PNG1 Antibody
Description
Molecular and Functional Characteristics of PNG1
Key features:
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Enzyme activity: PNG1 cleaves N-linked glycans from misfolded glycoproteins via its transglutaminase-like domain .
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Subcellular localization: Primarily nuclear, with cytoplasmic presence in yeast (S. cerevisiae) and Drosophila .
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Conservation: Homologs identified in humans (NGLY1), mice, plants (Neurospora crassa), and flies (D. melanogaster) .
Common assays:
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Western blotting: Detects PNG1 in yeast (42.5 kDa), Drosophila (44.7 kDa), and mammalian lysates .
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Immunofluorescence: Localizes PNG1 to nuclei in yeast and Drosophila ISCs .
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Activity profiling: Antibody-based pulldowns validate enzymatic activity loss in mutants (e.g., png1-1 D285N/E239D) .
Key validation data:
| Assay | Sample Type | Result | Source |
|---|---|---|---|
| Activity rescue | Yeast Δpng1 | 10-50% activity in D179E/P180A mutants | |
| ENGase inhibition | Drosophila midgut | Rabeprazole restores ISC proliferation |
Disease Relevance and Therapeutic Insights
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Neurodegeneration: PNG1 dysfunction correlates with polyubiquitinated protein accumulation, mimicking NGLY1 deficiency disorders .
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Cancer pathways: PNG1 knockdown alters ROS levels and CncC/NF-E2-related signaling in Drosophila epithelial cells .
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Therapeutic targets: ENGase inhibitors (e.g., Rabeprazole) rescue PNG1-related phenotypes, suggesting combinatorial treatment strategies .
Product Specs
**Constituents:** 50% Glycerol, 0.01M PBS, pH 7.4
Target Background
- The plant PNGase facilitates ERAD (Endoplasmic Reticulum-Associated Degradation) through its deglycosylation activity. Conversely, the catalytic mutant of AtPNG1 impairs glycoprotein ERAD by binding to N-glycans on the ERAD substrates. PMID: 22659524
- The AtPng1p gene product functions as a transglutaminase, representing the first characterized plant protein exhibiting TGase activity at the molecular level. [AtPng1p] PMID: 15299133
- AtPng1p, the first sequenced plant transglutaminase, shows minimal sequence homology to its animal counterparts, except for the catalytic triad. However, it possesses calcium-dependent activity, which enabled the construction of a three-dimensional model. PMID: 18622667
