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Safety Information

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

Signal Word

Danger

Hazard Statements

H334

Precautionary Statements

P261 - P284 - P501

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

JAN Code

R1153-500UG-PW:
R1153-1MG:
R1153-VAR:
R1153-1MG-KC:
R1153-PH:
R1153-500UG:
R1153-1MG-PW:
R1153-BULK:
R1153PROC:
R1153-BULK-N:

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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Jens Möller et al.
Scientific reports, 3, 2884-2884 (2013-10-08)
To clear pathogens from host tissues or biomaterial surfaces, phagocytes have to break the adhesive bacteria-substrate interactions. Here we analysed the mechanobiological process that enables macrophages to lift-off and phagocytose surface-bound Escherichia coli (E. coli). In this opsonin-independent process, macrophage
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)
Cytosolic nuclease TREX1 regulates oligosaccharyltransferase activity independent of nuclease activity to suppress immune activation
Hasan M, et al.
Immunity, 43(3), 463-474 (2015)
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
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