GlycoErase™ PRKAA1 Knockout CHO-K1 Cell Line

GlycoErase™ PRKAA1 knockout CHO-K1 cell line is a CHO-K1 model with PRKAA1 (AMPK α1 catalytic subunit) deleted. AMPK senses cellular energy via AMP/ATP changes and phosphorylates key metabolic enzymes to curb ATP-consuming biosynthesis. This knockout is suitable for dissecting energy-stress signaling, metabolic rewiring, and AMPK-dependent pathway pharmacology.

KO Cell Lines

Hamster

Epithelial, adherent

1:3~1:5

CHO-K1

Chinese hamster ovary

>90%

The sterility test indicated an absence of microbial growth.

STR identification

Negative

Negative for HIV, HBV and HCV.

We conduct cell genetic stability studies in full compliance with ICH guidelines. Our expertise enables us to design and execute a comprehensive testing program tailored to your specific needs and regulatory requirements.

PCR, Sanger Sequencing

FBS & Penicillin/Streptomycin & Proline & RPMI

Functional assay

1 M cells/vial*2

Frozen

Dry ice

Made to order

Upon receipt, this product must be immediately transferred from dry ice to liquid nitrogen (-150°C to -190°C) and stored in a liquid nitrogen tank. Cell viability is critically dependent on proper handling. We cannot guarantee viability if these instructions are not strictly adhered to.

This product is provided for research only, not suitable for human or animal use. Due to the inherent limitations of infectious agent testing, investigators must exercise extreme caution when handling cells provided by Creative Biolabs, treating all cells as potentially biohazardous.

PRKAA1

Protein Kinase Amp-Activated Catalytic Subunit Alpha 1

AMPK; AMPKa1; AMPK alpha 1

The protein encoded by this gene belongs to the ser/thr protein kinase family. It is the catalytic subunit of the 5'-prime-AMP-activated protein kinase (AMPK). AMPK is a cellular energy sensor conserved in all eukaryotic cells. The kinase activity of AMPK is activated by the stimuli that increase the cellular AMP/ATP ratio. AMPK regulates the activities of a number of key metabolic enzymes through phosphorylation. It protects cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. Alternatively spliced transcript variants encoding distinct isoforms have been observed.