HK2 (Hexokinase II) Antibody (Center)
Purified Rabbit Polyclonal Antibody (Pab)
|Application ||IHC-P, WB, E|
|Calculated MW||102380 Da|
|Antigen Region||453-483 aa|
|Other Names||Hexokinase-2, Hexokinase type II, HK II, Muscle form hexokinase, HK2|
|Target/Specificity||This HK2 (Hexokinase II) antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 453-483 amino acids from the Central region of human HK2 (Hexokinase II).|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||HK2 (Hexokinase II) Antibody (Center) is for research use only and 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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