Serum glucose homeostasis is tightly controlled by a balance of glucose absorption via the gut, production primarily by the liver and utilization by both insulin-sentive and insulin insensitive transport of glucose in to various tissues. Such precise control of serum glucose levels involves hormonal and neuronal interactions in various types of cells. The loss of such homeostatic control of glucose is a diagnostic of diabetes. Type 2 diabetes mellitus is a leading cause of kidney failure, blindness and lower limb amputations and afflicts more than 170 million worldwide.
Recently, it has been shown that variation in the gene of a protein Glucose 6 phosphatase catalytic domain 2 (G6PC2) in pancreas may explain why different people have different levels of fasting glucose levels, a factor that affects disease risk (1). Molecular cloning of G6PC2 identified two splice variants that differ by the presence and absence of Exxon 4 in BALB/C and ob/ob mice and in insulinoma tissue (2). The longer cDNA including exon 4 has approximately 50% homology with glucose-6-phosphatase catalytic subunit (G6pc) across a variety of species including humans and is membrane bound in the endoplasmic reticulum. The significant homology between G6PC and G6PC2 has been observed across species and its membrane bound in the endoplasmic reticulum fraction. The shorter from of G6PC2 species variant was found in human pancreas and is located in intron 3 just 26 bp proximal to exon 4. The longer variant G6PC hydrolyzes glucose-6-phosphate to glucose and a phosphate group, however, despite sequence similarities the G6PC2 has little or no hydrolase activity (3). Slightly higher G6PC2 associated hydrolase activity is reported a cell over expressing this gene. The streptozotocin treated mice exhibit 3-fold higher expression ogG6PC2 expression suggesting glucose cycling in these mice may be an indicator of G6PC2 activity. Variation in G6PC2 may increase glucose cycling in β cells, resulting in altered generation of ATP, which would have implications for insulin secretion. In addition, G6PC2-induced alterations in β cell glucose metabolism would also have downstream effects on phosphoinositide 3-kinase activity, which regulates pancreas duodenum homeobox-1 (PDX1) binding to the insulin gene and subsequent insulin gene transcription (4).
The G6PC2-selective antibody was generated against a peptide from near N-terminus of the protein corresponding to amino acids 83-105 of the G6PC2 a 154 amino acid protein. The affinity purified mono epitope-specific rabbit polyclonal antibody strongly labels a 48kDa and a 20 kDa band in G6PC2 western blot control samples. The G6PC2 rabbit mono-epitope specific polyclonal antibodies are affinity purified on immobilized antigen affinity matrix, the affinity purified antibodies are also available in FITC and Biotin-conjugated form for use in IHC and cells labeling experiments. Limited quantities of antigenic blocking peptide and western blot positive controls samples are also available. FabGennix has a wide range of antibodies to kinases and phosphatase, for a complete listing please visit www. FabGennix.com
For research use only, not for diagnostic or therapeutic use.
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