Recombinant Human MCM7/PRL protein (denatured)
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Recombinant Human MCM7/PRL protein (denatured) is a Human Fragment protein, in the 1 to 414 aa range, expressed in Escherichia coli, with >85%, suitable for SDS-PAGE.
View Alternative Names
CDC47, MCM2, MCM7, DNA replication licensing factor MCM7, CDC47 homolog, P1.1-MCM3
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human MCM7/PRL protein (denatured) (AB177663)
15% SDS-PAGE analysis of ab177663 (3 μg)
Reactivity data
Product details
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
MCM7 is involved in maintaining genomic stability and ensuring accurate DNA replication. As part of the larger MCM2-7 hexameric complex it collaborates with other members to form the core component of the pre-replicative complex (pre-RC). By loading onto replication origins MCM7 helps license the DNA for duplication. This function contributes to cell cycle progression particularly the S phase where DNA synthesis occurs.
Pathways
MCM7 plays an important role in DNA replication-related signaling pathways. It functions within the cell cycle and DNA replication pathways interacting closely with other essential proteins like CDC45 and GINS complex. These partnerships facilitate the transition from the G1 to the S phase triggering the replication machinery's activation and ensuring cell division processes continue smoothly.
Specifications
Form
Liquid
General info
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 (PubMed : 25661590, PubMed : 32453425, PubMed : 34694004, PubMed : 34700328, PubMed : 35585232, PubMed : 9305914). 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 (PubMed : 32453425). Required for S-phase checkpoint activation upon UV-induced damage.
Sequence similarities
Belongs to the MCM family.
Post-translational modifications
O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner.. Ubiquitinated by ECS(LRR1) E3 ubiquitin-protein ligase complex when forks converge following formation of DNA interstrand cross-links. During mitosis, ubiquitinated by TRAIP when forks converge following formation of DNA interstrand cross-links (By similarity). Short ubiquitin chains on MCM7 promote recruitment of DNA glycosylase NEIL3 (By similarity). If the interstrand cross-link cannot be cleaved by NEIL3, the ubiquitin chains continue to grow on MCM7, promoting the unloading of the CMG helicase complex by the VCP/p97 ATPase (By similarity).
Subcellular localisation
Nucleus
Target data
Product promise
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