GCN1 Antibody [G16A4] | Primary Antibodies

Application: Reactivity: Human, Mouse, Rat

Usage Information

Dilution
WB1:1000

Application
WB

Reactivity
Human, Mouse, Rat

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
293 kDa 295 kDa,124 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Datasheet & SDS

Biological Description

Specificity
GCN1 Antibody [G16A4] detects endogenous levels of total GCN1 protein.

Clone
G16A4

Synonym(s)
GCN1L1, KIAA0219, GCN1, Stalled ribosome sensor GCN1, GCN1 eIF-2-alpha kinase activator homolog, GCN1-like protein 1, General control of amino-acid synthesis 1-like protein 1, Translational activator GCN1, HsGCN1

Background
GCN1 (GCN1 activator of EIF2AK4) is a large ribosome‑bound regulatory protein that functions as a collision sensor and upstream activator of the protein kinase GCN2, thereby integrating translational status and amino acid availability with the integrated stress response and co‑translational quality control. The protein contains extended HEAT‑like repeats and an EF3‑related region that contacts elongating ribosomes and forms a complex with its partner GCN20; this architecture allows GCN1 to bind disomes and higher‑order collided ribosome assemblies and to position GCN2 at the interface between ribosomal subunits and the A‑site region. During amino acid limitation or other stresses that slow elongation, ribosomes stall with unoccupied A sites, trailing ribosomes collide with the stalled ones, and GCN1 is recruited to these collided ribosomes, where it in turn recruits and stabilizes GCN2, enabling GCN2 activation by specific interactions with the collided ribosome and by local enrichment of uncharged tRNA cognate to the A‑site codon. Activated GCN2 phosphorylates the α subunit of eukaryotic initiation factor 2, which converts eIF2 into an inhibitor of ternary complex recycling, attenuates global cap‑dependent translation, and promotes selective translation of stress‑responsive mRNAs such as ATF4, thereby triggering a transcriptional program that upregulates amino acid transporters and biosynthetic enzymes and restores metabolic balance. Beyond this canonical amino acid response, GCN1 contributes to responses to UV irradiation and other stresses that induce ribosome pausing, and mammalian genetic analyses show that GCN1 is essential for embryonic development, cell proliferation, and proper G2/M progression, linking its ribosome‑associated functions to cell‑cycle regulation. GCN1 also participates directly in ribosome‑centric quality control: GCN1 binding to collided ribosomes promotes engagement of the RNF14–RNF25 ubiquitin ligase pathway, which targets elongation factor eEF1A and release factor eRF1 for ubiquitination and degradation and modifies ribosomal proteins, coupling persistent stalling to the clearance of key translation factors and reconfiguration of the translational machinery.

Background

GCN1 (GCN1 activator of EIF2AK4) is a large ribosome‑bound regulatory protein that functions as a collision sensor and upstream activator of the protein kinase GCN2, thereby integrating translational status and amino acid availability with the integrated stress response and co‑translational quality control. The protein contains extended HEAT‑like repeats and an EF3‑related region that contacts elongating ribosomes and forms a complex with its partner GCN20; this architecture allows GCN1 to bind disomes and higher‑order collided ribosome assemblies and to position GCN2 at the interface between ribosomal subunits and the A‑site region. During amino acid limitation or other stresses that slow elongation, ribosomes stall with unoccupied A sites, trailing ribosomes collide with the stalled ones, and GCN1 is recruited to these collided ribosomes, where it in turn recruits and stabilizes GCN2, enabling GCN2 activation by specific interactions with the collided ribosome and by local enrichment of uncharged tRNA cognate to the A‑site codon. Activated GCN2 phosphorylates the α subunit of eukaryotic initiation factor 2, which converts eIF2 into an inhibitor of ternary complex recycling, attenuates global cap‑dependent translation, and promotes selective translation of stress‑responsive mRNAs such as ATF4, thereby triggering a transcriptional program that upregulates amino acid transporters and biosynthetic enzymes and restores metabolic balance. Beyond this canonical amino acid response, GCN1 contributes to responses to UV irradiation and other stresses that induce ribosome pausing, and mammalian genetic analyses show that GCN1 is essential for embryonic development, cell proliferation, and proper G2/M progression, linking its ribosome‑associated functions to cell‑cycle regulation. GCN1 also participates directly in ribosome‑centric quality control: GCN1 binding to collided ribosomes promotes engagement of the RNF14–RNF25 ubiquitin ligase pathway, which targets elongation factor eEF1A and release factor eRF1 for ubiquitination and degradation and modifies ribosomal proteins, coupling persistent stalling to the clearance of key translation factors and reconfiguration of the translational machinery.

References
https://pubmed.ncbi.nlm.nih.gov/38474243/ https://pubmed.ncbi.nlm.nih.gov/41037622/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%