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Mad-1 Antibody

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  • 询价
  • Cell Signaling Technology已认证
  • USA
  • 2025年08月21日
  • W
  • Rabbit
  • H,M,R
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    • 详细信息
    • 文献和实验
    • 技术资料
    • 抗体英文名

      Mad-1 Antibody

    • 抗原

      synthetic peptide corresponding to the carboxy terminus region of Mad-1

    • 应用范围

      W

    • 宿主

      Rabbit

    • 保质期

      详见说明书

    • 适应物种

      H,M,R

    • 库存

      大量

    • 级别

      详见MSDS文件

    • 供应商

      CST

    • 是否单克隆

      2

    • 保存条件

      -20°c

    • 规格

      100 ul (10 western blots)/carrier free & custom formulation / quantity

    规格:产品价格:¥请询价
    规格:100 ul (10 western blots)产品价格:¥请询价
    规格:carrier free & custom formulation / quantity产品价格:¥请询价

    pathway more info application references datasheet PDF MSDS PDF protocols

    Applications Key:  W=Western Blotting
    Reactivity Key:  H=Human  M=Mouse  R=Rat
    Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

    Applications Reactivity Sensitivity MW (kDa) Source
    W H M R Endogenous 22 Rabbit
    Protocols
    Specificity / Sensitivity

    Mad-1 Antibody detects endogenous levels of Mad-1 . It does not cross-react with other Mad family members at physiological levels.

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to the carboxy terminus region of Mad-1. Antibodies are purified by protein A and peptide affinity chromatography.

    Western Blotting

    Western Blotting

    Western blot analysis of extracts from HT-1080 (human) and NBT-II (rat) cells, using Mad-1 Antibody.

    Background

    Members of the Myc/Max/Mad network function as transcriptional regulators with roles in various aspects of cell behavior including proliferation, differentiation and apoptosis (1). These proteins share a common basic-helix-loop-helix leucine zipper (bHLH-ZIP) motif required for dimerization and DNA-binding. Max was originally discovered based on its ability to associate with c-Myc and found to be required for the ability of Myc to bind DNA and activate transcription (2). Subsequently, Max has been viewed as a central component of the transcriptional network, forming homodimers as well as heterodimers with other members of the Myc and Mad families (1). The association between Max and either Myc or Mad can have opposing effects on transcriptional regulation and cell behavior (1). The Mad family consists of four related proteins; Mad1, Mad2 (Mxi1), Mad3 and Mad4, and the more distantly related members of the bHLH-ZIP family, Mnt and Mga. Like Myc, the Mad proteins are tightly regulated with short half-lives. In general, Mad family members interfere with Myc-mediated processes such as proliferation, transformation and prevention of apoptosis by inhibiting transcription (3,4).

    1. Baudino, T.A. and Cleveland, J.L. (2001) Mol. Cell. Biol. 21, 691-702.
    2. Blackwood, E.M. and Eisenman, R.N. (1991) Science 251, 1211-1217.
    3. Henriksson, M. and Lüscher, B. (1996) Adv. Cancer Res. 68, 109-182.
    4. Grandori, C. et al. (2000) Annu. Rev. Cell Dev. Biol. 16, 653-699.
    Application References

    Have you published research involving the use of our products? If so we'd love to hear about it. Please let us know !

    Companion Products

    For Research Use Only. Not For Use In Diagnostic Procedures.

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    图标文献和实验
    相关实验
    • Optimization of the MAD Algorithm for Virtual Screening

      The approach termed Determination and Mapping of Activity-Specific Descriptor Value Ranges (MAD) is a conceptually novel molecular similarity method for the identification of active compounds. MAD is based on mapping of compounds to different

    • Generation of Antibody Molecules Through Antibody Engineering

      been overcome to a large extent using genetic-engineering techniques to produce chimeric mouse/human and completely human antibodies. Such an approach is particularly suitable because of the domain structure of the antibody molecule ( 2 ), where functional

    • The Antibody Molecule

      The importance of antibody molecules was first recognized in the 1890s, when it was shown that immunity to tetanus and diphtheria was caused by antibodies against the bacterial exotoxins (1 ). Around the same time, it was shown that antisera

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