重组大鼠Cathepsin K蛋白(His tag) (ab235712)
Key features and details
- Expression system: Escherichia coli
- Purity: > 90% SDS-PAGE
- Tags: His tag N-Terminus
- Suitable for: SDS-PAGE
描述
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产品名称
重组大鼠Cathepsin K蛋白(His tag)
参阅全部 Cathepsin K 蛋白酶 -
纯度
> 90 % SDS-PAGE. -
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
Rat -
序列
VPDSIDYRKKGYVTPVKNQGQCGSCWAFSSAGALEGQLKKKTGKLLALSP QNLVDCVSENYGCGGGYMTTAFQYVQQNGGIDSEDAYPYVGQDESCMYNA TAKAAKCRGYREIPVGNEKALKRAVARVGPVSVSIDASLTSFQFYSRGVY YDENCDRDNVNHAVLVVGYGTQKGNKYWIIKNSWGESWGNKGYVLLARNK NNACGITNLASFPKM -
预测分子量
28 kDa including tags -
氨基酸
115 to 329 -
标签
His tag N-Terminus -
额外的序列信息
N-terminal 6xHis-tagged. Full length mature chain without signal peptide and without propeptide.
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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 ab235712 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
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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 -20°C or -80°C. Avoid freeze / thaw cycle.
pH: 7.2
Constituents: Tris buffer, 50% Glycerol (glycerin, glycerine)
常规信息
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别名
- Cathepsin K
- Cathepsin O
- Cathepsin O1
see all -
功能
Closely involved in osteoclastic bone resorption and may participate partially in the disorder of bone remodeling. Displays potent endoprotease activity against fibrinogen at acid pH. May play an important role in extracellular matrix degradation. -
组织特异性
Predominantly expressed in osteclasts (bones). -
疾病相关
Defects in CTSK are the cause of pycnodysostosis (PKND) [MIM:265800]. PKND is an autosomal recessive osteochondrodysplasia characterized by osteosclerosis and short stature. -
序列相似性
Belongs to the peptidase C1 family. -
细胞定位
Lysosome. - 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)
ab235712 尚未被引用在任何文献中。