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Human MCM4 Recombinant Protein (N-His) (HC208012)

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Overview
Catalog No.HC208012
Description
Recombinant Human MCM4 Protein, N-His (HC208012) expressed in E. coli, spanning Asn275-Asp775. Purity: >90% by SDS-PAGE.
Highlights
  • His-Tagged — N-terminal 6×His tag for IMAC purification.
  • E. coli Expression — High-yield, cost-effective production.
  • High Purity — >90% purity verified by SDS-PAGE.
Expression systemE. coli
AccessionP33991
Protein lengthAsn275-Asp775
ApplicationsELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress
SpeciesHomo sapiens (Human)
Nature Recombinant
Endotoxin level Please contact with the lab for this information.
Purity >90% as determined by SDS-PAGE.
Predicted molecular weight 58.78 kDa
Form Lyophilized
Storage buffer Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol.

Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA.

Reconstitution Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details.
Shipping In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise.
Stability and Storage Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt.
Alternate NamesCDC21, CDC21 homolog, DNA replication licensing factor MCM4, EC:3.6.4.12, MCM4, P1-CDC21
Background

DNA replication licensing factor MCM4 is a ~96 kDa protein. 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.

1. Tsuji, T. et al. (2006) Molecular biology of the cell 17, 4459-72. PMID: 16899510
2. Ishimi, Y. et al. (2015) Journal of biochemistry 157, 561-9. PMID: 25661590
3. Rzechorzek, NJ. et al. (2020) Nucleic acids research 48, 6980-6995. PMID: 32453425
4. Jones, ML. et al. (2021) The EMBO journal 40, e108819. PMID: 34694004
5. Jenkyn-Bedford, M. et al. (2021) Nature 600, 743-747. PMID: 34700328
6. Baris, Y. et al. (2022) Nature 606, 204-210. PMID: 35585232
7. Ishimi, Y. (1997) The Journal of biological chemistry 272, 24508-13. PMID: 9305914
Note For research use only
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Formula
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