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Merck

CHOK1

SAFC

CHOZN® CHO K1 Host Cell Line

Suspension-adapted in CD media

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About This Item

UNSPSC-Code:
12352200
Preise und Verfügbarkeit sind derzeit nicht verfügbar.

Beschreibung

CHOK1 cell line derived from ECACC CHO K1

Qualitätsniveau

Versandbedingung

dry ice

Lagertemp.

−196°C

Verwandte Kategorien

Allgemeine Beschreibung

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.

Ursprung der Zelllinie

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

Physikalische 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.

Rechtliche Hinweise

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

Lagerklassenschlüssel

10 - Combustible liquids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable


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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
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
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
T M Trask et al.
The Journal of biological chemistry, 275(32), 24400-24406 (2000-05-29)
Alignment of tropoelastin molecules during the process of elastogenesis is thought to require fibrillin-containing microfibrils. In this study, we have demonstrated that amino-terminal domains of two microfibrillar proteins, fibrillin-1 and fibrillin-2, interact with tropoelastin in solid phase binding assays. The
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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