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CHO Cells

CHO cells, or Chinese Hamster Ovary cells, are a widely used cell line in biopharmaceutical research and production.
These mammalian cells are derived from the ovary of the Chinese hamster and are known for their ability to efficiently express and secrete recombinant proteins.
CHO cells are a versatile tool for the development of therapeutic antibodies, vaccines, and other biopharmaceutical products.
Researchers utilize CHO cells to study cellular processes, optimize expression systems, and evaluate the safety and efficacy of potential drug candidates.
With their well-characterized growth characteristics and post-translational modification capabilities, CHO cells remain a pivotal model system for advanceing biopharmaceutical discovry and manufactoring.
Experiance the power of CHO cell research with PubCompare.ai, your AI-driven platform for optimizing protocols and identifying the most effective methods.

Most cited protocols related to «CHO Cells»

1
Env Protein Expression in HEK293 and CHO Cells
The Env proteins from various env genes described above were expressed in wild type, adherent HEK293T cells or the 293F variant that is adapted for suspension cultures, or in CHO-K1 cells, essentially as described [25] (link), [27] (link), [46] (link), [64] (link). HEK293T and CHO-K1 cells were maintained in Dulbecco's modified Eagle's medium (DMEM) supplemented with 10% fetal calf serum (FCS), penicillin (100 U/ml), streptomycin (100 µg/ml), Glutamax (Invitrogen), non-essential amino acids (0.1 mM), sodium pyruvate (0.1 mM) and HEPES (0.1 mM). For gp140 trimer production, HEK293T or CHO-K1 cells were seeded at a density of 5.5×104/ml in a Corning Hyperflask. After 3 days, when the cells had reached a density of 1.0×106/ml, they were transfected using polyethyleneimine (PEI) as described elsewhere [65] (link). Briefly, PEI-MAX (1.0 mg/ml) in water was mixed with expression plasmids for Env and Furin [5] (link) in OPTI-MEM. For one Corning Hyperflask, 600 µg of Env plasmid, 150 µg of Furin plasmid and 3 mg of PEI-MAX were added in 550 ml of growth media. Culture supernatants were harvested 72 h after transfection. BG505 gp120 used in differential scanning calorimetry (DSC) experiments was produced in HEK293F cells using a protocol similar to that previously described [25] (link).
Sanders R.W., Derking R., Cupo A., Julien J.P., Yasmeen A., de Val N., Kim H.J., Blattner C., de la Peña A.T., Korzun J., Golabek M., de los Reyes K., Ketas T.J., van Gils M.J., King C.R., Wilson I.A., Ward A.B., Klasse P.J, & Moore J.P. (2013). A Next-Generation Cleaved, Soluble HIV-1 Env Trimer, BG505 SOSIP.664 gp140, Expresses Multiple Epitopes for Broadly Neutralizing but Not Non-Neutralizing Antibodies. PLoS Pathogens, 9(9), e1003618.
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Publication 2013
Amino Acids, Essential Calorimetry, Differential Scanning Cells CHO Cells Culture Media Fetal Bovine Serum FURIN protein, human Gene Products, Protein GP 140 HEPES HIV Envelope Protein gp120 Penicillins Plasmids Polyethyleneimine Proteins Pyruvate Sodium Streptomycin Transfection
2
Immunolocalization of PCM-1 in Xenopus A6 Cells
Affinity-purified PCM-1 antibody was injected into Xenopus A6 cells cultured on glass coverslips at 2 mg/ml in injection buffer (100 mM KCl, 10 mM potassium phosphate, pH 7.4). At 24 or 48 h after injection, coverslips were fixed with methanol at −20°C and processed for immunofluorescence as above. Control injections were performed using rabbit IgG (Sigma-Aldrich) at the same concentration in injection buffer. Purified dynamitin (Wittmann and Hyman, 1999 (link)) at a concentration of 9 mg/ml was injected into CHO cells. After 2–4 h of incubation, cells were fixed and processed for immunofluorescence. Control cells were injected with fluorescently labeled secondary antibody.
