AK, ADK, Adenosine Kinase, Adenosine 5-Phosphotransferase.
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
ADK produced in E.Coli is a single, non-glycosylated polypeptide chain containing 384 amino acids (1-361a.a.) and having a molecular mass of 42.5kDa.
ADK is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Adenosine Kinase is a key enzyme found in high concentrations within mammalian tissues. It plays a critical role in regulating both intra- and extracellular levels of adenosine and adenine nucleotides by catalyzing the transfer of a phosphate group from ATP to adenosine. Due to adenosine's significant impact on various systems like the cardiovascular, nervous, respiratory, and immune systems, inhibitors of Adenosine Kinase are of significant pharmacological interest. These inhibitors increase intravascular adenosine concentrations and demonstrate anti-inflammatory properties.
This ADK protein is produced in E. coli and is a single, non-glycosylated polypeptide chain. It consists of 384 amino acids (with the first 361 amino acids being the active protein) and has a molecular weight of 42.5kDa. A 23 amino acid His-tag is fused to the N-terminus to facilitate purification, which is carried out using proprietary chromatographic methods.
The ADK protein is supplied in a solution at a concentration of 1mg/ml. The solution contains the following components: 20% glycerol, 20mM Tris-HCl buffer (pH 8.0), 1mM EDTA, and 50mM NaCl.
The specific activity of this ADK protein is greater than 100 pmol/min/μg. Specific activity is defined as the amount of enzyme required to convert 1.0 picomole of adenosine to AMP per minute at a pH of 7.5 and a temperature of 37°C in a coupled enzyme assay system utilizing pyruvate kinase (PK) and lactate dehydrogenase (LDH).
AK, ADK, Adenosine Kinase, Adenosine 5-Phosphotransferase.
MGSSHHHHHH SSGLVPRGSH MGSMAAADEP KPKKLKVEAP QALSENVLFG MGNPLLDISA VVDKDFLDKY SLKPNDQILA EDKHKELFDE LVKKFKVEYH AGGSTQNSMK VAQWLIQEPH KAATFFGCIG IDKFGEILKR KAADAHVDAH YYEQNEQPTG TCAACITGGN RSLVANLAAA NCYKKEKHLD LERNWVLVEK ARVYYIAGFF LTVSPESVLK VARYAAENNR VFTLNLSAPF ISQFFKEALM DVMPYVDILF GNETEAATFA REQGFETKDI KEIAKKAQAL PKVNSKRQRT VIFTQGRDDT IVAAENDVTA FPVLDQNQEE IIDTNGAGDA FVGGFLSQLV SDKPLTECIR AGHYAASVII RRTGCTFPEK PDFH.
Adenosine kinase is widely expressed in various tissues, with elevated levels in the placenta, liver, muscle, and kidney . The enzyme’s primary function is to phosphorylate adenosine, a process that is vital for maintaining cellular energy balance and nucleotide metabolism . The recombinant form of mouse adenosine kinase is typically produced using E. coli expression systems, which allows for the generation of high-purity enzyme preparations .
Adenosine itself is a primordial metabolite and regulator of numerous biochemical reactions related to metabolism and genetics . By converting adenosine to AMP, ADK helps regulate the availability of adenosine for various signaling pathways. This regulation is critical because adenosine can activate specific signaling pathways by binding to adenosine receptors .