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R1153

Sigma-Aldrich

RNase B Glycoprotein Standard from bovine pancreas

≥90% (SDS-PAGE), lyophilized powder

Sinónimos:

Ribonuclease B from bovine pancreas, RNase B

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About This Item

Número de CAS:
9001-99-4
EC Number:
232-646-6
MDL number:
MFCD00132184
UNSPSC Code:
12352204
NACRES:
NA.32

product name

RNase B Glycoprotein Standard from bovine pancreas, Proteomics Grade

grade

Proteomics Grade

Quality Level

200

assay

≥90% (SDS-PAGE)

form

lyophilized powder

storage temp.

−20°C

InChI

1S/C9H14N4O3/c10-2-1-8(14)13-7(9(15)16)3-6-4-11-5-12-6/h4-5,7H,1-3,10H2,(H,11,12)(H,13,14)(H,15,16)

InChI key

CQOVPNPJLQNMDC-UHFFFAOYSA-N

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Application

RNase B is a preferred substrate with PNGase F for demonstration of N-linked deglycosylation using SDS-PAGE or MALDI-MS. The activity of PNGase F is routinely assayed using RNase B by monitoring the pronounced mobility shift in 12% gels after deglycosylation. Proteomics Grade RNase B has been used as a source of N-glycans following enzymatic digestions and subsequent purification. It has also been used as a glycoprotein standard.

Other Notes

Bovine pancreatic RNase B is a glycoprotein that contains only N-linked glycans. It is a globular protein composed of a single domain that occurs naturally as a lesser component in mixture along with ribonuclease A (RNase A), which is the non-glycosylated core form. RNase B contains a single glycosylation site at Asn34 at which from five to nine mannose residues are attached to the chitobiose core, i.e. Man5-9GlcNAc2. Due to the heterogeneity in the glycosylation at Asn34, RNase B exists as five glycosylated varients, with a molecular weight of approx. 15 kDa.

Quality

RNAse B Glycoprotein Standard has been highly purified to remove contaminating RNase A.

pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H334

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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»

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Cytosolic nuclease TREX1 regulates oligosaccharyltransferase activity independent of nuclease activity to suppress immune activation
Hasan M, et al.
Immunity, 43(3), 463-474 (2015)
Integrated GlycoProteome Analyzer (I-GPA) for automated identification and quantitation of site-specific N-glycosylation
Park GW, et al.
Scientific Reports, 6, 21175-21175 (2016)
Fabian Higel et al.
mAbs, 6(4), 894-903 (2014-05-23)
N-glycosylation is a complex post-translational modification with potential effects on the efficacy and safety of therapeutic proteins and known influence on the effector function of biopharmaceutical monoclonal antibodies (mAbs). Comprehensive characterization of N-glycosylation is therefore important in biopharmaceutical development. In
Maroof Hasan et al.
Immunity, 43(3), 463-474 (2015-09-01)
TREX1 is an endoplasmic reticulum (ER)-associated negative regulator of innate immunity. TREX1 mutations are associated with autoimmune and autoinflammatory diseases. Biallelic mutations abrogating DNase activity cause autoimmunity by allowing immunogenic self-DNA to accumulate, but it is unknown how dominant frameshift
Alex M Yoshikawa et al.
Nature communications, 12(1), 7106-7106 (2021-12-09)
Glycosylation is one of the most abundant forms of post-translational modification, and can have a profound impact on a wide range of biological processes and diseases. Unfortunately, efforts to characterize the biological function of such modifications have been greatly hampered
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