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Merck
CN

R7884

核糖核酸酶B 来源于牛胰腺

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

别名:

RNase B

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关于此项目

化学文摘社编号:
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%
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Quality Level

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

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

在细胞周期平台分析期间,牛胰腺核糖核酸酶B可用于消化RNA。

Biochem/physiol Actions

通过枯草杆菌蛋白酶消化天然RNase B(包含RNase B的氨基酸残基21-124)产生的天然RNase BS对PNGase F消化敏感。 牛胰腺RNase B的分子内N-聚糖具有伴侣蛋白的作用。 已有研究发现RNase B比RNase A起效更快,而RNase A在再生过程中易于聚集。Asn-寡糖(对应于RNase B的最主要糖链)的刺激作用表面RNase B的N-聚糖可促进大体积中间体转化为折叠的紧密物种。

Packaging

包装尺寸取决于蛋白质含量

Preparation Note

通过亲和层析纯化


pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

存储类别

11 - Combustible Solids

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

法规信息

低风险生物材料

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历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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商品

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



全球贸易项目编号

货号GTIN
R7884-500UG04061836807344
R7884-100MG04061836801892
R7884-5MG04061833290323