|Other Names||Glucose-6-phosphatase 2, G-6-Pase 2, G6Pase 2, Islet-specific glucose-6-phosphatase catalytic subunit-related protein, G6PC2, IGRP|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP8684a was selected from the N-term region of human G6PC2. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||May hydrolyze glucose-6-phosphate to glucose in the endoplasmic reticulum. May be responsible for glucose production through glycogenolysis and gluconeogenesis (By similarity).|
|Cellular Location||Endoplasmic reticulum membrane; Multi-pass membrane protein|
|Tissue Location||Specifically expressed in pancreas and also detected to a lower extent in testis. Expressed by most islet cells in the pancreas (at protein level)|
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Provided below are standard protocols that you may find useful for product applications.
G6PC2 may hydrolyze glucose-6-phosphate to glucose in the endoplasmic reticulum. It may be responsible for glucose production through glycogenolysis and gluconeogenesis. G6PC2 is an enzyme belonging to the glucose-6-phosphatase catalytic subunit family. These enzymes are part of a multicomponent integral membrane system that catalyzes the hydrolysis of glucose-6-phosphate, the terminal step in gluconeogenic and glycogenolytic pathways, allowing the release of glucose into the bloodstream. The family member is found in pancreatic islets and does not exhibit phosphohydrolase activity, but it is a major target of cell-mediated autoimmunity in diabetes.
Lieberman,S.M., et.al., Proc. Natl. Acad. Sci. U.S.A. 100 (14), 8384-8388 (2003)Shieh,J.J., et.al., FEBS Lett. 562 (1-3), 160-164 (2004)
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