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R1153

Sigma-Aldrich

RNase B Glycoprotein Standard from bovine pancreas

≥90% (SDS-PAGE), lyophilized powder

Synonym(s):

Ribonuclease B from bovine pancreas, RNase B

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About This Item

CAS Number:
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)

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘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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