GlycoFlux™ Human PGK1 Overexpression CHO-K1 Cell Line

GlycoFlux™ human PGK1 overexpression CHO-K1 cell line produces PGK1 at high levels, a glycolytic enzyme that generates 3-phosphoglycerate while also acting as a moonlighting protein in angiogenesis and tumor progression. This versatile cell line enables research on metabolism, hemolytic anemia, neurological disorders, and cancer biology.

Overexpression 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.

qPCR, Sanger Sequencing

FBS & Penicillin/Streptomycin & Proline & DMEM

Mechanistic studies; Exploration of glycosylation and signaling pathways in cancer, metabolic, and immune-related diseases; Drug target validation and other functional assays.

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.

PGK1

Phosphoglycerate Kinase 1

PGKA; MIG10; HEL-S-68p

The protein encoded by this gene is a glycolytic enzyme that catalyzes the conversion of 1,3-diphosphoglycerate to 3-phosphoglycerate. The encoded protein may also act as a cofactor for polymerase alpha. Additionally, this protein is secreted by tumor cells where it participates in angiogenesis by functioning to reduce disulfide bonds in the serine protease, plasmin, which consequently leads to the release of the tumor blood vessel inhibitor angiostatin. The encoded protein has been identified as a moonlighting protein based on its ability to perform mechanistically distinct functions. Deficiency of the enzyme is associated with a wide range of clinical phenotypes hemolytic anemia and neurological impairment. Pseudogenes of this gene have been defined on chromosomes 19, 21 and the X chromosome.