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R7884

Sigma-Aldrich

Ribonuclease B from bovine pancreas

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

Synonyme(s) :

RNase B

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About This Item

Numéro CAS:
9001-99-4
Numéro de classification (Commission des enzymes):
3.1.27.5 (BRENDA, IUBMB)
Numéro CE :
232-646-6
Numéro MDL:
MFCD00132184
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.32

Source biologique

bovine pancreas

Gamme de produits

BioReagent

Pureté

≥80% (SDS-PAGE)

Forme

powder

Activité spécifique

≥50 Kunitz units/mg protein

Concentration

≥60%

Technique(s)

cell based assay: suitable

Adéquation

suitable for molecular biology

Application(s)

cell analysis

Activité étrangère

protease ≤0.001 units/mg solid

Température de stockage

−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)

Clé InChI

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.

Actions biochimiques/physiologiques

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.

Conditionnement

Package size based on protein content

Notes préparatoires

Purified by affinity chromatography

Inhibiteur

Réf. du produit
Description
Tarif

Pictogrammes

Health hazard
GHS08

Mention d'avertissement

Danger

Mentions de danger

H334

Conseils de prudence

P261 - P284 - P501

Classification des risques

Resp. Sens. 1

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

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.
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
Vijay Ramakrishnan et al.
American journal of hematology, 85(9), 675-686 (2010-07-24)
Interaction of myeloma cells with the bone marrow microenvironment is mediated in large part through different cytokines, especially VEGF and IL6. These cytokines, especially IL6, leads to upregulation of the JAK/STAT pathway in myeloma cell, contributing to increased proliferation, decreased
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
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Rapid Glycan Prep & Analysis by LC-MS Workflow

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

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