anti-LTα Therapeutic Antibody. J Immunol Methods Epub ahead.
Chronopoulou E et al. (2014) Hybridoma Technology for The Generation of Rodent mAbs via Classical Fusion. In: Ossipow V, N Fischer (Eds.) Monoclonal Antibodies: Methods and Protocols, Methods in Molecular Biology. 2nd Ed. New York: Springer Science+Business Media.: pp47–70.
Date Y et al. (2014) Label-Free Impedimetric Immunoassay for Trace Levels of Polychlorinated Biphenyls in Insulating Oil. Anal Chem 86(6): 2989–2996.
García-Barreno B et al. (2014) Characterization of An Enhanced Antigenic Change in The Pandemic 2009 H1N1 Influenza Virus Haemagglutinin. J Gen Virol 95(PART 5): 1033–1042.
Tan GS et al. (2014) Characterization of a Broadly Neutralizing Monoclonal Antibody That Targets The Fusion Domain of Group 2 Influenza A Virus Hemagglutinin. J Virol 88(23): 13580–13592.
Kelly-Cirino CD & Mantis NJ. (2009) Neutralizing Monoclonal Antibodies Directed Against Defined Linear Epitopes on Domain 4 of Anthrax Protective Antigen. Infect Immun 77(11): 4859–4867.
Weidanz J a et al. (2006) Levels of Specific Peptide-HLA Class I Complex Predicts Tumor Cell Susceptibility to CTL Killing. J Immunol 177(8): 5088–5097.
Rodríguez L et al. (2015) Generation of Monoclonal Antibodies Specific of The Postfusion Conformation of The Pneumovirinae Fusion (F) Protein. J Virol Methods.
Young J et al. (2015) A Novel Immunoassay to Measure Total Serum Lymphotoxin-α Levels in The Presence of An Anti-LTα Therapeutic Antibody. J Immunol Methods Epub ahead.
Chronopoulou E et al. (2014) Hybridoma Technology for The Generation of Rodent mAbs via Classical Fusion. In: Ossipow V, N Fischer (Eds.) Monoclonal Antibodies: Methods and Protocols, Methods in Molecular Biology. 2nd Ed. New York: Springer Science+Business Media.: pp47–70.
Date Y et al. (2014) Label-Free Impedimetric Immunoassay for Trace Levels of Polychlorinated Biphenyls in Insulating Oil. Anal Chem 86(6): 2989–2996.
García-Barreno B et al. (2014) Characterization of An Enhanced Antigenic Change in The Pandemic 2009 H1N1 Influenza Virus Haemagglutinin. J Gen Virol 95(PART 5): 1033–1042.
Tan GS et al. (2014) Characterization of a Broadly Neutralizing Monoclonal Antibody That Targets The Fusion Domain of Group 2 Influenza A Virus Hemagglutinin. J Virol 88(23): 13580–13592.
Kelly-Cirino CD & Mantis NJ. (2009) Neutralizing Monoclonal Antibodies Directed Against Defined Linear Epitopes on Domain 4 of Anthrax Protective Antigen. Infect Immun 77(11): 4859–4867.
Weidanz J a et al. (2006) Levels of Specific Peptide-HLA Class I Complex Predicts Tumor Cell Susceptibility to CTL Killing. J Immunol 177(8): 5088–5097.
Hybridoma Development with ClonaCell™ in Different Species:
Chronopoulou E et al. (2014) Hybridoma Technology for the Generation of Rodent mAbs via Classical Fusion. In: Ossipow V, N Fischer (Eds.) Monoclonal Antibodies: Methods and Protocols, Methods in Molecular Biology. 2nd Ed. New York: Springer Science+Business Media.: pp47–70.
Cesaro A et al. (2012) An Inflammation Loop Orchestrated by S100A9 and Calprotectin Is Critical for Development of Arthritis. PLoS One 7(9): e45478.
Smith S a. et al. (2012) Persistence of Circulating Memory B Cell Clones with Potential for Dengue Virus Disease Enhancement for Decades following Infection. J Virol 86(5): 2665–2675.
Fang L et al. (2008) Essential Role of TNF Receptor Superfamily 25 (TNFRSF25) in the Development of Allergic Lung Inflammation. J Exp Med 205(5): 1037–1048.
Ulbrandt ND et al. (2006) Isolation and Characterization of Monoclonal Antibodies Which Neutralize Human Metapneumovirus In Vitro and In Vivo. J Virol 80(16): 7799–7806.
Grimaldi JC et al. (1999) Depletion of Eosinophils in Mice through the Use of Antibodies Specific for C-C Chemokine Receptor 3 (CCR3). J Leukoc Biol 65(6): 846–853.
Cesaro A et al. (2012) An Inflammation Loop Orchestrated by S100A9 and Calprotectin Is Critical for Development of Arthritis. PLoS One 7(9): e45478.
Smith S a. et al. (2012) Persistence of Circulating Memory B Cell Clones with Potential for Dengue Virus Disease Enhancement for Decades following Infection. J Virol 86(5): 2665–2675.
Fang L et al. (2008) Essential Role of TNF Receptor Superfamily 25 (TNFRSF25) in the Development of Allergic Lung Inflammation. J Exp Med 205(5): 1037–1048.
