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安全信息

SAB4501106

Sigma-Aldrich

Anti-ZZZ3 antibody produced in rabbit

affinity isolated antibody

别名:

ZZ-type zinc finger-containing protein 3, ZZZ3

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About This Item

UNSPSC代码:
12352203
NACRES:
NA.41

生物来源

rabbit

质量水平

偶联物

unconjugated

抗体形式

affinity isolated antibody

抗体产品类型

primary antibodies

克隆

polyclonal

表单

buffered aqueous solution

分子量

antigen 102 kDa

种属反应性

rat, mouse, human

浓度

~1 mg/mL

技术

ELISA: 1:5000
western blot: 1:500-1:1000

NCBI登记号

UniProt登记号

运输

wet ice

储存温度

−20°C

靶向翻译后修饰

unmodified

基因信息

human ... ZZZ3(26009)

相关类别

一般描述

Anti-ZZZ3 Antibody detects endogenous levels of total ZZZ3 protein.

免疫原

The antiserum was produced against synthesized peptide derived from human ZZZ3.

Immunogen Range: 341-390

特点和优势

Evaluate our antibodies with complete peace of mind. If the antibody does not perform in your application, we will issue a full credit or replacement antibody. Learn more.

外形

Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.

免责声明

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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储存分类代码

10 - Combustible liquids

WGK

nwg

闪点(°F)

Not applicable

闪点(°C)

Not applicable

法规信息

新产品

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分析证书(COA)

Lot/Batch Number

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Wenyi Mi et al.
Nature communications, 9(1), 3759-3759 (2018-09-16)
Recognition of histones by epigenetic readers is a fundamental mechanism for the regulation of chromatin and transcription. Most reader modules target specific post-translational modifications on histones. Here, we report the identification of a reader of histone H3, the ZZ-type zinc
Wenyi Mi et al.
Nature communications, 8(1), 1088-1088 (2017-10-24)
Recognition of modified histones by "reader" proteins constitutes a key mechanism regulating diverse chromatin-associated processes important for normal and neoplastic development. We recently identified the YEATS domain as a novel acetyllysine-binding module; however, the functional importance of YEATS domain-containing proteins
Antoine Graindorge et al.
Nature communications, 10(1), 5317-5317 (2019-11-24)
Regulatory RNAs exert their cellular functions through RNA-binding proteins (RBPs). Identifying RNA-protein interactions is therefore key for a molecular understanding of regulatory RNAs. To date, RNA-bound proteins have been identified primarily through RNA purification followed by mass spectrometry. Here, we

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