Destrin Rabbit pAb, BF405 conjugated(bs-12997R-BF405)-100ul

Destrin Rabbit pAb, BF405 conj

ugated(bs-12997R-BF405)-100ul
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  • ¥2980
  • Bioss已认证
  • bs-12997R-BF405
  • 2025年09月30日
  • 产品信息以Bioss网站为准
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      100ul

    产品编号bs-12997R-BF405
    英文名称Destrin Rabbit pAb, BF405 conjugated
    中文名称BF405标记的肌动蛋白解聚因子抗体
    英文别名2610043P17Rik; ACTDP; Actin depolymerizing factor; Actin-depolymerizing factor; ADF; AU042046; bA462D18.2; corn1; DEST_HUMAN; Destrin(actin depolymerizing factor); Destrin; DSN; Dstn; Sid 23; sid23p.
    产品应用ICC/IF=1:50-200, IF=1:100-500

    Not yet tested in other applications.
    Optimal working dilutions must be determined by the end user.

    抗体来源Rabbit
    免疫原KLH conjugated synthetic peptide derived from human Destrin
    亚型IgG
    纯化方法affinity purified by Protein A
    克隆类型Polyclonal
    浓度1mg/ml
    储存液0.01M TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.
    研究领域

    Signal Transduction > Cytoskeleton / ECM > Cytoskeleton > Microfilaments > Actin etc > Actin Binding Proteins

    组织特异性Widely distributed in various tissues.
    翻译后修饰ISGylated (Probable).
    相似性Belongs to the actin-binding proteins ADF family.
    Contains 1 ADF-H domain._x000D_
    功能Actin-depolymerizing protein. Severs actin filaments (F-actin) and binds to actin monomers (G-actin). Acts in a pH-independent manner.
    保存条件Shipped at 4℃. Store at -20℃ for one year. Avoid repeated freeze/thaw cycles.
    背景资料Actin-depolymerizing factor (ADF), also known as destrin, is a member of the ADF/Cofilin/destrin superfamily that has the ability to rapidly depolymerize F-Actin in a stoichiometric manner. The Actin-depolymerizing activity of ADF is reversibly controlled by changes in KCl concentration but is insensitive to calcium concentration. ADF depolymerizes F-Actin by interacting directly with F-Actin protomers. ADF shares 71% sequence homology with Cofilin, however the two proteins differ in their interaction with Actin. The difference in the function of ADF and Cofilin results from the subtle difference in their amino acid sequence rather than possible differences in posttranslational modifications. As a result of different cleavage sites on ADF and Cofilin, the proteins differ in their overall tertiary folds. Sensitivity to polyphosphoinositides may be a common feature in vitro among Actin-binding proteins such as ADF and Cofilin that can bind to G-Actin and regulate the state of Actin polymerization. ADF and Cofilin are Actin-depolymerizing proteins whose activities are possibly regulated by their phosphorylation/dephosphorylation.

     

    应用推荐稀释比例
    {ICC/IF}{1:50-200}
    {IF}{1:100-500}

     

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