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Research area: Cancer
The gene AK1 (adenylate kinase isoenzyme 1) is mapped to human chromosome 9 on the location 9q34.11.[1] It belongs to the nucleotide monophosphate kinase family.[2] The AK1 protein is found in the cytosol of skeletal muscle, brain, and heart.[3]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. [4] 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.[1] It belongs to the nucleotide monophosphate kinase family.[2] The AK1 protein is found in the cytosol of skeletal muscle, brain, and heart.[3]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. [4] Recombinant human AK1 protein, fused to His-tag at N-terminus, was expressed in Escherichia coli and purified by using conventional chromatography.
生物化学的/生理学的作用
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.[3] Low levels of AK1 cause imbalance in adenine nucleotide pools.[5] Defects in AK1 are the cause of a form of hemolytic anemia.[6] [1] This gene is also upregulated in the brains of AD (Alzheimer′s disease) patients and downregulated in Duchenne muscular dystrophy.[1] It is responsible for abnormal phosphorylation of tau via AMPK-GSK3β (AMP-activated protein kinase-glycogen synthase kinase-3β), thereby causing tau-mediated neurodegeneration.[7]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.[8]
物理的形状
1 mg/mL solution in 20 mM Tris-HCl buffer (pH 7.5) containing 10% glycerol.
調製ノート
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その他情報
MGSSHHHHHH SSGLVPRGSH MEEKLKKTKI IFVVGGPGSG KGTQCEKIVQ KYGYTHLSTG DLLRSEVSSG SARGKKLSEI MEKGQLVPLE TVLDMLRDAM VAKVNTSKGF LIDGYPREVQ QGEEFERRIG QPTLLLYVDA GPETMTQRLL KRGETSGRVD DNEETIKKRL ETYYKATEPV IAFYEKRGIV RKVNAEGSVD SVFSQVCTHL DALK
保管分類コード
11 - Combustible Solids
WGK
WGK 3
引火点(°F)
Not applicable
引火点(℃)
Not applicable
適用法令
試験研究用途を考慮した関連法令を主に挙げております。化学物質以外については、一部の情報のみ提供しています。 製品を安全かつ合法的に使用することは、使用者の義務です。最新情報により修正される場合があります。WEBの反映には時間を要することがあるため、適宜SDSをご参照ください。
Jan Code
SRP6121-100UG:
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試験成績書(COA)
Lot/Batch Number
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)
The many isoforms of human adenylate kinases
Panayiotou C, et al.
The International Journal of Biochemistry & Cell Biology, 49, 75-83 (2014)
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)
Adenylate Kinase: A Ubiquitous Enzyme Correlated with Medical Conditions
Mihaela Ileana Ionescu
The Protein Journal, 38(2), 120-133 (2019)
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