100% Quality Guarantee
PhD-Level Technical Support
Human NEMF Recombinant Protein (N-His)
Key Features

Human NEMF Recombinant Protein (N-His) (GXRP11007)

SKU GXRP11007
Product Type Recombinant Protein
Species Human
Expression System E. coli
Tag N-His
$458 - $2,412

Request a formal quotation

A PDF quote with its own quote number, ready for your purchasing office to raise a PO against. Back within 4 working hours, from a PhD scientist — not an autoresponder.

  • PO-ready PDFQuote number, VAT, Incoterms
  • Volume pricing appliedDiscounts from 2 kits up
  • Valid 30 daysPrices held while you get sign-off
Anything we should know? optional

No account needed. We use your details only to prepare and send this quote. If it's urgent, say so in the box and we'll come back the same working day.

Global Shipping: 80+ Countries
White Glove Service: Available upon request
Batch Consistency: Contact Sales
Distributors: 60+ Countries

Description

system_update_altDatasheetsystem_update_altMSDS

Human NEMF Recombinant Protein (N-His)

Human NEMF Recombinant Protein (N-His) is a recombinant protein expressed in E. coli, spanning Asp959-Lys1076, with an N-terminal His tag. Predicted molecular weight: 15.56 kDa. Purity: >90% as determined by SDS-PAGE. Supplied lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol. Applications: ELISA, immunogen, SDS-PAGE and Western blot. Ribosome quality control complex subunit NEMF is a ~122 kDa protein. Key component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates the extraction of incompletely synthesized nascent chains from stalled ribosomes as well as their ubiquitin-mediated proteasomal degradation. For research use only.

Thereby, frees 60S subunit ribosomes from the stalled translation complex and prevents the accumulation of nascent polypeptide chains that are potentially toxic for the cell. Within the RQC complex, NEMF specifically binds stalled 60S ribosomal subunits by recognizing an exposed, nascent chain-conjugated tRNA moiety and promotes the recruitment of LTN1 to stalled 60S subunits. Following binding to stalled 60S ribosomal subunits, NEMF mediates CAT tailing by recruiting alanine-charged tRNA to the A-site and directing the elongation of stalled nascent chains independently of mRNA or 40S subunits, leading to non-templated C-terminal alanine extensions (CAT tails). Mainly recruits alanine-charged tRNAs, but can also other amino acid-charged tRNAs.

View AllClose

0 Reviews

0
Based on 0 reviews

No reviews yet. Be the first to share your experience!

View AllClose