重组人AMD1蛋白(ab128442)
Key features and details
- Expression system: Escherichia coli
- Purity: > 80% 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AMD1蛋白 -
纯度
> 80 % SDS-PAGE.
ab128442 is purified using conventional chromatography techniques -
表达系统
Escherichia coli -
Accession
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蛋白长度
Protein fragment -
无动物成分
No -
性质
Recombinant -
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种属
Human -
序列
MGSSHHHHHH SSGLVPRGSH MGSHMSSMFV SKRRFILKTC GTTLLLKALV PLLKLARDYS GFDSIQSFFY SRKNFMKPSH QGYPHRNFQE EIEFLNAIFP NGAAYCMGRM NSDCWYLYTL DFPESRVISQ PDQTLEILMS ELDPAVMDQF YMKDGVTAKD VTRESGIRDL IPGSVIDATM FNPCGYSMNG MKSDGTYWTI HITPEPEFSY VSFETNLSQT SYDDLIRKVV EVFKPGKFVT TLFVNQSSKC RTVLASPQKI EGFKRLDCQS AMFNDYNFVF TSFAKKQQQQ QS -
预测分子量
33 kDa including tags -
氨基酸
68 to 334 -
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 ab128442 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, 20% Glycerol (glycerin, glycerine), 0.58% Sodium chloride
常规信息
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别名
- Adenosylmethionine decarboxylase 1
- AdoMetDC
- AMD1
see all -
通路
Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1. -
序列相似性
Belongs to the eukaryotic AdoMetDC family. -
翻译后修饰
Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain. - 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)
ab128442 尚未被引用在任何文献中。