UMP-CMP kinase/CMPK1 Protein, Human (sf9, His)

The UMP-CMP kinase (CMPK1) protein utilizes ATP as a phosphate donor to catalyze the phosphorylation of pyrimidine nucleoside monophosphate, thereby playing a key role in cellular processes. This enzymatic activity is integral to the de novo biosynthesis of pyrimidine nucleotides and contributes to the synthesis of important cellular building blocks. UMP-CMP kinase/CMPK1 Protein, Human (sf9, His) is the recombinant human-derived UMP-CMP kinase/CMPK1 protein, expressed by Sf9 insect cells , with N-His labeled tag. The total length of UMP-CMP kinase/CMPK1 Protein, Human (sf9, His) is 196 a.a., with molecular weight of ~27 kDa.

The UMP-CMP kinase, also known as CMPK1, is a crucial enzyme that catalyzes the phosphorylation of pyrimidine nucleoside monophosphates utilizing ATP as a phosphate donor. This enzymatic activity holds significance in de novo pyrimidine nucleotide biosynthesis, representing a key step in the synthesis of essential cellular components. CMPK1 exhibits a preference for uridine monophosphate (UMP) and cytidine monophosphate (CMP) as phosphate acceptors in this process. Additionally, CMPK1 displays broad nucleoside diphosphate kinase activity, emphasizing its versatility in catalyzing the transfer of phosphate groups between different nucleoside diphosphates. The multifaceted functions of CMPK1 underscore its pivotal role in cellular nucleotide metabolism and its potential implications for various cellular processes.

Human

Sf9 insect cells

N-His

P30085 (M1-G196)

51727  [NCBI]

Approximately 27 kDa

Greater than 95% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.