Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
PYGL encodes a homodimeric protein that catalyses the cleavage of alpha-1,4-glucosidic bonds to release glucose-1-phosphate from liver glycogen stores. Additionally we are shipping PYGL Kits (37) and PYGL Proteins (19) and many more products for this protein.
Showing 10 out of 83 products:
Human Polyclonal PYGL Primary Antibody for ICC, IF - ABIN4348737
Nogales-Gadea, Mormeneo, García-Consuegra, Rubio, Orozco, Arenas, Martín, Lucia, Gómez-Foix, Martí, Andreu: Expression of glycogen phosphorylase isoforms in cultured muscle from patients with McArdle's disease carrying the p.R771PfsX33 PYGM mutation. in PLoS ONE 2010
The in vivo consequences of disrupting the G(L)-phosphorylase a interaction, using a mouse model containing a Tyr284Phe substitution in the phosphorylase a-binding region of the hepatic glycogen (show GYS1 Antibodies)-associated protein phosphatase-1 (show PPP1CB Antibodies) protein, is reported.
Susceptibility to excessive liver glycogen (show GYS1 Antibodies) storage in patients with type 1 diabetes.
Deficiency of liver glycogen phosphorylase is predominantly the result of missense mutations affecting enzyme activity. There are no common mutations and the severity of clinical symptoms varies significantly.
4-alpha-glucanotransferase action of porcine liver GDE (show AGL Antibodies) on four 6(4)-O-alpha-maltooligosyl-pyridylamino(PA)-maltooctaoses, in the presence or absence of an acceptor, maltohexaose, was examined.
This gene encodes a homodimeric protein that catalyses the cleavage of alpha-1,4-glucosidic bonds to release glucose-1-phosphate from liver glycogen stores. This protein switches from inactive phosphorylase B to active phosphorylase A by phosphorylation of serine residue 15. Activity of this enzyme is further regulated by multiple allosteric effectors and hormonal controls. Humans have three glycogen phosphorylase genes that encode distinct isozymes that are primarily expressed in liver, brain and muscle, respectively. The liver isozyme serves the glycemic demands of the body in general while the brain and muscle isozymes supply just those tissues. In glycogen storage disease type VI, also known as Hers disease, mutations in liver glycogen phosphorylase inhibit the conversion of glycogen to glucose and results in moderate hypoglycemia, mild ketosis, growth retardation and hepatomegaly. Alternative splicing results in multiple transcript variants encoding different isoforms.
glycogen phosphorylase, liver form
, liver glycogen phosphorylase
, phosphorylase, glycogen; liver (Hers disease, glycogen storage disease type VI)
, glycogen storage disease type VI-related protein
, phosphorylase, glycogen; liver