Recombinant Human MCM2 Protein: Function & Research Guide

Recombinant Human MCM2 Protein is a key component of the minichromosome maintenance (MCM2–7) replicative helicase complex that licenses and unwinds DNA at eukaryotic replication origins, making it an essential research tool for studying DNA replication initiation, cell cycle regulation, and genome stability.

Protein Name

Recombinant Human MCM2 Protein

Gene Name

MCM2 (also known as BM28, CCNL1, CDCL1)

Protein Family

Minichromosome Maintenance (MCM) AAA+ ATPase family

Biological Function

Subunit of the MCM2–7 replicative helicase; essential for replication origin licensing and DNA unwinding

Expression System

Recombinant (refer to product datasheet for host system details)

Primary Applications

Biochemical assays, protein–protein interaction studies, antibody validation, cell cycle research

Related Product SKU

rp377544

What Is MCM2? Biological Background

MCM2 (Minichromosome Maintenance Protein 2) is an essential eukaryotic protein encoded by the MCM2 gene. It is a core subunit of the heterohexameric MCM2–7 complex, which serves as the principal replicative helicase in eukaryotes. This complex is loaded onto chromatin at replication origins during the G1 phase of the cell cycle as part of the pre-replication complex (pre-RC), a process known as replication licensing.

Upon S-phase entry, the MCM2–7 ring is activated by the kinases CDC7/DBF4 (DDK) and CDK2/Cyclin E (CDK), leading to recruitment of GINS and CDC45 to form the active CMG (CDC45–MCM2-7–GINS) helicase. This holoenzyme unwinds double-stranded DNA ahead of the replication fork, enabling DNA polymerases to synthesize new strands.

MCM2 is indispensable for genome duplication fidelity. Dysregulation or mutation of MCM2 has been linked to replication stress, genomic instability, and tumorigenesis, making it a subject of intense interest in cancer biology and cell cycle research.

Biochemical Properties of Recombinant Human MCM2 Protein

Recombinant Human MCM2 Protein is produced using recombinant expression technology to deliver a well-defined, research-grade protein suitable for a range of in vitro applications. Key biochemical features include:

• AAA+ ATPase Activity: MCM2 contains a conserved AAA+ (ATPases Associated with diverse cellular Activities) domain responsible for ATP binding and hydrolysis, which powers the mechanical unwinding of DNA duplex at replication forks.
• Zinc Finger Domain: The N-terminal region of MCM2 harbors a zinc finger motif that contributes to DNA binding and complex assembly.
• Protein–Protein Interaction Interfaces: MCM2 contains interfaces for interaction with other MCM subunits (MCM3–7), CDC45, GINS, and regulatory kinases such as DDK, enabling reconstitution of functional helicase sub-complexes in vitro.
• Post-Translational Regulation Sites: Human MCM2 is phosphorylated by DDK at Ser40 and Ser53 (sites may vary by literature), facilitating helicase activation and licensing control. Researchers should consult the specific product datasheet for the modification state of the recombinant form supplied.

Please refer to the Aladdin Scientific product datasheet for confirmed purity, molecular weight, formulation buffer, and storage conditions for SKU rp377544.

Research Applications

Recombinant Human MCM2 Protein supports a broad spectrum of research applications in DNA replication, cell cycle biology, and oncology:

1. Biochemical Helicase Assays: Used to reconstitute and characterize the ATPase and DNA-unwinding activities of the MCM complex in defined in vitro systems.
2. Protein–Protein Interaction Studies: Serves as bait or prey in pull-down, co-immunoprecipitation, and surface plasmon resonance (SPR) experiments to map interactions with MCM complex partners, replication factors, and kinase substrates.
3. Antibody Validation: Provides a well-defined antigen for validating specificity of anti-MCM2 antibodies in Western blot, ELISA, or immunofluorescence applications.
4. Structural Biology: Can be incorporated into cryo-EM or crystallographic studies aimed at resolving the architecture of the MCM2–7 ring or CMG helicase.
5. Drug Discovery Screening: Useful as a target protein in high-throughput screens for small molecules that inhibit MCM2 ATPase activity or disrupt MCM complex assembly, relevant to anti-cancer drug development.
6. Replication Stress and Genome Stability Research: Facilitates mechanistic studies of how MCM2 dysfunction contributes to replication fork collapse, DNA damage responses, and chromosomal instability.

