重组人Proteasome 20S beta 6蛋白(ab116187)
Key features and details
- Expression system: Escherichia coli
- Purity: > 85% SDS-PAGE
- Tags: His tag N-Terminus
- Suitable for: SDS-PAGE, MS
描述
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产品名称
重组人Proteasome 20S beta 6蛋白 -
纯度
> 85 % SDS-PAGE.
ab116187 was purified using conventional chromatography techniques. -
表达系统
Escherichia coli -
Accession
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蛋白长度
Full length protein -
无动物成分
No -
性质
Recombinant -
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种属
Human -
序列
MGSSHHHHHHSSGLVPRGSHMTTIMAVQFDGGVVLGADSRTTTGSYIANR VTDKLTPIHDRIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTA ASLFKEMCYRYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGG SGSSYIYGYVDATYREGMTKEECLQFTANALALAMERDGSSGGVIRLAAI AESGVERQVLLGDQIPKFAVATLPPA -
预测分子量
24 kDa including tags -
氨基酸
35 to 239 -
标签
His tag N-Terminus
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相关产品
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Related Products
技术指标
Our Abpromise guarantee covers the use of ab116187 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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应用
SDS-PAGE
Mass Spectrometry
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质谱法
MALDI-TOF -
形式
Liquid -
Concentration information loading...
制备和贮存
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稳定性和存储
Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.
pH: 8.00
Constituents: 0.02% DTT, 0.32% Tris HCl, 10% Glycerol (glycerin, glycerine), 0.88% Sodium chloride
常规信息
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别名
- DELTA
- LMPY
- Macropain delta chain
see all -
功能
The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This unit is responsible of the peptidyl glutamyl-like activity. May catalyze basal processing of intracellular antigens. -
序列相似性
Belongs to the peptidase T1B family. -
细胞定位
Cytoplasm. Nucleus. - Information by UniProt
图片
实验方案
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
数据表及文件
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SDS download
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Datasheet download
文献 (0)
ab116187 尚未被引用在任何文献中。