- CITATIONS: 1
|Application ||WB, IHC-P, E|
|Calculated MW||102486 Da|
|Antigen Region||78-108 aa|
|Other Names||Hexokinase-1, Brain form hexokinase, Hexokinase type I, HK I, HK1|
|Target/Specificity||This HK1 (Hexokinase) antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 78-108 amino acids from the N-terminal region of human HK1 (Hexokinase).|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|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||HK1 (Hexokinase) Antibody (N-term) 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||Isoform 2 is erythrocyte specific. Isoform 3 and isoform 4 are testis-specific|
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. The hexokinase 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 the hexokinase 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. HK1 encodes the ubiquitously expressed isoform. Its 5' end includes an exon which is unique to this transcript and which encodes a distinct N-terminus that contains the porin binding domain (PBD). The porin binding domain mediates 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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