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Elizabethkingia miricola PNGaseF Recombinant Protein

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Product nameElizabethkingia miricola PNGaseF Recombinant Protein
Uniprot IDP21163
Uniprot linkhttp://www.uniprot.org/uniprot/P21163
Origin speciesSchizosaccharomyces pombe
Expression systemProkaryotic expression
SequenceMAHNHRHKHKLSVHSDNQSQISIEVGRDAPAAAATDLSGIIGPQMTKSPASSVTHFSTPSMLPIGGTSLDDELLAPVDDL NLDLGLDDLLGDEQGANAPAIEADEQAETSSIHLPSDIMEDDSSRPAAAGVEEGQVVESATAPQQEKINPQKTVRRQRAI IDPVTELSSKQMKKQLADTSSITSPLCLNTSSIVFNATVNFTRNGKFNTSIFSSNLNPKVNELLQADFKQAILRKRKNES PEEVEPAKHQRTDTSTENQETAEVLDPEEIAAAELANITEAAIATLPQETVVQPEGEAPELGSPMGFPVTALESADDSLF DAPPVMLDEADLLGSERLDSSVSEALPSSQTAKDSLRNKWDPYTEGEKVSFQTLSAGCNREEAVQLFFDVLVLATKDVIS VKQDVAIQNEITLTAKRGMLLSSL
Molecular weight45,52 kDa
Purity estimated90%
BufferPBS, imidazole 300mM
Formliquid
Delivery conditionDry Ice
Delivery lead time in business days10-25
Storage condition4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection)
BrandProteoGenix
Host speciesEscherichia coli (E.coli)
ApplicationsELISA,WB
Fragment TypePartial
NCBI ReferenceNP_588151.1
Aliases /SynonymsPeptide -N-Glycosidase F, PNGase F, PNGaseF
ReferencePX-P3070
NoteFor research use only

Description of Elizabethkingia miricola PNGaseF Recombinant Protein

General information on Elizabethkingia miricola PNGaseF Recombinant Protein-15000u

PNGase F is a recombinant glycosidase cloned from Elizabethkingia miricola and overexpressed in E. coli. It cleaves a complete glycan from a glycoprotein and it deaminates the asparagine to aspartic acid, but leaves the oligosaccharide undamaged. PNGase F will not eliminate oligosaccharides containing Alpha-(1, 3)-linked core fucose usually found in plant glycoproteins. A tri-peptide with the oligosaccharide-linked asparagine as the central residue is the minimal substrate for PNGase F.

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Publication

  • 1: Kuhn P, Tarentino AL, Plummer TH Jr, Van Roey P. Crystal structure of peptide-N4-(N-acetyl-beta-D-glucosaminyl)asparagine amidase F at 2.2-A resolution. Biochemistry. 1994 Oct 4;33(39):11699-706. PubMed PMID: 7918386.
  • 2: Norris GE, Stillman TJ, Anderson BF, Baker EN. The three-dimensional structure of PNGase F, a glycosylasparaginase from Flavobacterium meningosepticum. Structure. 1994 Nov 15;2(11):1049-59. PubMed PMID: 7881905.
  • 3: Kuhn P, Guan C, Cui T, Tarentino AL, Plummer TH Jr, Van Roey P. Active site and oligosaccharide recognition residues of peptide-N4-(N-acetyl-beta-D-glucosaminyl)asparagine amidase F. J Biol Chem. 1995 Dec 8;270(49):29493-7. PubMed PMID: 7493989.
  • 4: Lemp D, Haselbeck A, Klebl F. Molecular cloning and heterologous expression of N-glycosidase F from Flavobacterium meningosepticum. J Biol Chem. 1990 Sep 15;265(26):15606-10. PubMed PMID: 2203781.
  • 5: Barsomian GD, Johnson TL, Borowski M, Denman J, Ollington JF, Hirani S, McNeilly DS, Rasmussen JR. Cloning and expression of peptide-N4-(N-acetyl-beta-D-glucosaminyl)asparagine amidase F in Escherichia coli. J Biol Chem. 1990 Apr 25;265(12):6967-72. PubMed PMID: 2182635.
  • 6: Tarentino AL, Quinones G, Trumble A, Changchien LM, Duceman B, Maley F, Plummer TH Jr. Molecular cloning and amino acid sequence of peptide-N4-(N-acetyl-beta-D-glucosaminyl)asparagine amidase from flavobacterium meningosepticum. J Biol Chem. 1990 Apr 25;265(12):6961-6. Erratum in: J Biol Chem 1990 Jul 5;265(19):11405. PubMed PMID: 2182634.

Reviews

  • Waltteri Hosia –

    Was the protein active?: Yes

    Very good product. I would buy again.

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