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Merck
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重要文件

SAB4501106

Sigma-Aldrich

Anti-ZZZ3 antibody produced in rabbit

affinity isolated antibody

同義詞:

ZZ-type zinc finger-containing protein 3, ZZZ3

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About This Item

分類程式碼代碼:
12352203
NACRES:
NA.41

生物源

rabbit

品質等級

共軛

unconjugated

抗體表格

affinity isolated antibody

抗體產品種類

primary antibodies

無性繁殖

polyclonal

形狀

buffered aqueous solution

分子量

antigen 102 kDa

物種活性

rat, mouse, human

濃度

~1 mg/mL

技術

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

NCBI登錄號

UniProt登錄號

運輸包裝

wet ice

儲存溫度

−20°C

目標翻譯後修改

unmodified

基因資訊

human ... ZZZ3(26009)

相關類別

一般說明

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

特點和優勢

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.

外觀

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

免責聲明

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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儲存類別代碼

10 - Combustible liquids

水污染物質分類(WGK)

nwg

閃點(°F)

Not applicable

閃點(°C)

Not applicable


分析證明 (COA)

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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
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
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

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