|Other Names||Hexokinase-2, Hexokinase type II, HK II, Muscle form hexokinase, HK2|
|Target/Specificity||The synthetic peptide sequence is selected from aa 416~431 of human HK2.|
|Format||The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized 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.|
|Cellular Location||Mitochondrion outer membrane. Note=Its hydrophobic N-terminal sequence may be involved in membrane binding.|
|Tissue Location||Predominant hexokinase isozyme expressed in insulin-responsive tissues such as skeletal muscle|
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Provided below are standard protocols that you may find useful for product applications.
In vertebrates there are four major glucose-phosphorylating isoenzymes, designated hexokinase I, II, III, and IV. Hexokinase is an allosteric enzyme inhibited by its product GLC-6-P. Hexokinase activity is involved in the first step in several metabolic pathways. HK3 is bound to the outer mitochondrial membrane. Its hydrophobic N-terminal sequence may be involved in membrane bindng. It is the predominant hexokinase isozyme expressed in insuline-responsive tissues such as skeletal muscle. The N- and C-terminal halves of this hexokinase show extensive sequence similarity to each other. The catalytic activity is associated with the C-terminus while regulatory function is associated wiht the N-terminus. Although found in NIDDM patients, genetic variations of HK2 do not contribute to the disease.
Lehto, M., et al., Diabetologia 38(12):1466-1474 (1995).Vidal-Puig, A., et al., Diabetes 44(3):340-346 (1995).Laakso, M., et al., Diabetes 44(3):330-334 (1995).Echwald, S.M., et al., Diabetes 44(3):347-353 (1995).Shinohara, Y., et al., Cancer Lett. 82(1):27-32 (1994).
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