Dammermann A, & Merdes A. (2002). Assembly of centrosomal proteins and microtubule organization depends on PCM-1. The Journal of Cell Biology, 159(2), 255-266.
Publication 2002
Buffers Cells CHO Cells Fluorescent Antibody Technique Immunoglobulins Methanol potassium phosphate Rabbits Xenopus laevis
3
Genome Editing in Diverse Cell Lines
HeLa, DE4, HEK293AC2, mouse MC57 cells were cultured in Dulbecco's modified Eagle's medium with 10% FBS and 1% L-glutamine, and K562 cells were cultured in Iscove's modified Dulbecco's medium, 10% FBS and 1% L-glutamine. CHO cells were cultured in ex-Cell-CD media (Sigma Aldrich, USA) with 2% L-glutamine. Cells were nucleofected using solution kits T and V (K562) (Lonza, USA) and a Amaxa® Cell Line Nucleofector® device as previously described (15 ,16 ) using protocols provided by Lonza (http://www.lonzabio.com/resources/product-instructions/protocols/). In brief, 1 × 106 cells were transfected with 2 μg of ZFN or TALEN plasmid pairs or 2 μg of Dual-GALNT6-ZFN. For CRISPR/Cas9 CHO Cosmc targeting, 2 μg Cas9 and gRNA plasmids were nucleofected, and for pCMV-Cas9-GFP expressing KRAS gRNA 2 μg plasmid was used. Cells were exposed to a cold shock 30°C for 2 days post-transfection, and incubated one day at 37°C after which DNA of the cell pool was prepared using Nucleospin kit as recommended by the supplier (Machery-Nagel, USA).
For consecutive targeting of the KRAS locus, K562 cells were subjected to fluorescence-activated cell sorting (FACS) 3 days after nucleofection for isolation of the 2% most highly GFP fluorescent cells that were then cultured for about 1 week. Thereafter, an aliquot of the cell pool was analysed by IDAA (first hit), whereas the rest of the cells were subjected to another two rounds of nucleofection and FACS to produce second and third hit pools, respectively, Furthermore, after the third hit, cells were also single-cell plated in 96-well plates and expanded to clonal cell lines.
Yang Z., Steentoft C., Hauge C., Hansen L., Thomsen A.L., Niola F., Vester-Christensen M.B., Frödin M., Clausen H., Wandall H.H, & Bennett E.P. (2015). Fast and sensitive detection of indels induced by precise gene targeting. Nucleic Acids Research, 43(9), e59.
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Publication 2015
Cell Lines Cells Cell Separation CHO Cells Clone Cells Clustered Regularly Interspaced Short Palindromic Repeats Cold Shock Stress Cultured Cells Culture Media Glutamine HeLa Cells K-ras Genes K562 Cells KRAS protein, human Medical Devices MEV protocol Mus Plasmids Transcription Activator-Like Effector Nucleases Transfection
4
Fluorescence Microscopy of Mitochondria in CHO Cells
The coverslip attached with cells was put on a chamber and examined with a fluorescence microscope (IX-71, Olympus) with a objective (PlanApo, NA1.45, Olympus). Monochromator equipped with Xe-lamp (polychrome II, Till-photonics, Gräfelfing, Germany) was driven by TILLVision 4.0 (Till-Photonic, Gräfelfing, Germany) to excite DsRed-mito (550 nm). Fluorescence was filtered by a filter cube (Mitotracker orange: 565DCLP (BS), D605/55m (Em); Chroma, Rockingham, Vermont, USA), and 2D fluorescent cell images were acquired by a CCD camera (IMAGO, Till-Photonics Germany; exposure: 500ms; resolution: 12-bit, pixels, pixel size: ). The images are scaled down to 8-bit for image analysis, and pixel width is about 165nm.
We have compared 2D (epi-fluorescence microscopy) and 3D (confocal fluorescence microscopy) CHO micrographs, and found that CHO cells are flat and most of the mitochondria in 2D micrographs are in focus and clear enough for high content image analysis (see Section S2.1 in Text S1). Therefore, 2D micrographs are the major data source used in this study.
Peng J.Y., Lin C.C., Chen Y.J., Kao L.S., Liu Y.C., Chou C.C., Huang Y.H., Chang F.R., Wu Y.C., Tsai Y.S, & Hsu C.N. (2011). Automatic Morphological Subtyping Reveals New Roles of Caspases in Mitochondrial Dynamics. PLoS Computational Biology, 7(10), e1002212.
