G1549
PNGase F from Elizabethkingia meningoseptica
ready-to-use solution, recombinant, expressed in E. coli
Sinónimos:
PNGase F
Iniciar sesiónpara Ver la Fijación de precios por contrato y de la organización
About This Item
Número de CAS:
Número MDL:
Código UNSPSC:
12352204
NACRES:
NA.54
Productos recomendados
recombinante
expressed in E. coli
Nivel de calidad
conjugado
(N-linked)
grado
Proteomics Grade
formulario
ready-to-use solution
actividad específica
≥1000 U/mg
caducidad
≥1 yr at -20 °C
mol peso
~36 kDa
Condiciones de envío
wet ice
temp. de almacenamiento
−20°C
¿Está buscando productos similares? Visita Guía de comparación de productos
Categorías relacionadas
Aplicación
Recombinant PNGase F has been purified by affinity chromatography and dialyzed into a 50% glycerol solution with 10 mM potassium phoosphate pH 7.5 to produce a stable product. The product contains low levels of buffer salts. This highly purified material can be used for preparative deglycosylation or for analytical applications in gel, in solution, or on blot membranes. The enzyme can be removed from preparative operations by utilizing its C-terminal 6x histidine fusion tag. PNGase F from Elizabethkingia meningoseptica has been used in deglycosylation assay in human plasma samples and in deglycosylation of chondroitin sulfate proteoglycan.
Used to deglycosylate protein.
Acciones bioquímicas o fisiológicas
PNGase F from Elizabethkingia meningoseptica has glycan-binding catalytic domain and a bowl-like domain at the N-terminus. It cleaves an entire glycan from a glycoprotein provided the glycosylated asparagine moiety is substituted on its amino and carboxyl terminus with a polypeptide chain. It is cost-effectively produced on a large scale in prokaryotic hosts and requires divalent zinc ions for its enzymatic activity.
Cleaves an entire glycan from a glycoprotein provided the glycosylated asparagine moiety is substituted on its amino and carboxyl terminus with a polypeptide chain.
Definición de unidad
One unit will catalyze the release of N-linked oligosaccharides from 1 nanomole of denatured ribonuclease B in one minute at 37°C at pH 7.5 monitored by SDS-PAGE. One Sigma unit of PNGase F activity is equal to 1 IUB milliunit.
Forma física
Supplied as 300 Units/mL enzyme in 50% (v/v) glycerol and 50% (v/v) 20 mM Potassium Phosphate, pH 7.5.
Código de clase de almacenamiento
10 - Combustible liquids
Clase de riesgo para el agua (WGK)
WGK 1
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
Certificados de análisis (COA)
Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»
¿Ya tiene este producto?
Encuentre la documentación para los productos que ha comprado recientemente en la Biblioteca de documentos.
Los clientes también vieron
N-glycosylation of apolipoprotein A1 in cardiovascular diseases
Majek P, et al.
Translational Research, 165(2), 360-362 (2015)
Characterization and analysis of extracellular matrix in malignant brain tumors and their cellular derivatives
Extracellular Matrix, 113-138 (2015)
Discovery and characterization of a novel extremely acidic bacterial N-glycanase with combined advantages of PNGase F and A
Wang T, et al.
Bioscience Reports, 34(6), e00149-e00149 (2014)
Identification and characterization of a novel prokaryotic peptide: N-glycosidase from Elizabethkingia meningoseptica
Sun G, et al.
The Journal of Biological Chemistry, jbc-M114 (2015)
T H Plummer et al.
The Journal of biological chemistry, 259(17), 10700-10704 (1984-09-10)
Endo-beta-N-acetylglucosaminidase F preparations from Flavobacterium meningosepticum have been found to contain peptide:N-glycosidase activity. Only the second activity, designated as peptide:N-glycosidase F, readily cleaves the beta-aspartylglycosylamine linkage of a fetuin triantennary complex glycopeptide, as shown by the isolation of the corresponding
Nuestro equipo de científicos tiene experiencia en todas las áreas de investigación: Ciencias de la vida, Ciencia de los materiales, Síntesis química, Cromatografía, Analítica y muchas otras.
Póngase en contacto con el Servicio técnico