R7884
Ribonuclease B from bovine pancreas
BioReagent, ≥50 Kunitz units/mg protein, ≥80% (SDS-PAGE)
Synonym(s):
RNase B
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About This Item
CAS Number:
UNSPSC Code:
12352204
EC Number:
232-646-6
NACRES:
NA.32
MDL number:
Specific activity:
≥50 Kunitz units/mg protein
Assay:
≥80% (SDS-PAGE)
Biological source:
bovine pancreas
Concentration:
≥60%
SMILES string
[nH]1cncc1CC(NC(=O)CCN)C(=O)O
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
biological source
bovine pancreas
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
Quality Level
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
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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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
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.
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
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
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