Recombinant人NUDT2 protein (ab87952)

概述

描述

  • 性质Recombinant
  • 来源Saccharomyces cerevisiae
  • 氨基酸序列
    • 种属Human
    • 序列MALRACGLIIFRRCLIPKVDNNAIEFLLLQASDGIHHWTPPKGHVEPGED DLETALRETQEEAGIEAGQLTIIEGFKRELNYVARNKPKTVIYWLAEVKD YDVEIRLSHEHQAYRWLGLEEACQLAQFKEMKAALQEGHQFLCSIEA

技术指标

Our Abpromise guarantee covers the use of ab87952 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • 应用

    SDS-PAGE

  • 形式Liquid
  • Concentration information loading...

制备和贮存

  • 稳定性和存储

    Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid repeated freeze / thaw cycles.

    Preservative: None
    Constituents: 30% Glycerol, 0.5% Triton-X-100, 50mM HEPES, 30mM Glutathione, 100mM Sodium chloride, 1mM DTT, pH 7.5

常规信息

  • 别名
    • 2310051L06Rik
    • 5''''-P1
    • AA939917
    • Ap4A hydrolase
    • Ap4A hydrolase 1
    • AP4A_HUMAN
    • Ap4Aase
    • APAH 1
    • APAH1
    • Bis(5' nucleosyl) tetraphosphatase [asymmetrical]
    • Bis(5''-nucleosyl)-tetraphosphatase [asymmetrical]
    • Diadenosine 5''
    • Diadenosine 5',5''' P1,P4 tetraphosphate asymmetrical hydrolase
    • Diadenosine 5',5''-P1,P4-tetraphosphate pyrophosphohydrolase
    • Diadenosine tetraphosphatase
    • EC 3.6.1.17
    • MGC10404
    • Nucleoside diphosphate linked moiety X motif 2
    • Nucleoside diphosphate-linked moiety X motif 2
    • nudix (nucleoside diphosphate linked moiety X)-type motif 2
    • Nudix motif 2
    • Nudix-type motif 2
    • NUDT 2
    • NUDT2
    • OTTHUMP00000021256
    • OTTHUMP00000021257
    • OTTHUMP00000021258
    • OTTHUMP00000021259
    • P4-tetraphosphate asymmetrical hydrolase
    see all
  • 功能Asymmetrically hydrolyzes Ap4A to yield AMP and ATP. Plays a major role in maintaining homeostasis.
  • 序列相似性Belongs to the Nudix hydrolase family.
    Contains 1 nudix hydrolase domain.
  • Information by UniProt

Recombinant Human NUDT2 protein (ab87952)参考文献

ab87952 has not yet been referenced specifically in any publications.

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