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STT3B knockout HepG2 cell line lacks STT3B protein, STT3 oligosaccharyltransferase complex catalytic subunit B, another essential OST subunit for N-glycosylation in liver cells. STT3B knockout in HepG2 cells enables study of N-linked glycosylation disruption in liver cancer, potentially causing congenital glycosylation disorders affecting hepatocytes and impacting N-glycan dependent processes in liver tumor development.
Product Type
KO Cell Lines
Species
Human
Cell Morphology
Epithelial-like, adherent
Passage Ratio
1:4~1:6
Cell Line
HepG2
Primary Disease
Hepatoblastoma
Lineage
Liver
Lineage Subtype
Hepatoblastoma
Specification
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 & FBS & Glutamine
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 Information
Target
STT3B
Full Name
STT3 oligosaccharyltransferase complex catalytic subunit B
Catalytic subunit of a protein complex that transfers oligosaccharides to asparagine residues; defects cause congenital disorder of glycosylation Ix (CDG1X).