Anti-Zebrafish Mcm4

0.5mg/ml if reconstituted with 0.2ml sterile DI water. Minichromosome maintenance complex component 4 (MCM4) is a core part of the MCM2-7 helicase complex, which is essential for the initiation and elongation phases of eukaryotic DNA replication. The MCM complex functions as the replicative helicase, unwinding double-stranded DNA at replication forks to enable the synthesis of new DNA strands.In zebrafish (Danio rerio), mcm4 is a highly conserved gene with critical roles during early embryogenesis and cell proliferation. Expression of mcm4 is enriched in rapidly dividing tissues and during periods of intense developmental activity, reflecting its importance in genome stability and cell cycle progression.Zebrafish models deficient in Mcm4 function have been used to study mechanisms of DNA replication stress, genomic instability, and the cellular response to DNA damage. Additionally, because of its conservation and similarity to human MCM4, zebrafish serves as a useful system for modeling MCM-related human disorders, such as Meier-Gorlin syndrome and cancer predisposition syndromes linked to replication licensing defects.The zebrafish MCM4 protein is a valuable tool for investigating DNA replication dynamics, cell cycle regulation, and the molecular basis of developmental and proliferative diseases. Protein function: Acts as a component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. [The UniProt Consortium]