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Peptide-N (4)- (N-acetyl-beta-glucosaminyl)asparagine amidase (PNG1), Recombinant Protein
Cat: RP02051
Species: Arabidopsis thaliana (Mouse-ear cress)
Datasheet:
Product Info
Full Product Name
Recombinant Arabidopsis thaliana Peptide-N (4)- (N-acetyl-beta-glucosaminyl)asparagine amidase (PNG1) , partial
Product Gene Name
PNG1 recombinant protein
Product Synonym Gene Name
PNG1
Purity
Greater or equal to 85% purity as determined by SDS-PAGE. (lot specific)
Format
Lyophilized or liquid (Format to be determined during the manufacturing process)
Host
E Coli or Yeast or Baculovirus or Mammalian Cell
Molecular Weight
82,446 Da
Storage
Store at -20℃. For long-term storage, store at -20℃ or -80℃. Store working aliquots at 4℃ for up to one week. Repeated freezing and thawing is not recommended.
Protein Family
Protein
NCBI/Uniprot Data
NCBI Accession #
NP_199768.1
NCBI GI #
15240508
NCBI GenBank Nucleotide #
NM_124335.3
NCBI GeneID
835019
NCBI Official Full Name
peptide-N-glycanase 1
NCBI Official Symbol
PNG1
NCBI Official Synonym Symbols
AtPNG1; K6M13.12; K6M13_12; peptide-N-glycanase 1
NCBI Protein Information
peptide-N-glycanase 1
NCBI Summary
Encodes a protein that has peptide:N-glycanase activity in enzymatic assay in heterologous systems (although the activity was not detected in wild-type plants).
UniProt Gene Name
PNG1
UniProt Synonym Gene Names
AtPNG1
UniProt Protein Name
Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase
UniProt Synonym Protein Names
Peptide:N-glycanase; AtPNG1
UniProt Primary Accession #
Q9FGY9
UniProt Secondary Accession #
Q84WJ1
UniProt Related Accession #
Q9FGY9
UniProt Comments
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 .
For research use only, not for clinical use.