Anti-MCM7 antibody, rabbit polyclonal
Product code70-120Size

100 µgStorage-20℃

Concentration

1.0 mg/ml

Buffer

PBS- with 50% glycerol

PurityPurified IgG fraction with protein A from rabbit antiserum

ImmunogenPurified His6-tagged human MCM7 protein encompassing 562 -719 aminoacids.

IsotypeRabbit IgG

Reactivity

human mouse, rat and hamster.

Special notes

N/A

Application

1. Western blotting (1/1,000~1/5,000 dilution)

Not tested in other species.

2. Immunoprecipitation (assay dependent)
3. Chromatin Immuno-Precipitation
4. Immunofluorescence staining (1/200~1/1,000 dilution)
5. Flow cytometry (assay dependent
Background

MCM7 (human; 718 aa, 80 kDa) acts as component of the MCM2-7 complex(MCM complex) which is the putative replicative helicase essential for 'once percell cycle' DNA replication initiation and elongation in eukaryotic cells. 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 theWalker A box of the adjacent subunit. The six ATPase active sites, however, arelikely to contribute differentially to the complex helicase activity. Required forS-phase checkpoint activation upon UV-induced damage.
Key words: DNA replication licensing factor, MCM complex, DNA replicationinitiation, G1/S transition, DNA damage response, DNA helicase.

Data Link

UniProtKB P33993 MCM7_HUMAN

Please note: All products are FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC
PROCEDURES. NOT FOR MILITARY USE.

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Data Images: 70-120 Anti-MCM7 antibody, rabbit polyclonal

Fig.1 Identification of MCM7 protein in whole cell extracts of human cells by western blotting using
anti-MCM7 antibody
Lane1. SiHa cells
Lane2. C33A cells
Lane.3 WI38 cells
All cell lines are cervical cancer derived. Samples are obtained from approximately 108 cells

Fig. 2 Identification of MCM7 protein in whole cell extracts of human and mouse cells by western
blotting using anti-MCM7 antibody.
Lane 1. Size marker proteins in kDa.
Lane 2. Extract of HeLa cells untreated (-).
Lane 3. Extract of HeLa cells treated with 100 nM adriamycin for 24 hr (+)
Lane 4. Extract of NIH3T3 (mouse) cells.
Anti-MCM7 antibody was used at 1/1,000 dilution.
* Indicates the band of MCM7 protein
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Fig. 3. Immunoprecipitation of MCM7 protein from crude extract ofhuman fibroblast cell line WI38 by using anti-MCM7 antibody.
Lane 1; Immunoprecipitation with pre-immune serum
Lane 2; Immnoprecipitation with anti-MCM7 antiserum.
Cells were labeled with S35 methionine and MCM7 was immunoprecipitated with the anti-MCM7
antibody followed by SDS-PAGE and autoradiography.

Fig. 4. Immunofluorecence staining and confocal microscopic analysis of MCM7 in G1 phase HeLa cellnucleus by using anti-MCM7 antibody after treatment with protein cross-linking reagent, DSP andchromatin extraction. The processed cells were fixed with formaldehyde before staining.
References: This antibody was described in Ref.1 and used in the following publications.
1. Fujita M et al. hCDC47, a human member of the MCM family. Dissociation of the nucleus-boundform during S phase. J Biol Chem. (1996)271:4349-54. PMID 8626784 . WB, IP, IF
2. Fujita M. et al. In vivo interaction of human MCM heterohexameric complexes with chromatin.
Possible involvement of ATP. J Biol Chem. (1997)272:10928-35. PMID 9099751. WB, IP
3. Fujita M. et al. (2002) Nuclear organization of DNA replication initiation proteins in mammaliancells. J Biol Chem. 277:10354-61. PMID 11779870. WB, IP, IF.
4. Sugimoto N. et al. Chromatin remodeler sucrose nonfermenting 2 homolog (SNF2H) is recruited
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onto DNA replication origins through interaction with Cdc10 protein-dependent transcript 1(Cdt1) and promotes pre-replication complex formation.
Nucleic Acids Res. 2015 Jul 13;43(12):5898-911. PMID: 25990725 WB, IP, ChIP, Flow Cyt: human
5. Sugimoto N. et al. Cdt1-binding protein GRWD1 is a novel histone-binding protein that facilitates
MCM loading through its influence on chromatin architecture. Nucleic Acids Res. 2015 Jul
13;43(12):5898-911. PMID:25990725. WB, ChIP: human
6. Sugimoto N. et al. Genome-wide analysis of the spatiotemporal regulation of firing and dormant
replication origins in human cells. Nucleic Acids Res. 2018 Jul 27;46(13):6683-6696. PMID:29893900. ChIP: human

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