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Merck

SRP6121

Sigma-Aldrich

AK1 human

recombinant, expressed in E. coli, ≥95% (SDS-PAGE)

Sinónimos:

no change, ATP-AMP phophotransferase, ATP-AMP transphosphorylase 1, Adenylate kinase isoenzyme 1, Adenylate monophosphate kinase, Myokinase

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About This Item

Comisión internacional de enzimas:
Código UNSPSC:
12352200
NACRES:
NA.32

origen biológico

human

recombinante

expressed in E. coli

Ensayo

≥95% (SDS-PAGE)

Formulario

liquid

mol peso

23.7 kDa (214 aa, 1-194 aa + NT His Tag)

purificado por

chromatography

envase

pkg of 100 μg

técnicas

activity assay: suitable

Nº de acceso NCBI

Condiciones de envío

dry ice

temp. de almacenamiento

−70°C

Información sobre el gen

human ... AK1(203)

Descripción general

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.

Acciones bioquímicas o fisiológicas

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]

Forma física

1 mg/mL solution in 20 mM Tris-HCl buffer (pH 7.5) containing 10% glycerol.

Nota de preparación

Centrifuge the vial prior to opening.

Otras notas

MGSSHHHHHH SSGLVPRGSH MEEKLKKTKI IFVVGGPGSG KGTQCEKIVQ KYGYTHLSTG DLLRSEVSSG SARGKKLSEI MEKGQLVPLE TVLDMLRDAM VAKVNTSKGF LIDGYPREVQ QGEEFERRIG QPTLLLYVDA GPETMTQRLL KRGETSGRVD DNEETIKKRL ETYYKATEPV IAFYEKRGIV RKVNAEGSVD SVFSQVCTHL DALK

Código de clase de almacenamiento

11 - Combustible Solids

Clase de riesgo para el agua (WGK)

WGK 3

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable


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Visite la Librería de documentos

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)
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)
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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