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CHOK1

SAFC

CHOZN® CHO K1 Host Cell Line

Suspension-adapted in CD media

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description

CHOK1 cell line derived from ECACC CHO K1

Quality Level

shipped in

dry ice

storage temp.

−196°C

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CHODHFRCLL1223CLL1221
CHOZN® CHO K1 Host Cell Line Suspension-adapted in CD media

SAFC

CHOK1

CHOZN® CHO K1 Host Cell Line

storage temp.

−196°C

storage temp.

−196°C

storage temp.

−196°C

storage temp.

−196°C

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

200

description

CHOK1 cell line derived from ECACC CHO K1

description

CHOZN® DHFR-/- ZFN-modified CHO cell line, dihydrofolate reductase knockout cell line

description

-

description

-

General description

A subclone of the parental CHO cell line, which was derived from the ovary of an adult Chinese hamster. Cells require proline due to the absence of the gene for proline synthesis, the block in the biosynthetic chain lies in the step converting glutamic acid to glutamine γ serialdehyde. They undergo morphological changes in response to cholera toxin.
CHO-K1 cells derived from ECACC CHO K1 and adapted to suspension and serum-free, chemically defined media. Cells are cGMP banked in chemically defined, animal component-free EX-CELL® CD CHO Fusion medium.

Cell Line Origin

Hamster Chinese ovary. The parental CHO-K1 cell line was originated by Puck in 1957.

Physical form

CHOZN CHO K1 cells are provided to customers in vials containing 1 mL at 107 cells/mL. Cells are banked in EX-CELL CD Fusion medium containing 4mM L glutamine and 7% DMSO.

Legal Information

The CHOZN CHO K1 cell line is sold for research use only. For use of this cell line in a commercial process, a commercial license must be taken.
CHOZN is a registered trademark of Merck KGaA, Darmstadt, Germany
EX-CELL is a registered trademark of Merck KGaA, Darmstadt, Germany

Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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Cheng-Yu Chung et al.
Biotechnology journal, 12(2) (2016-12-13)
Immunoglobin G with α-2,6 sialylation has been reported to have an impact on antibody-dependent cellular cytotoxicity and anti-inflammatory efficacy. However, production of antibodies with α-2,6 sialylation from Chinese hamster ovary cells is challenging due to the inaccessibility of sialyltransferases for
Hideharu Abe et al.
The Journal of biological chemistry, 287(24), 20430-20442 (2012-04-05)
Activation of mesangial cells (MCs), which is characterized by induction of smooth muscle α-actin (SMA) expression, contributes to a key event in various renal diseases; however, the mechanisms controlling MC differentiation are still largely undefined. Activated Smad1 induced SMA in
Qiong Wang et al.
Biotechnology and bioengineering, 119(1), 102-117 (2021-10-15)
The N-glycan pattern of an IgG antibody, attached at a conserved site within the fragment crystallizable (Fc) region, is a critical antibody quality attribute whose structural variability can also impact antibody function. For tailoring the Fc glycoprofile, glycoengineering in cell
Nouran Abualsaud et al.
Frontiers in cell and developmental biology, 8, 627090-627090 (2021-03-09)
Neuropeptide Y (NPY) has been implicated in the regulation of cellular motility under various physiological and pathological conditions, including cancer dissemination. Yet, the exact signaling pathways leading to these effects remain unknown. In a pediatric malignancy, neuroblastoma (NB), high NPY
Mena Abdelsayed et al.
The Journal of physiology, 593(18), 4201-4223 (2015-07-02)
Cardiac arrhythmias are often associated with mutations in SCN5A the gene that encodes the cardiac paralogue of the voltage-gated sodium channel, NaV 1.5. The NaV 1.5 mutants R1193Q and E1784K give rise to both long QT and Brugada syndromes. Various

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