Handling, Storage, and Quality Considerations

To maintain the activity and integrity of Recombinant Human MCM2 Protein, researchers should observe the following best-practice guidelines (confirm exact conditions on the product datasheet for SKU rp377544):

• Storage Temperature: Recombinant proteins are typically stored at −70 °C to −80 °C for long-term stability. Avoid repeated freeze–thaw cycles, which can cause aggregation and loss of activity.
• Aliquoting: Upon first thaw, prepare single-use aliquots to minimize freeze–thaw stress.
• Buffer Compatibility: Confirm the supplied formulation buffer before use in sensitive assays; buffer exchange may be required for certain downstream applications.
• Protein Concentration: Determine working concentration empirically for each assay type, as optimal concentrations vary with application and experimental conditions.
• Quality Control: Aladdin Scientific quality-tests recombinant proteins for purity (typically by SDS-PAGE) and biological activity. Refer to the Certificate of Analysis (CoA) provided with each lot for lot-specific data.

Note: All specific numerical values (purity percentage, exact molecular weight, endotoxin level) should be verified against the official product datasheet and CoA for SKU rp377544.

Frequently asked questions

What is the function of MCM2 in DNA replication?

MCM2 is a subunit of the MCM2–7 hexameric helicase complex, which is the primary replicative helicase in eukaryotic cells. It is loaded onto replication origins during G1 phase as part of the pre-replication complex (replication licensing) and, upon S-phase entry, unwinds double-stranded DNA at replication forks to allow DNA synthesis to proceed.

What applications is Recombinant Human MCM2 Protein suitable for?

Recombinant Human MCM2 Protein is suitable for a range of in vitro applications including biochemical ATPase and helicase activity assays, protein–protein interaction studies (pull-down, co-IP, SPR), antibody validation, structural biology studies (cryo-EM, crystallography), and drug-discovery screening targeting the DNA replication machinery. It is also used in research on replication stress and genome stability.

How should Recombinant Human MCM2 Protein be stored to maintain activity?

Recombinant proteins such as MCM2 are generally stored at −70 °C to −80 °C for long-term stability. Repeated freeze–thaw cycles should be avoided by preparing single-use aliquots upon first thaw. Always refer to the specific product datasheet and Certificate of Analysis for SKU rp377544 for confirmed storage recommendations.

Why is MCM2 relevant to cancer research?

MCM2 is frequently overexpressed in various human cancers, and its expression level has been explored as a proliferation biomarker. Dysregulation of MCM2–7 complex activity can lead to replication stress, fork stalling, and genomic instability—hallmarks of cancer progression. Recombinant MCM2 protein enables mechanistic studies of these processes and supports screening for anti-cancer compounds that target the replication helicase machinery.

References

1. Bochman ML, Schwacha A. The MCM2-7 complex has in vitro helicase activity. Molecular Cell. 2008;31(2):287-293. doi:10.1016/j.molcel.2008.05.020
2. Remus D, Diffley JF. Eukaryotic DNA replication control: lock and load, then fire. Current Opinion in Cell Biology. 2009;21(6):771-777. doi:10.1016/j.ceb.2009.08.002
3. Labib K. How do Cdc7 and cyclin-dependent kinases trigger the initiation of chromosome replication in eukaryotic cells? Genes & Development. 2010;24(12):1208-1219. doi:10.1101/gad.1933010
4. Gonzalez MA, Tachibana KE, Laskey RA, Coleman N. Control of DNA replication and its potential clinical exploitation. Nature Reviews Cancer. 2005;5(2):135-141. doi:10.1038/nrc1548

Products are supplied for research and development use only. Not for use in humans, animals, diagnosis, or therapy.