GlycoErase™ HEK293F-ΔGALNT18 Cell Line (CAT#: GLJF-0425-JF292)

Description	This GALNT18 knockout (HEK293F) cell line lacks the GALNT18 protein, a polypeptide N-acetylgalactosaminyltransferase 18. Enables polypeptide N-acetylgalactosaminyltransferase activity. Involved in protein O-linked glycosylation. Predicted to be located in Golgi membrane. Loss of GALNT18 function may disrupt O-linked glycosylation.
Product Type	KO Cell Lines
Species	Human
Cell Morphology	Epithelial-like, adherent
Passage Ratio	1:2~1:4
Cell Line	HEK293F
Lineage	Embryonic kidney

Cell Viability	>90%
Sterility Test	The sterility test indicated an absence of microbial growth.
Identity Test	STR identification
Mycoplasma Test	Negative
Virus Test	Negative for HIV, HBV and HCV.
Genetic Stability Testing	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.
Validation	PCR, Sanger Sequencing
Culture Medium	DMEM
Application	Functional assay
Size	2 M cells/vial*2
Product Format	Frozen
Shipping	Dry ice
Availability Status	Made to order
Handling Notes	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.
Product Disclaimer	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.

Target	GALNT18
Full Name	Polypeptide N-acetylgalactosaminyltransferase 18
Alternative Name	GalNAc-T18, MGC71806, GALNT15, GALNTL4
Location	11p15.4
Gene ID	374378
Summary	Polypeptide N-acetylgalactosaminyltransferase predicted to be involved in protein O-linked glycosylation; potentially localized to the Golgi membrane.