Přejít k obsahu
Merck
Všechny fotografie(1)

Hlavní dokumenty

R7884

Sigma-Aldrich

Ribonuclease B from bovine pancreas

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

Synonyma:

RNase B

Přihlásitk zobrazení cen stanovených pro organizaci a smluvních cen


About This Item

Číslo CAS:
Číslo enzymu podle klasifikace EK:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.32

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

Hledáte podobné produkty? Navštivte Průvodce porovnáváním produktů

Související kategorie

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

Č. produktu
Popis
Stanovení ceny

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


Vyberte jednu z posledních verzí:

Osvědčení o analýze (COA)

Lot/Batch Number

Nevidíte správnou verzi?

Potřebujete-li konkrétní verzi, můžete vyhledat daný certifikát podle čísla dávky nebo čísla šarže.

Již tento produkt vlastníte?

Dokumenty související s produkty, které jste v minulosti zakoupili, byly za účelem usnadnění shromážděny ve vaší Knihovně dokumentů.

Navštívit knihovnu dokumentů

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
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

Sortimentní položky

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

Náš tým vědeckých pracovníků má zkušenosti ve všech oblastech výzkumu, včetně přírodních věd, materiálových věd, chemické syntézy, chromatografie, analytiky a mnoha dalších..

Obraťte se na technický servis.