Ulbrandt ND et al. (2006) Isolation and Characterization of Monoclonal Antibodies Which Neutralize Human Metapneumovirus In Vitro and In Vivo. J Virol 80(16): 7799–7806.
Grimaldi JC et al. (1999) Depletion of Eosinophils in Mice through the Use of Antibodies Specific for C-C Chemokine Receptor 3 (CCR3). J Leukoc Biol 65(6): 846–853.
Pharmacology and Drug Discovery:
Cabral TM et al. (2014) Development of Neutralizing Monoclonal Antibodies against The Pandemic H1N1 Virus (2009) Using Plasmid DNA Immunogen. J Virol Methods 195: 54–62.
Retamal M et al. (2014) Epitope Mapping of The 2009 Pandemic and the A/Brisbane/59/2007 Seasonal (H1N1) Influenza Virus Haemagglutinins Using mAbs and Escape Mutants. J Gen Virol 95(Pt_11): 2377–2389.
Hostetter DR et al. (2007) Hip Is A Pro-Survival Substrate of Granzyme B. J Biol Chem 282(38): 27865–27874.
Jin C et al. (2006) Immunoglobulin G Specifically Binding Plant N-glycans with High Affinity Could Be Generated in Rabbits But Not in Mice. Glycobiology 16(4): 349–357.
Kuroki M et al. (2005) Preparation of Human IgG and IgM Monoclonal Antibodies for MK-1/Ep-CAM by Using Human Immunoglobulin Gene-Transferred Mouse and Gene Cloning of Their Variable Regions. Anticancer Res 25(6A): 3733–3739.
Retamal M et al. (2014) Epitope Mapping of The 2009 Pandemic and the A/Brisbane/59/2007 Seasonal (H1N1) Influenza Virus Haemagglutinins Using mAbs and Escape Mutants. J Gen Virol 95(Pt_11): 2377–2389.
Hostetter DR et al. (2007) Hip Is A Pro-Survival Substrate of Granzyme B. J Biol Chem 282(38): 27865–27874.
Jin C et al. (2006) Immunoglobulin G Specifically Binding Plant N-glycans with High Affinity Could Be Generated in Rabbits But Not in Mice. Glycobiology 16(4): 349–357.
Kuroki M et al. (2005) Preparation of Human IgG and IgM Monoclonal Antibodies for MK-1/Ep-CAM by Using Human Immunoglobulin Gene-Transferred Mouse and Gene Cloning of Their Variable Regions. Anticancer Res 25(6A): 3733–3739.
Immunology Research:
Flyak AI et al. (2015) Mechanism of Human Antibody-Mediated Neutralization of Marburg Virus. Cell 160(5): 893–903.
Fang L et al. (2008) Essential Role of TNF Receptor Superfamily 25 (TNFRSF25) in The Development of Allergic Lung Inflammation. J Exp Med 205(5): 1037–1048.
Matsumoto SC et al. (2006) Retinal Dysfunction in Patients with Chronic Chagas’ Disease Is Associated to Anti-Trypanosoma Cruzi Antibodies That Cross-React with Rhodopsin. FASEB J 21: 1–21.
Fang L et al. (2008) Essential Role of TNF Receptor Superfamily 25 (TNFRSF25) in The Development of Allergic Lung Inflammation. J Exp Med 205(5): 1037–1048.
Matsumoto SC et al. (2006) Retinal Dysfunction in Patients with Chronic Chagas’ Disease Is Associated to Anti-Trypanosoma Cruzi Antibodies That Cross-React with Rhodopsin. FASEB J 21: 1–21.
Cancer Research:
Chen D et al. (2014) Increased Expression of Id1 and Id3 Promotes Tumorigenicity by Enhancing Angiogenesis and Suppressing Apoptosis in Small Cell Lung Cancer. Genes Cancer 5-6(May): 212–225.
Stern HM et al. (2010) Development of Immunohistochemistry Assays to Assess GALNT14 and FUT3/6 in Clinical Trials of Dulanermin and Drozitumab. Clin Cancer Res 16(5): 1587–1596.
Chen Y et al. (2007) Armed Antibodies Targeting The Mucin Repeats of The Ovarian Cancer Antigen, MUC16, Are Highly Efficacious in Animal Tumor Models. Cancer Res 67(10): 4924–4932.
Wittman VP et al. (2006) Antibody Targeting to A Class I MHC-Peptide Epitope Promotes Tumor Cell Death. J Immunol 177(6): 4187–4195.
Stern HM et al. (2010) Development of Immunohistochemistry Assays to Assess GALNT14 and FUT3/6 in Clinical Trials of Dulanermin and Drozitumab. Clin Cancer Res 16(5): 1587–1596.
Chen Y et al. (2007) Armed Antibodies Targeting The Mucin Repeats of The Ovarian Cancer Antigen, MUC16, Are Highly Efficacious in Animal Tumor Models. Cancer Res 67(10): 4924–4932.
Wittman VP et al. (2006) Antibody Targeting to A Class I MHC-Peptide Epitope Promotes Tumor Cell Death. J Immunol 177(6): 4187–4195.
