GlycoErase™ GALNT16 Knockout CHO-K1 Cell Line (CAT#: GLJF-0425-JF34)

Description	The GALNT16 knockout CHO-K1 cell line investigates GALNT16, polypeptide N-acetylgalactosaminyltransferase 16, in CHO-K1 cells. GALNT16 is an N-acetylgalactosaminyltransferase. GALNT16 knockout in CHO cells may disrupt O-linked glycosylation; its WBS region location adds interest for studying genetic context of glycosylation in CHO.
Product Type	KO Cell Lines
Species	Hamster
Cell Morphology	Epithelial, adherent
Passage Ratio	1:3~1:5
Cell Line	CHO-K1
Lineage	Chinese hamster ovary

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	FBS & Penicillin/Streptomycin & Proline & RPMI
Application	Functional assay
Size	1 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	GALNT16
Full Name	Polypeptide N-acetylgalactosaminyltransferase 16
Alternative Name	KIAA1130, GALNTL1, GalNAc-T16
Location	14q24.1
Gene ID	57452
Summary	Transfers GalNAc to serine and threonine residues, contributing to O-linked glycosylation and influencing protein structure and function.