Anti-STBD1 antibody

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

STBD1 also known as Starch Binding Domain 1 functions as a glycogen-binding protein with a molecular weight of approximately 42 kDa. This protein plays an important role in glycogen metabolism by facilitating the proper organization of glycogen granules within cells. STBD1 shows expression in a wide range of tissues with particularly high levels detected in liver and muscle tissues. Its expression pattern suggests its involvement in energy storage and utilization processes.

Biological function summary

This protein contributes significantly to cellular energy management. STBD1 interacts with glycogen likely assisting in its recognition and binding which is necessary for glycogen's structural integrity and function. It is not known to be a part of any large complex but works closely with enzymes that break down glycogen into glucose. By maintaining glycogen's readiness for breakdown STBD1 supports the cell’s ability to rapidly mobilize energy under conditions of necessity.

Pathways

This protein aids the glycogen homeostasis and glucose metabolism pathways. It functions alongside enzymes such as glycogen phosphorylase and glycogen synthase both of which play essential roles in glycogen turnover. By safeguarding glycogen’s integrity and availability STBD1 indirectly influences the efficiency of these pathways which are important for maintaining blood glucose levels and overall energy balance in the body.

STBD1 links to metabolic conditions such as diabetes and glycogen storage diseases. In diabetes impaired glycogen metabolism can contribute to poor glucose regulation with STBD1 potentially affecting glycogen availability. Altered STBD1 expression or function might also participate in glycogen storage diseases where abnormal glycogen accumulation occurs disrupting normal cellular functions. STBD1's connection with proteins like glycogen synthase highlights its potential impact in these disorders suggesting it as a point of interest for therapeutic exploration.