GYS1
GYS1 (glycogen synthase 1) is the muscle glycogen synthase, an enzyme that extends glycogen by adding glucose units from UDP-glucose to a growing alpha-1,4-glucan chain. It is also known as GSY and GYS, and was previously named glycogen synthase 1 (muscle). Browse Assay Genie's current range of GYS1 research reagents below, or read on for the biology behind the target.
GYS1 takes part in the glycogen biosynthetic process together with glycogenin and glycogen branching enzyme. Glycogenin forms a primer of a few glucose units, and GYS1 extends this primer. It does so by transferring the glycosyl residue from UDP-glucose to the non-reducing end of an alpha-1,4-glucan. The result is the formation of alpha-1,4-glycoside linkages as glucose monomers are added to the growing glycogen molecule.
The protein is catalogued by UniProt as glycogen [starch] synthase, muscle, and belongs to the glycosyltransferase 3 family. HGNC places the GYS1 gene in the glycosyl transferases group 1 domain containing group. The enzyme carries the EC number 2.4.1.11. Mouse and rat each have a Gys1 ortholog, so the enzyme can be studied in common rodent models. The related glycogen synthase GYS2 is a separate gene product.
According to the NCBI Gene summary, mutations in the GYS1 gene are associated with muscle glycogen storage disease. Alternatively spliced transcript variants encoding different isoforms have also been reported. Earlier symbols and names for the gene include GSY, GYS and glycogen synthase 1 (muscle). Researchers studying the GYS1 protein, whether by GYS1 antibody or GYS1 ELISA kit based methods, are usually interested in glycogen metabolism and in how defects in this enzyme relate to storage disease.
GYS1 extends the glycogenin-formed primer with glucose from UDP-glucose, making it a central enzyme for studying how glycogen is built.
Mutations in the GYS1 gene are associated with muscle glycogen storage disease, which makes the protein relevant to disease mechanism research.
As a member of the glycosyltransferase 3 family acting on UDP-Glc and alpha-1,4-glucan, GYS1 is a model for glycosyl transfer.
Alternatively spliced transcript variants encoding different isoforms have been reported for GYS1, supporting work on gene expression and isoform biology.
GYS1 is a glycogen synthase that works with glycogenin and glycogen branching enzyme in glycogen biosynthesis. It extends the glucose primer made by glycogenin, transferring glucose from UDP-glucose to the non-reducing end of an alpha-1,4-glucan and forming alpha-1,4-glycoside linkages.
GYS1 is the HGNC symbol for glycogen synthase 1. UniProt names the protein glycogen [starch] synthase, muscle. Aliases include GSY and GYS, and the gene was previously named glycogen synthase 1 (muscle). NCBI notes that alternatively spliced transcript variants encode different isoforms.
Mouse and rat both have a Gys1 ortholog. In humans, mutations in the GYS1 gene are associated with muscle glycogen storage disease. Check the datasheet of any product for its validated reactivity before using it with a particular species.
Other glycogen synthase family members and related glycogen metabolism targets with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P13807; product specifications from Assay Genie datasheets.