Mad1 (6-21)

目录号: PL08182 纯度: ≥98%
Mad1 (6-21) 是 Mad1 蛋白的 6-21 片段。Mad1 (6-21) 与哺乳动物 Sin3A PAH2 结合,Kd 为 ~29 nM。
CAS No. :880150-82-3
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中文名称
Mad1 (6-21)
英文名称
Mad1 (6-21)
英文别名
Mad1 (6-21);L-Arginine, L-arginyl-L-methionyl-L-asparaginyl-L-isoleucyl-L-glutaminyl-L-methionyl-L-leucyl-L-leucyl-L-α-glutamyl-L-alanyl-L-alanyl-L-α-aspartyl-L-tyrosyl-L-leucyl-L-α-glutamyl- (9CI)
Cas No.
880150-82-3
分子式
C84H140N24O26S2
分子量
1966.29
包装储存
Sealed storage, away from moisture and light, under nitrogenPowder -80°C 2 years;-20°C 1 ye
详情描述
Mad1 (6-21) 是 Mad1 蛋白的 6-21 片段。Mad1 (6-21) 与哺乳动物 Sin3A PAH2 结合,Kd 为 ~29 nM。
产品详情
Mad1 (6-21) 是 Mad1 蛋白的 6-21 片段。Mad1 (6-21) 与哺乳动物 Sin3A PAH2 结合,Kd 为 ~29 nM。
生物活性
Mad1 (6-21) is the 6-21 fragment of Mad1 protein. Mad1 (6-21) binds to mammalian Sin3A PAH2 with a K d of ~29 nM.
性状
Solid
体外研究(In Vitro)
The PAH2 domain of mSin3A adopts a left-handed, up-and-down, four-helix bundle structure with residues in all four helices as well as in the turn regions defining a compact structural domain with an extensive hydrophobic core. Helices α1 and α2 form a deep hydrophobic pocket, which constitutes the primary interaction surface for the Mad1 (6-21) peptide. The Mad1 (6-21) forms an amphipathic α helix in the complex and interacts with PAH2 mainly through the apolar surface of the helix. has not independently confirmed the accuracy of these methods. They are for reference only.
运输条件
Room temperature in continental US; may vary elsewhere.
储存方式
Sealed storage, away from moisture and light, under nitrogenPowder -80°C 2 years;-20°C 1 ye
SequenceShortening
RMNIQMLLEAADYLER
Solvent&Solubility
In Vitro:

H2O


Peptide Solubility and Storage Guidelines:1.  Calculate the length of the peptide.2.  Calculate the overall charge of the entire peptide according to the following table:
参考文献
[1]. K Brubaker, et al. Solution structure of the interacting domains of the Mad-Sin3 complex: implications for recruitment of a chromatin-modifying complex. Cell. 2000 Nov 10;103(4):655-65.
搜索质检报告(COA)
[1]. K Brubaker, et al. Solution structure of the interacting domains of the Mad-Sin3 complex: implications for recruitment of a chromatin-modifying complex. Cell. 2000 Nov 10;103(4):655-65.

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