Skip to product information
1 of 1

GSPT1/ERF3A GST&His Protein, Human

GSPT1/ERF3A GST&His Protein, Human

Catalog Number: UA010964 Reactivity: Human Conjugation: Unconjugated Brand: UA BIOSCIENCE
Price:
Regular price $908.00 SGD
Regular price Sale price $908.00 SGD
Size:
For shipping services or bulk orders, you may request a quotation.
Secure checkout with
View full details

Product Details

Product Specification


Species Human
Synonyms ERF3A;eRF3aFLJ38048;ETF3A;eukaryotic peptide chain release factor GTP-binding subunit ERF3A;Eukaryotic peptide chain release factor subunit 3a;FLJ39067;G1 to S phase transition 1,551G9.2;G1 to S phase transition protein 1 homolog;GST1
Accession P15170-1
Amino Acid Sequence Phe294-Asp499, with C-terminal GST&His
Expression System Baculovirus-InsectCells
Molecular Weight 51kDa (Reducing)
Purity >85% by SDS-PAGE
Endotoxin <0.1EU/μg
Conjugation Unconjugated
Physical Appearance Liquid
Storage Buffer 50mM Tris, 20mM GSH, 5%Glycerol, pH8.0
Stability & Storage · 12 months from date of receipt, lyophilized powder stored at -20 to -80℃.
· 3 months, -20 to -80℃ under sterile conditions after reconstitution.
· 1 week, 2 to 8℃ under sterile conditions after reconstitution.
· Please avoid repeated freeze-thaw cycles.
Reference

Cell. 2016 Nov 17;167(5):1229-1240.e15.
Cell. 2006 Jun 16;125(6):1125-36.

Background

GSPT1/ERF3A mediates ETF1/ERF1 delivery to stop codons: The eRF1-eRF3-GTP complex binds to a stop codon in the ribosomal A-site.GTP hydrolysis by GSPT1/ERF3A induces a conformational change that leads to its dissociation, permitting ETF1/ERF1 to accommodate fully in the A-site. Binding of eRF1, eRF3, and GTP to pretermination complexes first induces a structural rearrangement that is manifested as a 2 nucleotide forward shift of the toeprint attributed to pretermination complexes that leads to GTP hydrolysis followed by rapid hydrolysis of peptidyl tRNA.

Picture

SDS-PAGE

1μg (R: reducing condition, N: non-reducing condition).

Customer Reviews

Be the first to write a review
0%
(0)
0%
(0)
0%
(0)
0%
(0)
0%
(0)