GlycoErase™ HEK293F-ΔGALNT2 Cell Line (CAT#: GLJF-0425-JF293)

Description	This GALNT2 knockout (HEK293F) cell line lacks the GALNT2 protein, a polypeptide N-acetylgalactosaminyltransferase 2. This gene encodes a member of the glycosyltransferase 2 protein family. Members of this family initiate mucin-type O-glycosylation of peptides in the Golgi apparatus. The encoded protein transfers N-acetylgalactosamine to serine or threonine residues on target peptides. Loss of GALNT2 function may disrupt mucin-type O-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	GALNT2
Full Name	Polypeptide N-acetylgalactosaminyltransferase 2
Alternative Name	GalNAc-T2
Location	1q42.13
Gene ID	2590
Summary	Initiates mucin-type O-glycosylation in the Golgi apparatus; may be involved in O-linked glycosylation of the immunoglobulin A1 hinge region.