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Merck
CN

R5500

核糖核酸酶A 来源于牛胰腺

Type XII-A, ≥90% (SDS-PAGE), 75-125 Kunitz units/mg protein

别名:

RNAsea, RNase A, 核糖核酸 3′-嘧啶寡核苷酸水解酶, 核糖核酸酶 I, 胰核糖核酸酶

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关于此项目

化学文摘社编号:
NACRES:
NA.54
UNSPSC Code:
12352204
EC Number:
232-646-6
MDL number:
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产品名称

核糖核酸酶A 来源于牛胰腺, Type XII-A, ≥90% (SDS-PAGE), 75-125 Kunitz units/mg protein

SMILES string

[nH]1cnc(c1)CC(NC(=O)CCN)C(=O)O

InChI key

CQOVPNPJLQNMDC-UHFFFAOYSA-N

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)

biological source

bovine pancreas

type

Type XII-A

assay

≥90% (SDS-PAGE)

form

lyophilized powder

specific activity

75-125 Kunitz units/mg protein

mol wt

~13,700

technique(s)

cell based assay: suitable

impurities

salt, essentially free

suitability

suitable for mRNA or total RNA extracted from cells and tissues

application(s)

diagnostic assay manufacturing

foreign activity

protease, essentially free

storage temp.

−20°C

Quality Level

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Analysis Note

蛋白测定方法:E.

Application

  • RNase A用于去除DNA质粒和基因组DNA制品和蛋白质样品中的RNA。
  • RNase A还用于RNA序列分析和保护测定。
  • RNase A已用作计算辅助药物设计的工具。
  • RNase A为RNA序列分析提供支持。
  • RNase A水解蛋白质样品中的RNA。
  • RNase A为DNA纯化提供支持。

Biochem/physiol Actions

核糖核酸酶A是一种内切核糖核酸酶,可在嘧啶核苷酸后切割单链RNA。它在3'磷酸基末端进行攻击。核糖核酸酶不会水解DNA,因为DNA缺乏形成环状中间体所必需的2′-OH基团。RNA酶还可以水解蛋白质样品中的RNA。RNase A可被His12和His119的烷基化所抑制并被钾盐和钠盐所活化。

Features and Benefits

我们高度稳定的核糖核酸酶A——RNase A,适合于RNA去除、RNA测序和DNA纯化。

General description

RNase A(核糖核酸酶A)是一种内切核糖核酸酶,在嘧啶核苷酸后裂解单链RNA的磷酸二酯键。它可切割3′磷酸基末端(例如,pG-pG-pC-pA-pG将切割为pG-pG-pCp 和A-pG)。对单链RNA表现出最高活性。RNase A是含有四个二硫键的单链多肽。它与RNase B不同,并非糖蛋白。核糖核酸酶不会水解DNA,因为DNA缺乏形成环状中间体所必需的2′-OH基团。RNase A还可以水解蛋白质样品中的RNA。RNase A可被His12和His119的烷基化抑制并被钾盐和钠盐活化。RNAse在重金属离子存在时受到抑制。此外,RNase也被DNA竞争性抑制。

Preparation Note

盐分级和色谱纯化。

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

存储类别

11 - Combustible Solids

wgk

WGK 3

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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Vlad Zabrouskov et al.
Biochemistry, 45(3), 987-992 (2006-01-18)
Although deamidation at asparagine and glutamine has been found in numerous studies of a variety of proteins, in almost all cases the analytical methodology that was used could detect only a single site of deamidation. For the extensively studied case
Amaya Albalat et al.
Methods in molecular biology (Clifton, N.J.), 984, 153-165 (2013-02-07)
The analysis of proteins and peptides in biological fluids is becoming more important as they are potential sources of diagnostic biomarkers of disease. The complexity of body fluids is such that no single technique can both identify and quantify all
Aarón Millán-Oropeza et al.
Proteomes, 10(1) (2022-01-26)
In proteomics, it is essential to quantify proteins in absolute terms if we wish to compare results among studies and integrate high-throughput biological data into genome-scale metabolic models. While labeling target peptides with stable isotopes allow protein abundance to be
Xin-Miao Fu et al.
Biochimica et biophysica acta, 1814(4), 487-495 (2011-01-18)
Protein disulfide isomerase (PDI) and its pancreatic homolog (PDIp) are folding catalysts for the formation, reduction, and/or isomerization of disulfide bonds in substrate proteins. However, the question as to whether PDI and PDIp can directly attack the native disulfide bonds
Romina Ponzielli et al.
Nucleic acids research, 36(21), e144-e144 (2008-10-23)
High-throughput, microarray-based chromatin immunoprecipitation (ChIP-chip) technology allows in vivo elucidation of transcriptional networks. However this complex is not yet readily accessible, in part because its many parameters have not been systematically evaluated and optimized. We address this gap by systematically

实验方案

This procedure may be used for determination of Ribonuclease A (RNase A) activity.

本实验方案可用于测定核糖核酸酶A(RNase A)的活性。

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