MCM4 Antibody
Purified Rabbit Polyclonal Antibody (Pab)
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Application ![]()
| WB, IHC-P |
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Primary Accession | P33991 |
Reactivity | Human |
Host | Rabbit |
Clonality | Polyclonal |
Calculated MW | 96558 Da |
Gene ID | 4173 |
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Other Names | DNA replication licensing factor MCM4, CDC21 homolog, P1-CDC21, MCM4, CDC21 |
Dilution | WB~~1:1000 IHC-P~~N/A |
Format | 0.01M PBS, pH 7.2, 0.09% (W/V) Sodium azide, Glycerol 50% |
Storage | Store at -20 °C.Stable for 12 months from date of receipt |
Name | MCM4 (HGNC:6947) |
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Synonyms | CDC21 |
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:16899510, 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:16899510, PubMed:25661590, PubMed:32453425, PubMed:9305914). |
Cellular Location | Nucleus. Chromosome. Note=Associated with chromatin before the formation of nuclei and detaches from it as DNA replication progresses. |
For Research Use Only. Not For Use In Diagnostic Procedures.
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell 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 the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity.
REFERENCES
Musahl C.,et al.Eur. J. Biochem. 230:1096-1101(1995).
Connelly M.A.,et al.Genomics 47:71-83(1998).
Ladenburger E.M.,et al.Cytogenet. Cell Genet. 77:268-270(1997).
Hu B.,et al.Nucleic Acids Res. 21:5289-5293(1993).
Ishimi Y.,et al.J. Biol. Chem. 272:24508-24513(1997).

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