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Publication 2011
Cells CHO Cells Fluorescence Microscopy, Confocal Microscopy, Fluorescence Mitochondria Mitomycin mitotracker orange
5
Rapid CRISPR sgRNA Construction
The Cas9 sequence from the S. pyogenes strain M1 GAS genome with a 3′ nuclear localization signal was codon-optimized for CHO cells, synthesized (for sequence, see Supplementary Materials and Methods) and subcloned into the mammalian expression vector pJ607-03 (DNA 2.0, Menlo Park, CA, Fig. 1A). The plasmid was then transformed into DH5α subcloning cells (Life Technologies, Paisley, U.K.). Transformant clones were selected on 100 µg/mL Ampicillin (Sigma–Aldrich, St. Louis, MO) LB plates. The chosen sgRNA target sequences are listed in Supplementary Table SI. The sgRNA expression constructs were designed by fusing tracrRNA and crRNA into a chimeric sgRNA (Jinek et al., 2012 (link)) and located immediately downstream of a U6 promoter (Chang et al., 2013 (link)). The sequences of the U6 promoter, scaffold and terminator are shown in Supplementary Materials and Methods. Initially, the sgRNA expression cassette (Fig. 1A) was synthesized as a gBlock (Integrated DNA Technologies, Leuven, Belgium) and subcloned into the pRSFDuet-1 vector (Novagen, Merck, Damstadt, Germany) using KpnI and HindIII restriction sites. This pRSFDuet-1/sgRNA expression vector was used as backbone in a PCR-based uracil-specific excision reagent (USER) cloning method (Hansen et al., 2012 (link); Nour-Eldin et al., 2006 (link)). This method was designed to easily and rapidly change the 19 bp-long variable region (N19) of the sgRNA in order to generate our sgRNA constructs. From the pRSFDuet-1/sgRNA expression vector, a 4,221 bp-long amplicon (expression vector backbone) was generated by PCR (1×: 98°C for 2 min; 30×: 98°C for 10 s, 57°C for 30 s, 72°C for 4 min 12 s; 1×: 72°C for 5 min) using two uracil-containing primers (sgRNA Backbone_fw and sgRNA Backbone_rv, Integrated DNA Technologies, Supplementary Table SII) and the X7 DNA polymerase (Nørholm, 2010 (link)). Subsequent to Fastdigest DpnI (Thermo Fisher Scientific, Waltham, MA) treatment, the amplicon was purified from a 2% agarose TBE gel using the QIAEX II Gel Extraction Kit (Qiagen, Hilden, Germany). In parallel, 54 bp-long and 53 bp-long single stranded oligos (sense and antisense strand, respectively) comprising the variable region of the sgRNA were synthesized (TAG Copenhagen, Denmark, Supplementary Table SII). The sense and antisense single stranded oligos (100 µM) were annealed in NEBuffer4 (New England Biolabs, Ipswich, MA) by incubating the oligo mix at 95°C for 5 min in a heating block and the oligo mix was subsequently allowed to slowly cool to RT by turning off the heating block. The annealed oligos were then mixed with the gel purified expression vector backbone and treated with USER enzyme (New England Biolabs) according to manufacturer's recommendations. After USER enzyme treatment, the reaction mixture was transformed into E. coli Mach1 competent cells (Life Technologies) according to standard procedures. Transformant clones were selected on 50 µg/mL Kanamycin (Sigma–Aldrich) LB plates. All constructs were verified by sequencing and purified by NucleoBond Xtra Midi EF (Macherey-Nagel, Düren, Germany) according to manufacturer's guidelines.
Ronda C., Pedersen L.E., Hansen H.G., Kallehauge T.B., Betenbaugh M.J., Nielsen A.T, & Kildegaard H.F. (2014). Accelerating Genome Editing in CHO Cells Using CRISPR Cas9 and CRISPy, a Web-Based Target Finding Tool. Biotechnology and Bioengineering, 111(8), 1604-1616.
Publication 2014
2',5'-oligoadenylate Ampicillin Cells Chimera CHO Cells Clone Cells Cloning Vectors Codon crRNA, Transactivating DNA-Directed DNA Polymerase Enzymes Escherichia coli Genome Kanamycin Mammals Nuclear Localization Signals Oligonucleotide Primers Oligonucleotides Plasmids RNA, CRISPR Guide Sepharose Strains Streptococcus pyogenes Uracil Vertebral Column

