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NGLY1 Antibody (Center) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | Q96IV0 |
|---|---|
| Clone Names | 81028096 |
| Gene ID | 55768 |
|---|---|
| Other Names | Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase, PNGase, hPNGase, N-glycanase 1, Peptide:N-glycanase, NGLY1, PNG1 |
| Target/Specificity | The synthetic peptide sequence used to generate the antibody AP6689c was selected from the Center region of human NGLY1. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | NGLY1 |
|---|---|
| Synonyms | PNG1 |
| Function | Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation. Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp. Prefers proteins containing high-mannose over those bearing complex type oligosaccharides. Can recognize misfolded proteins in the endoplasmic reticulum that are exported to the cytosol to be destroyed and deglycosylate them, while it has no activity toward native proteins. Deglycosylation is a prerequisite for subsequent proteasome-mediated degradation of some, but not all, misfolded glycoproteins. |
| Cellular Location | Cytoplasm. |
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Provided below are standard protocols that you may find useful for product applications.
Background
NGLY1 is an enzyme that catalyzes hydrolysis of an N(4)-(acetyl-beta-D-glucosaminyl) asparagine residue to N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue. The enzyme may play a role in the proteasome-mediated degradation of misfolded glycoproteins.
References
Altrich-VanLith,M.L., J. Immunol. 177 (8), 5440-5450 (2006)Katiyar,S., Mol. Biol. Cell 16 (10), 4584-4594 (2005)
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