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

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Vista general
Número de catálogoHC208012
Descripción
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.
Sistema de expresiónE. coli
Número de accesoP33991
Longitud de proteínaAsn275-Asp775
AplicacionesELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress
EspeciesHomo sapiens (Human)
Naturaleza Recombinant
Nivel de endotoxinas Please contact with the lab for this information.
Pureza >90% as determined by SDS-PAGE.
Peso molecular predicho 58.78 kDa
Forma Lyophilized
Buffer de almacenamiento Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol.

Consulte la información específica del buffer en la copia impresa del datasheet o en el COA específico del lote.

Reconstitución Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details.
Envío In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise.
Estabilidad y almacenamiento 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.
Nombres alternativosCDC21, CDC21 homolog, DNA replication licensing factor MCM4, EC:3.6.4.12, MCM4, P1-CDC21
Fondo

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
Nota For research use only
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Formula
Mass (g) = Concentration (mol/L) × Volume (L) × MW (g/mol)
Enter any 2 of Mass, Concentration, Volume + Molecular Weight to solve for the unknown.
Mass
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Concentration
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Volume
Molecular Weight *
g/mol
Formula
C₁ × V₁ = C₂ × V₂
Enter any 3 of the 4 values to solve for the unknown.
Stock Solution
C₁ (Stock Conc.)
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V₁ (Stock Vol.)
=
Working Solution
C₂ (Working Conc.)
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V₂ (Working Vol.)
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