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MilliporeSigma

R7884

Ribonuclease B from bovine pancreas

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

Synonyme(s) :

RNase B

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A propos de cet article

Numéro CAS:
Numéro CE :
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%
Service technique
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biological source

bovine pancreas

Quality Level

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

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

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


pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Classe de stockage

11 - Combustible Solids

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)



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Articles

PNGase Fast denaturing buffer and enzyme provide results similar to a conventional 20-hour protocol, reducing workflow time to about 1 hour.


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
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



Numéro d'article de commerce international

RéférenceGTIN
R7884-500UG04061836807344
R7884-100MG04061836801892
R7884-5MG04061833290323