

| Numéro de catalogue | HC208012 |
|---|---|
| Description |
Recombinant Human MCM4 Protein, N-His (HC208012) expressed in E. coli, spanning Asn275-Asp775. Purity: >90% by SDS-PAGE.
Highlights
|
| Système d'expression | E. coli |
| Numéro d'accès | P33991 |
| Longueur de protéine | Asn275-Asp775 |
| Applications | ELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress |
| Espèces | Homo sapiens (Human) |
| Nature | Recombinant |
| Niveau d'endotoxines | Please contact with the lab for this information. |
| Pureté | >90% as determined by SDS-PAGE. |
| Masse moléculaire prédite | 58.78 kDa |
| Forme | Lyophilized |
| Tampon de stockage | Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol. Reférez-vous aux informations spécifiques sur le tampon dans la copie papier du datasheet ou dans le COA spécifique au lot. |
| 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. |
| Expédition | In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise. |
| Stabilité et stockage | 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. |
| Noms alternatifs | CDC21, CDC21 homolog, DNA replication licensing factor MCM4, EC:3.6.4.12, MCM4, P1-CDC21 |
| Contexte | 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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