Rabbit Polyclonal GYG1 Antibody

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     All lanes : Anti-GYG1 Antibody (C-Term) at 1:2000 dilution Lane 1: Hela whole cell lysate Lane 2: HepG2 whole cell lysate Lane 3: Mouse heart lysate Lane 4: Mouse skeletal muscle lysate Lane 5: Rat heart lysate Lysates/proteins at 20 µg per lane. Secondary Goat Anti-Rabbit IgG,  (H+L), Peroxidase conjugated at 1/10000 dilution. Predicted band size : 39 kDa Blocking/Dilution buffer: 5% NFDM/TBST.    

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     Overlay histogram showing HepG2 cells stained with P34462(green line).  The cells were fixed with 2% paraformaldehyde (10 min) and then permeabilized with 90% methanol for 10 min.  The cells were then icubated in 2% bovine serum albumin to block non-specific protein-protein interactions followed by the antibody (P34462,  1:25 dilution) for 60 min at 37ºC.  The secondary antibody used was Goat-Anti-Rabbit IgG, DyLight® 488 Conjugated Highly Cross-Adsorbed(1583138) at 1/200 dilution for 40 min at 37ºC.  Isotype control antibody (blue line) was rabbit IgG1 (1μg/1x10^6 cells) used under the same conditions.  Acquisition of >10, 000 events was performed.    

The GYG1 antibody is a crucial tool in studying glycogen metabolism and associated disorders. Glycogenin-1. encoded by the GYG1 gene, is a self-glucosylating enzyme essential for initiating glycogen synthesis by forming oligosaccharide primers that serve as substrates for glycogen synthase. Mutations in GYG1 are linked to glycogen storage disease type XV (GSD XV), a rare disorder characterized by muscle weakness, cardiomyopathy, and abnormal glycogen accumulation.

GYG1 antibodies are widely used to detect glycogenin-1 expression in tissues like skeletal muscle, heart, and liver, where glycogen metabolism is physiologically significant. These antibodies enable researchers to investigate protein localization, expression levels, and post-translational modifications through techniques such as Western blotting, immunohistochemistry, and immunofluorescence.

In research, GYG1 antibodies have helped clarify mechanisms underlying glycogen synthesis regulation and pathologies. For example, studies using these antibodies revealed reduced or dysfunctional glycogenin-1 in GSD XV patients and animal models, highlighting its role in glycogen chain initiation. Additionally, they aid in distinguishing primary glycogenin deficiencies from secondary disruptions in glycogen metabolism caused by other enzymatic defects.

Most commercially available GYG1 antibodies are raised in rabbits or mice against specific epitopes of human glycogenin-1. with validation in multiple species. Their specificity and reliability make them indispensable for both basic research and diagnostic applications related to glycogen-associated diseases.