Anti-CMPK2 antibody produced in rabbit

Cytidine/uridine monophosphate kinase 2 (CMPK2) is expressed in mitochondria. The protein Cmpk2 is similar to thymidylate kinase than to cytosolic Cmpk1. Cmpk2 has thymidylate kinase domain and the C-terminal domain contains all the consensus motifs: P-loop (ATP/ GTP binding motif A), LID (domain in lipase) domain, adenine-base binding loop, catalytic site, and potential substrate binding site. In human chromosome, the gene is localized on 2p25.2.

Cmpk2 utilizes ATP (adenosine triphosphate) as phosphate donor to phosphorylate dUMP (deoxyuridine monophosphate), dCMP (deoxycytidine monophosphate), CMP (cytosine monophosphate), and UMP (uridine monophosphate). The order of substrate specificity for Cmpk2 is UMP, the highest, followed by dCMP, CMP and UMP. Cmpk2 also phosphorylates monophosphate nucleoside analogs ddC (zalcitabine), dFdC (gemcitabine), araC (vidarabine), BVDU (brivudine), and FdUrd (fluorodeoxyuridine). Cmpk2 expression is found in leukemic cells like chronic myelogenous leukemia K-562 and lymphoblastic leukemia MOLT-4, implicates its pathophysiology. The catalytic activity of Cmpk2 is similar to human adenylate kinase 9.

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The action of this antibody can be blocked using blocking peptide SBP3500816.

Supplied at 1 mg/mL in PBS with 0.02% sodium azide.

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