|Other Names||Hexokinase-1, Brain form hexokinase, Hexokinase type I, HK I, HK1|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP8141c was selected from the center region of human HK1-R468. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|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||Isoform 2 is erythrocyte specific. Isoform 3 and isoform 4 are testis-specific|
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Provided below are standard protocols that you may find useful for product applications.
Hexokinases phosphorylate glucose to produce glucose-6-phosphate, thus committing glucose to the glycolytic pathway. This gene encodes a ubiquitous form of hexokinase which localizes to the outer membrane of mitochondria. Mutations in this gene have been associated with hemolytic anemia due to hexokinase deficiency. Alternative splicing of this gene results in five transcript variants which encode different isoforms, some of which are tissue-specific. Each isoform has a distinct N-terminus; the remainder of the protein is identical among all the isoforms. A sixth transcript variant has been described, but due to the presence of several stop codons, it is not thought to encode a protein. Transcript Variant: Variant 4 (HKI-tb) has four testis-specific exons in the 5' end, one of which includes an additional 54 nt fragment unique to variants 4 and 5. Both variants 3 and 4 encode isoform HKI-ta/tb, which has a unique N-terminus. Isoform HKI-ta/tb lacks the porin binding domain (PBD) required for association with the mitochondrial membrane.
van Wijk, R., et al., Blood 101(1):345-347 (2003).Murakami, K., et al., Acta Haematol. 108(4):204-209 (2002).Murakami, K., et al., Mol. Genet. Metab. 67(2):118-130 (1999).Aleshin, A.E., et al., Structure 6(1):39-50 (1998).Ruzzo, A., et al., Blood 91(1):363-364 (1998).
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