GlycoErase™ PPP1R3A Knockout Glycoengineered Cell (CAT#: GLJF-0825-JF57)

Description	GlycoErase™ PPP1R3A knockout glycoengineered cell eliminates the skeletal muscle glycogen-targeting regulatory subunit of PP1, which directs PP1 to glycogen and regulates glycogen synthase and phosphorylase kinase. This model is valuable for studies of muscle glycogen metabolism and energy regulation.
Product Type	KO Cell Lines
Cell Line	As requested by the client.

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
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	PPP1R3A
Full Name	Protein Phosphatase 1 Regulatory Subunit 3A
Alternative Name	GM; PP1G; PPP1R3
Location	7q31.1
Gene ID	5506
Summary	The glycogen-associated form of protein phosphatase-1 (PP1) derived from skeletal muscle is a heterodimer composed of a 37-kD catalytic subunit and a 124-kD targeting and regulatory subunit. This gene encodes the regulatory subunit which binds to muscle glycogen with high affinity, thereby enhancing dephosphorylation of glycogen-bound substrates for PP1 such as glycogen synthase and glycogen phosphorylase kinase.