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R7884

Sigma-Aldrich

Ribonuclease B from bovine pancreas

BioReagent, ≥50 Kunitz units/mg protein, ≥80% (SDS-PAGE)

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Synonym(s):
RNase B
CAS Number:
9001-99-4
Enzyme Commission number:
3.1.27.5 (BRENDA, IUBMB)
EC Number:
232-646-6
MDL number:
MFCD00132184
UNSPSC Code:
12352204
NACRES:
NA.32

biological source

bovine pancreas

Quality Level

200

product line

BioReagent

assay

≥80% (SDS-PAGE)

form

powder

specific activity

≥50 Kunitz units/mg protein

concentration

≥60%

technique(s)

cell based assay: suitable

suitability

suitable for molecular biology

application(s)

cell analysis

foreign activity

protease ≤0.001 units/mg solid

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

Ribonuclease B from bovine pancreas is used in the digestion of RNA during cell cycle platform analysis.

Biochem/physiol Actions

Native RNase BS generated by subtilisin digestion of native RNase B comprising of amino acid residues 21-124 of RNase B, is sensitive to PNGase F digestion. Intramolecular N-glycans of bovine pancreatic RNase B function like chaperone. RNase B is found to be much faster than RNase A, while RNase A is liable to aggregate during regeneration. The stimulatory effect of Asn-oligosaccharide (which corresponds to the most predominant sugar chain of RNase B) reveals that the N-glycans of RNase B facilitates the transformation of bulky intermediates into folded, compact species.

Packaging

Package size based on protein content

Preparation Note

Purified by affinity chromatography

inhibitor

Product No.
Description
Pricing

pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H334

Hazard Classifications

Resp. Sens. 1

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Certificates of Analysis (COA)

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Véronique Blanchard et al.
Biochemistry, 47(11), 3435-3446 (2008-02-26)
In glycoanalysis protocols, N-glycans from glycoproteins are most frequently released with peptide- N (4)-( N-acetyl-beta-glucosaminyl)asparagine amidase F (PNGase F). As the enzyme is an amidase, it cleaves the NH-CO linkage between the Asn side chain and the Asn-bound GlcNAc residue.
Audra A Hargett et al.
Molecules (Basel, Switzerland), 26(14) (2021-07-25)
Protein glycosylation is important in many organisms for proper protein folding, signaling, cell adhesion, protein-protein interactions, and immune responses. Thus, effectively determining the extent of glycosylation in glycoprotein therapeutics is crucial. Up to now, characterizing protein glycosylation has been carried
Yang Xu et al.
iScience, 25(8), 104753-104753 (2022-08-10)
N-Acetylglucosamine (GlcNAc) is an essential monosaccharide required in almost all organisms. Fluorescent labeling of the peptidoglycan (PG) on N-acetylglucosamine has been poorly explored. Here, we report on the labeling of the PG with a bioorthogonal handle on the GlcNAc. We
H Yamaguchi et al.
Journal of biochemistry, 120(3), 474-477 (1996-09-01)
This paper describes a chaperone-like function of the intramolecular N-glycans of bovine pancreatic RNase B. We studied air-oxidative regeneration from reductively denatured species of RNase B and its nonglycosylated form, RNase A. RNase B was reactivated much faster than RNase
Rafał Kolenda et al.
Frontiers in microbiology, 9, 1905-1905 (2018-09-07)
Bacterial host tropism is a primary determinant of the range of host organisms they can infect. Salmonella serotypes are differentiated into host-restricted and host-adapted specialists, and host-unrestricted generalists. In order to elucidate the underlying molecular mechanisms of host specificity in
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