SRP6121
AK1 human
recombinant, expressed in E. coli, ≥95% (SDS-PAGE)
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biological source
human
recombinant
expressed in E. coli
Assay
≥95% (SDS-PAGE)
form
liquid
mol wt
23.7 kDa (214 aa, 1-194 aa + NT His Tag)
purified by
chromatography
packaging
pkg of 100 μg
technique(s)
activity assay: suitable
NCBI accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... AK1(203)
General description
Research area: Cancer
The gene AK1 (adenylate kinase isoenzyme 1) is mapped to human chromosome 9 on the location 9q34.11. It belongs to the nucleotide monophosphate kinase family. The AK1 protein is found in the cytosol of skeletal muscle, brain, and heart.The structure of AKs (adenylate kinases) comprises of three functional domains: the catalytic and oligomerization regulatory enzyme (CORE) domain, the ligand interaction domain (LID) domain, and the substrate binding site. In human tissues, a total of nine distinct isoenzymes of adenylate kinase are known, namely AK1 to AK9. Recombinant human AK1 protein, fused to His-tag at N-terminus, was expressed in Escherichia coli and purified by using conventional chromatography.
The gene AK1 (adenylate kinase isoenzyme 1) is mapped to human chromosome 9 on the location 9q34.11. It belongs to the nucleotide monophosphate kinase family. The AK1 protein is found in the cytosol of skeletal muscle, brain, and heart.The structure of AKs (adenylate kinases) comprises of three functional domains: the catalytic and oligomerization regulatory enzyme (CORE) domain, the ligand interaction domain (LID) domain, and the substrate binding site. In human tissues, a total of nine distinct isoenzymes of adenylate kinase are known, namely AK1 to AK9. Recombinant human AK1 protein, fused to His-tag at N-terminus, was expressed in Escherichia coli and purified by using conventional chromatography.
Biochem/physiol Actions
AK1 (adenylate kinase isoenzyme 1) is an enzyme involved in regulating the adenine nucleotide composition within a cell by catalyzing the reversible transfer of the terminal phosphate group between ATP and AMP. Low levels of AK1 cause imbalance in adenine nucleotide pools. Defects in AK1 are the cause of a form of hemolytic anemia. This gene is also upregulated in the brains of AD (Alzheimer′s disease) patients and downregulated in Duchenne muscular dystrophy. It is responsible for abnormal phosphorylation of tau via AMPK-GSK3β (AMP-activated protein kinase-glycogen synthase kinase-3β), thereby causing tau-mediated neurodegeneration.AK1 plays an important role in the regulation of cancer cell metabolism, metabolic signaling, as well as cell migration and invasion. It also aids in the progression of malignant transformation.
Physical form
1 mg/mL solution in 20 mM Tris-HCl buffer (pH 7.5) containing 10% glycerol.
Preparation Note
Centrifuge the vial prior to opening.
Other Notes
MGSSHHHHHH SSGLVPRGSH MEEKLKKTKI IFVVGGPGSG KGTQCEKIVQ KYGYTHLSTG DLLRSEVSSG SARGKKLSEI MEKGQLVPLE TVLDMLRDAM VAKVNTSKGF LIDGYPREVQ QGEEFERRIG QPTLLLYVDA GPETMTQRLL KRGETSGRVD DNEETIKKRL ETYYKATEPV IAFYEKRGIV RKVNAEGSVD SVFSQVCTHL DALK
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
常规特殊物品
Certificates of Analysis (COA)
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Find documentation for the products that you have recently purchased in the Document Library.
Neuropathogenic role of adenylate kinase-1 in A?-mediated tau phosphorylation via AMPK and GSK3?.
Park H, et al.
Human Molecular Genetics, 21, 2725-2725 (2012)
Defective metabolic signaling in adenylate kinase AK1 gene knock-out hearts compromises post-ischemic coronary reflow.
Dzeja PP, et al.
The Journal of Biological Chemistry, 282, 31366-31366 (2007)
Adenylate Kinase: A Ubiquitous Enzyme Correlated with Medical Conditions
Mihaela Ileana Ionescu
The Protein Journal, 38(2), 120-133 (2019)
Metabolism of circulating ADP in the bloodstream is mediated via integrated actions of soluble adenylate kinase-1 and NTPDase1/CD39 activities.
Yegutkin GG, et al.
Faseb Journal, 26, 3875-3875 (2012)
The many isoforms of human adenylate kinases
Panayiotou C, et al.
The International Journal of Biochemistry & Cell Biology, 49, 75-83 (2014)
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