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E. coli Elongation Factor 4 Protein, His Tag (active enzyme)

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EF4-E5143-50ug
$450.00
In Stock - Delivery in 1-2 business days
EF4-E5143-500ug
$2,600.00
In Stock - Delivery in 2-3 weeks
EF4-E5143
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Product Details
Performance Data
Reviews & Citations
Resources
  • Product Details
  • Performance Data
  • Reviews & Citations
  • Important Statement
  • Resources
Synonyms

Elongation Factor 4

Source

E. coli Elongation Factor 4 Protein, His Tag (EF4-E5143) is expressed from E. coli cells. It contains AA Lys 2 - Lys 599 (Accession # C4ZYJ2).

Predicted N-terminus: Met

Molecular Characterization
Other Tags and Version Biotin & Other Labeled Version

This protein carries a polyhistidine tag at the N-terminus.

The protein has a calculated MW of 68.5 kDa. The protein migrates as 65-80 kDa when calibrated against Star Ribbon Pre-stained Protein Marker under reducing (R) condition (SDS-PAGE).

Purity

>90% as determined by SDS-PAGE.

Formulation

Supplied as 0.2 μm filtered solution in PBS, 0.5 M NaCl, 1 M Arginine, pH7.4 with glycerol as protectant.

Contact us for customized product form or formulation.

Shipping and Storage

This product is supplied and shipped on dry ice.

Please avoid repeated freeze-thaw cycles.

This product is stable after storage at:
  • The product MUST be stored at -70°C or lower upon receipt;
  • -70°C for 3 months under sterile conditions.
ACRO Quality Management System

Background

Elongation Factor 4 (EF4), also known as ​​LepA​​, is a highly conserved ​​GTPase translation factor​​ present across bacteria, mitochondria, and chloroplasts. It regulates protein synthesis by interacting with the ribosome during translation elongation. Unlike canonical elongation factors (e.g., EF-G) that promote forward translocation, EF4 catalyzes ​​back-translocation of tRNAs​​ on the ribosome, effectively acting as a molecular ’reverse gear‘ to reposition tRNAs and mRNA. This unique function allows EF4 to maintain translational fidelity under stress conditions (e.g., low pH or high ionic strength) by rescuing stalled ribosomes and correcting errors in protein synthesis.