Most recents protocols related to «CHO Cells»

1
PD-1/PD-L1 Blocking Antibody Assay
Not available on PMC !

Example 10

This example provides in vitro IC50 data for the blocking of the interaction between recombinant human PD-1 (PD-1-Fc Chimera; Sino Biologics) and human PD-L1 expressed CHO cells by anti-PD-L1 antibody G12. Here, CHO cells expressing PD-L1 were pre-incubated with G12 prior to the addition of rhPD-1-Fc chimeric protein. After incubation and washing, PD-1 binding to cell surface expressed PD-L1 was detected using an Alexa-Fluor 647 tagged anti-PD-1 antibody by flow cytometry (Intellicyt HTFC; FL-4H). This example shows that anti-PD-L1 monoclonal antibody G12 was able to inhibit efficiently the binding of PD-1 to PD-L1 expressed on the surface of CHO cells.

Results: As shown in FIG. 8 and Table 4, the IC50 for blocking of the PD-1/PD-L1 cellular interaction by G12 is 1.76E-09 M. Data was collected on the Intellicyt HTFC flow cytometer, processed using FlowJo software, and analyzed and plotted in Graph Pad Prizm using non-linear regression fit. Data points are shown as the median fluorescence detected in the FL-4H channel+/−Std Error.

TABLE 4
G12
Inhibition of PD-1/PD-L1CHO-PD-L1/1.76E−09
Interaction IC50 (M)rhPD-1-Fc

US11878058B2. Antigen binding proteins that bind PD-L1 (2024-01-23). Sorrento Therapeutics, Inc. [US]. Inventors: Heyue Zhou [US], Randy Gastwirt [US], Barbara A. Swanson [US], John Dixon Gray [US], Gunnar F. Kaufmann [US].
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Patent 2024
Alexa Fluor 647 Antibodies, Anti-Idiotypic Antigens Binding Proteins Biological Factors CD274 protein, human Cell Communication Cells Chimera CHO Cells Flow Cytometry Fluorescence Homo sapiens Immunoglobulins isononanoyl oxybenzene sulfonate Monoclonal Antibodies Proteins Psychological Inhibition
2
Binding Affinity of CD40-CEA Bispecific Antibodies
Not available on PMC !

Example 6

Aim and Background

The aim of this study was to assess the binding of the CD40-CEA RUBY™ bispecific antibodies to CEACAM5 expressed on cells and evaluate potential cross-reactivity to CEACAM1. In this study both CEACAM5 transfected cells and human tumor cells with endogenous CEACAM5 expression were used.

Materials and Methods

The human CEACAM5 and CEACAM1 genes were cloned into pcDNA3.1, and the vector was subsequently stably transfected into CHO cells. The tumor cell line MKN45, expressing high levels of CEACAM5, LS174T expressing intermediate levels of CEACAM5, and HT29 and LOVO expressing low levels of CEACAM5 (Table 16), CHO-CEACAM5, CHO-CEACAM1 and to CHO wt cells were incubated with titrated concentrations of CD40-CEA bispecific antibodies. Binding of the antibodies was detected using fluorochrome-conjugated anti-human IgG and analyzed using flow cytometry.

Results and Conclusions

The data demonstrate that all tested CD40-CEACAM5 RUBYs bind to CEACAM5 expressed on CHO-CEACAM5 (FIG. 6A-FIG. 6E), and MKN45 (high expressing) (FIG. 8A-FIG. 8C) and LS174T (intermediate expressing) human tumor cells (FIG. 8D-FIG. 8F). Low or no binding was observed to the CEACAM5 low expressing tumor cells, the LOVO cells (FIG. 8G-FIG. 8I). In addition, a low cross-reactivity to CEACAM1 or stickiness to CHO wt cells was observed with some of the CD40-CEA bispecific antibodies at very high concentrations (FIG. 7). In conclusion, all the CD40-CEA RUBY™ bispecific antibodies bind to CEACAM5 and with low or no binding to CEACAM1.

TABLE 16
Summary of CEA expression levels on CEACAM5 transfected
CHO cells and CEA expressing human tumor cells.
Tumor cell line and CEA
transfected CHO cellsReceptors/cell
HT2911 300
LOVO 5 500
LS174T51 500
MKN45353 000 
CHO-CEACAM5125 000 

US11873348B2. Peptides (2024-01-16). ALLIGATOR BIOSCIENCE AB [SE]. Inventors: Peter Ellmark [SE], Karin Hagerbrand [SE], Laura Varas [SE], Mattias Levin [SE], Anna Säll [SE], Laura von Schantz [SE].
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Patent 2024
anti-IgG Antibodies Antibodies, Bispecific biliary glycoprotein I CEACAM5 protein, human Cell Line, Tumor Cells CHO Cells Cloning Vectors Cross Reactions Flow Cytometry Fluorescent Dyes Genes Homo sapiens HT29 Cells Neoplasms
3
Development of Anti-IL-17RA Monoclonal Antibodies
Not available on PMC !

Example 7

The development of fully human monoclonal antibodies directed against human IL-17RA was carried out using Abgenix (now Amgen Fremont Inc.) XenoMouse® technology (U.S. Pat. Nos. 6,114,598; 6,162,963; 6,833,268; 7,049,426; 7,064,244, which are incorporated herein by reference in their entirety; Green et al, 1994, Nature Genetics 7:13-21; Mendez et al., 1997, Nature Genetics 15:146-156; Green and Jakobovitis, 1998, J. Ex. Med. 188:483-495)). TABLE 4 shows the portions of the IL-17RA protein used as an immunogen and cell lines used to generate and screen anti-IL-17RA antibodies.

TABLE 4
ReagentDescription
IL-17RA.FcHuman IL-17RA extracellular domain with a
C-terminal human Fc domain. Expressed in a
stable CHO cell line.
IL-17RA-FLAG-polyHisHuman IL-17RA extracellular domain with a
(SEQ ID NO: 431)C-terminal FLAG-polyHis tag. Expressed by
transient transfection in COS PKB cells.
IL-17RA CHO cellsHuman IL-17RA full-length expressed on the
surface of CHO cells.

IgG2 XenoMouse® mice were immunized/boosted with IL-17RA-Fc (group 1) and IL-17RA-FLAG-polyHis (group 2). Serum titers were monitored by ELISA and mice with the best titers were fused to generate hybridomas. The resulting polyclonal supernatants were screened for binding to IL-17RA by ELISA, and the positive supernatants were screened for binding to IL-17RA CHO cells by FMAT. Positive supernatants were subjected to additional screening. IgG2 XenoMouse® mice were immunized with the following immunogens: IL-17RA-Fc (group 3) and IL-17RA-FLAG-pHis (group 4) and were tested following additional immunizations.

US11858999B2. IL-17 receptor A antigen binding proteins (2024-01-02). AMGEN K-A, INC. [US]. Inventors: Joel E. Tocker [US], Jacques J. Peschon [US], David Fitzpatrick [AU], James F. Smothers [US], Christopher Mehlin [US], Ai Ching Lim [US].
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Patent 2024
Anti-Antibodies Antigens Binding Proteins Cell Lines CHO Cells COS Cells Enzyme-Linked Immunosorbent Assay GPI protein, human Homo sapiens Human Development Hybridomas IgG2 IL17RA protein, human Immunization Monoclonal Antibodies Mus Natural Childbirth Proteins Serum Transfection Transients
4
Anti-CD22 Antibody Binding Profiles
Not available on PMC !

Example 3

FIG. 4 summarizes target binding activity of the anti-CD22 heavy chain-only antibodies described herein. Column 1 indicates the Clone ID number of the anti-CD22 heavy chain-only antibody. Column 2 indicates the binding affinity to protein (KD) measured in molarity. Column 3 indicates the dissociation constant of binding to protein (K-off rate) measured in seconds. Column 4 indicates binding to Daudi cells measured as fold over background MFI signal. Column 5 indicates binding to CHO cells stably expressing cyno CD22 measured as fold over background MFI signal. Column 6 indicates binding to CHO cells that do not express CD22 protein measured as fold over background MFI signal.

US11873336B2. Heavy chain antibodies binding to CD22 (2024-01-16). TeneoBio, Inc. [US]. Inventors: Shelley Force Aldred [US], Wim van Schooten [US], Heather Anne N. Ogana [US], Laura Marie Davison [US], Katherine Harris [US], Udaya Rangaswamy [US], Nathan D. Trinklein [US].
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Patent 2024
Binding Proteins Cell Lines Cells CHO Cells Clone Cells Immunoglobulin Heavy Chains Neoplasm Metastasis Proteins
5
Potent ADCC Activities of Engineered Antibodies
Not available on PMC !

Example 3

The potency of 88D2C6 and 137D1H10, along with 370D2C10 (all fused to human IgG1 constant regions, with ADCC-activating mutations in Fc), in mediating ADCC was measured with CCR8-overexpressing CHO K1 and U2OS cells. All three antibodies exhibited high ADCC activities (FIG. 2).

All three antibodies exhibited potent ADCC activities. Among them, however, 88D2C6 had considerably higher potency (EC50: 0.01743 nM with CHO cells and 0.1108 for U2OS cells).

US11873342B2. Anti-CCR8 monoclonal antibodies and uses thereof (2024-01-16). LaNova Medicines Limited [CN]. Inventors: Runsheng Li [CN], Wentao Huang [CN].
Full text: Click here
Patent 2024
Antibodies CCR8 protein, human Cells CHO Cells Cytotoxicities, Antibody-Dependent Cell Gain of Function Mutation Homo sapiens IgG1

Top products related to «CHO Cells»

1
Fetal bovine serum (fbs) by Thermo Fisher Scientific
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Fetal Bovine Serum (FBS) is a cell culture supplement derived from the blood of bovine fetuses. FBS provides a source of proteins, growth factors, and other components that support the growth and maintenance of various cell types in in vitro cell culture applications.
2
Lipofectamine 2000 by Thermo Fisher Scientific
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Lipofectamine 2000 is a cationic lipid-based transfection reagent designed for efficient and reliable delivery of nucleic acids, such as plasmid DNA and small interfering RNA (siRNA), into a wide range of eukaryotic cell types. It facilitates the formation of complexes between the nucleic acid and the lipid components, which can then be introduced into cells to enable gene expression or gene silencing studies.
3
Dulbecco modified eagle medium (dmem) by Thermo Fisher Scientific
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DMEM (Dulbecco's Modified Eagle's Medium) is a cell culture medium formulated to support the growth and maintenance of a variety of cell types, including mammalian cells. It provides essential nutrients, amino acids, vitamins, and other components necessary for cell proliferation and survival in an in vitro environment.
4
Penicillin streptomycin by Thermo Fisher Scientific
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Penicillin/streptomycin is a commonly used antibiotic solution for cell culture applications. It contains a combination of penicillin and streptomycin, which are broad-spectrum antibiotics that inhibit the growth of both Gram-positive and Gram-negative bacteria.
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Streptomycin by Thermo Fisher Scientific
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Streptomycin is a broad-spectrum antibiotic used in laboratory settings. It functions as a protein synthesis inhibitor, targeting the 30S subunit of bacterial ribosomes, which plays a crucial role in the translation of genetic information into proteins. Streptomycin is commonly used in microbiological research and applications that require selective inhibition of bacterial growth.
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Penicillin is a type of antibiotic used in laboratory settings. It is a broad-spectrum antimicrobial agent effective against a variety of bacteria. Penicillin functions by disrupting the bacterial cell wall, leading to cell death.
7
L glutamine by Thermo Fisher Scientific
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L-glutamine is an amino acid that is commonly used as a dietary supplement and in cell culture media. It serves as a source of nitrogen and supports cellular growth and metabolism.
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Cho k1 cells by American Type Culture Collection
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CHO-K1 cells are a widely used Chinese hamster ovary (CHO) cell line. CHO-K1 cells are adherent in culture and are commonly used for the expression and production of recombinant proteins.
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Fetal bovine serum (fbs) by Merck Group
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FBS, or Fetal Bovine Serum, is a commonly used cell culture supplement. It is derived from the blood of bovine fetuses and provides essential growth factors, hormones, and other nutrients to support the growth and proliferation of a wide range of cell types in vitro.
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GlutaMAX is a chemically defined, L-glutamine substitute for cell culture media. It is a stable source of L-glutamine that does not degrade over time like L-glutamine. GlutaMAX helps maintain consistent cell growth and performance in cell culture applications.

More about "CHO Cells"

Chinese Hamster Ovary (CHO) cells are a widely utilized mammalian cell line in the biopharmaceutical industry.
These cells, derived from the ovary of the Chinese hamster, are renowned for their ability to efficiently express and secrete recombinant proteins, making them a crucial tool for the development of therapeutic antibodies, vaccines, and other biopharmaceutical products.
Researchers leveraging CHO cells can study cellular processes, optimize expression systems, and evaluate the safety and efficacy of potential drug candidates.
The well-characterized growth characteristics and post-translational modification capabilities of CHO cells make them a pivotal model system for advancing biopharmaceutical discovery and manufacturing.
Fetal Bovine Serum (FBS) is commonly used as a growth supplement in CHO cell culture media, providing essential nutrients and growth factors.
Lipofectamine 2000, a transfection reagent, is often utilized to facilitate the introduction of genetic material into CHO cells.
Dulbecco's Modified Eagle Medium (DMEM) is a widely used basal medium for CHO cell culture, supplemented with penicillin, streptomycin, and L-glutamine to support cell growth and survival.
The CHO-K1 cell line is a commonly used subclone of the original CHO cell line, known for its robust growth characteristics and ease of genetic manipulation.
GlutaMAX, a stable L-glutamine alternative, is also frequently employed in CHO cell culture to provide a reliable source of this essential amino acid.
Experiance the power of CHO cell research with PubCompare.ai, your AI-driven platform for optimizing protocols and identifying the most effective methods.